Continued from EC 1.9 to EC 1.12
EC 1.13.11 With incorporation of two atoms of oxygen
EC 1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed function oxidases)
EC 1.13.99 Miscellaneous
Accepted name: catechol 1,2-dioxygenase
Reaction: catechol + O2 = cis,cis-muconate
For diagram click here.
Other name(s): catechol-oxygen 1,2-oxidoreductase; 1,2-pyrocatechase; catechase; catechol 1,2-oxygenase; catechol dioxygenase; pyrocatechase; pyrocatechol 1,2-dioxygenase; CD I; CD II
Systematic name: catechol:oxygen 1,2-oxidoreductase
Comments: Requires Fe3+. Involved in the metabolism of nitro-aromatic compounds by a strain of Pseudomonas putida.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9027-16-1
References:
1. Hayaishi, O. Direct oxygenation by O2, oxygenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 353-371.
2. Hayaishi, O., Katagiri, M. and Rothberg, S. Studies on oxygenases: pyrocatechase. J. Biol. Chem. 229 (1957) 905-920.
3. Sistrom, W.R. and Stanier, R.Y. The mechanism of formation of β-ketoadipic acid by bacteria. J. Biol. Chem. 210 (1954) 821-836.
4. Zeyer, J., Kocher, H.P. and Timmis, N.Influence of para-substituents on the oxidative metabolism of o-nitrophenols by Pseudomonas putida B2. Appl. Environ. Microbiol. 52 (1986) 334-339. [PMID: 3752997]
Accepted name: catechol 2,3-dioxygenase
Reaction: catechol + O2 = 2-hydroxymuconate-6-semialdehyde
For diagram of reaction click here.
Glossary: 2-hydroxymuconate-6-semialdehyde = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate
Other name(s): 2,3-pyrocatechase; catechol 2,3-oxygenase; catechol oxygenase; metapyrocatechase; pyrocatechol 2,3-dioxygenase; xylE (gene name)
Systematic name: catechol:oxygen 2,3-oxidoreductase (decyclizing)
Comments: Requires FeII. The enzyme initiates the meta-cleavage pathway of catechol degradation.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-46-3
References:
1. Hayaishi, O. Direct oxygenation by O2, oxygenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 8, Academic Press, New York, 1963, pp. 353-371.
2. Kojima, Y., Itada, N. and Hayaishi, O. Metapyrocatechase: a new catechol-cleaving enzyme. J. Biol. Chem. 236 (1961) 2223-2228. [PMID: 13757654]
3. Nozaki, M., Kagamiyama, H. and Hayaishi, O. Metapyrocatechase. I. Purification, crystallization and some properties. Biochem. Z. 338 (1963) 582-590. [PMID: 14087325]
4. Nakai, C., Hori, K., Kagamiyama, H., Nakazawa, T. and Nozaki, M. Purification, subunit structure, and partial amino acid sequence of metapyrocatechase. J. Biol. Chem. 258 (1983) 2916-2922. [PMID: 6826545]
5. Junker, F., Field, J.A., Bangerter, F., Ramsteiner, K., Kohler, H.-P., Joannou, C.L., Mason, J.R., Leisinger, T. and Cook, A.M. Oxygenation and spontaneous deamination of 2-aminobenzenesulphonic acid in Alcaligenes sp. strain O-1 with subsequent meta ring cleavage and spontaneous desulphonation to 2-hydroxymuconic acid. Biochem. J. 300 (1994) 429-436. [PMID: 8002948]
6. Junker, F., Leisinger, T. and Cook, A.M. 3-Sulphocatechol 2,3-dioxygenase and other dioxygenases (EC 1.13.11.2 and EC 1.14.12.-) in the degradative pathways of 2-aminobenzenesulphonic, benzenesulphonic and 4-toluenesulphonic acids in Alcaligenes sp. strain O-1. Microbiology 140 (1994) 1713-1722. [PMID: 8075807]
Accepted name: protocatechuate 3,4-dioxygenase
Reaction: 3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate
For diagram click here.
Glossary: 3,4-dihydroxybenzoate = protocatechuate
Other name(s): protocatechuate oxygenase; protocatechuic acid oxidase; protocatechuic 3,4-dioxygenase; protocatechuic 3,4-oxygenase
Systematic name: protocatechuate:oxygen 3,4-oxidoreductase (decyclizing)
Comments: Requires Fe3+. The enzyme, which participates in the degradation of aromatic compounds, catalyses the intradiol addition of both oxygen atoms from molecular oxygen, resulting in ortho-cleavage of the aromatic ring. The type of cleavage leads to mineralization via the intermediate 3-oxoadipate.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-47-4
References:
1. Fujisawa, H. and Hayaishi, O. Protocatechuate 3,4-dioxygenase. I. Crystallization and characterization. J. Biol. Chem. 243 (1968) 2673-2681. [PMID: 4967959]
2. Gross, S.R., Gafford, R.D. and Tatum, E.L. The metabolism of protocatechuic acid by Neurospora.J. Biol. Chem. 219 (1956) 781-796.
3. Stanier, R.Y. and Ingraham, J.L. Protocatechuic acid oxidase. J. Biol. Chem. 210 (1954) 799-820.
Accepted name: gentisate 1,2-dioxygenase
Reaction: 2,5-dihydroxybenzoate + O2 = maleylpyruvate
Other name(s): gentisate oxygenase; 2,5-dihydroxybenzoate dioxygenase; gentisate dioxygenase; gentisic acid oxidase
Systematic name: gentisate:oxygen 1,2-oxidoreductase (decyclizing)
Comments: Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-48-5
References:
1. Hayaishi, O. Direct oxygenation by O2, oxygenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 353-371.
2. Sugiyama, S., Yano, K., Komagata, K. and Arima, K. Metabolites of aromatic compounds by microbes. Part VII. Gentisic acid oxidase. Bull. Agric. Chem. Soc. Jpn 24 (1960) 243-248.
3. Sugiyama, S., Yano, K. and Arima, K. Metabolites of aromatic compounds by microbes. Part VII. Further studies of gentisic acid oxidase. Bull. Agric. Chem. Soc. Jpn 24 (1960) 249-254.
Accepted name: homogentisate 1,2-dioxygenase
Reaction: homogentisate + O2 = 4-maleylacetoacetate
For diagram of reaction click here.
Other name(s): homogentisicase; homogentisate oxygenase; homogentisate dioxygenase; homogentisate oxidase; homogentisic acid oxidase; homogentisic acid oxygenase; homogentisic oxygenase
Systematic name: homogentisate:oxygen 1,2-oxidoreductase (decyclizing)
Comments: Requires Fe2+.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-49-6
References:
1. Adachi, K., Iwayama, Y., Tanioka, H. and Takeda, Y. Purification and properties of homogentisate oxygenase from Pseudomonas fluorescens. Biochim. Biophys. Acta 118 (1966) 88-97. [PMID: 5954067]
2. Crandall, D.I. and Halikis, D.N. Homogentisic acid oxidase. I. Distribution in animal tissues and relation to tyrosine metabolism in rat kidney. J. Biol. Chem. 208 (1954) 629-638.
3. Hayaishi, O. Direct oxygenation by O2, oxygenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 353-371.
4. Kita, H., Kamimoto, M., Senoh, S., Adachi, T. and Takeda, Y. Cystallization and some properties of 3,4-dihydroxyphenylacetate-2,3-oxygenase. Biochem. Biophys. Res. Commun. 18 (1965) 66-70.
5. Knox, W.E. and Edwards, S.W. Homogentisate oxidase of liver. J. Biol. Chem. 216 (1955) 479-487.
6. Ravdin, R.G. and Crandall, D.I. The enzymatic conversion of homogentisic acid to 4-fumarylacetoacetic acid. J. Biol. Chem. 189 (1951) 137-149.
Accepted name: 3-hydroxyanthranilate 3,4-dioxygenase
Reaction: 3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde
For diagram of reaction click here.
Other name(s): 3-hydroxyanthranilate oxygenase; 3-hydroxyanthranilic acid oxygenase; 3-hydroxyanthranilic oxygenase; 3-hydroxyanthranilic acid oxidase; 3HAO
Systematic name: 3-hydroxyanthranilate:oxygen 3,4-oxidoreductase (decyclizing)
Comments: Requires Fe2+.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-50-9
References:
1. Decker, R.H., Kang, H.H., Leach, F.R. and Henderson, L.M. Purification and properties of 3-hydroxyanthranilic acid oxidase. J. Biol. Chem. 236 (1961) 3076-3082.
2. Hayaishi, O. Direct oxygenation by O2, oxygenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 353-371.
[EC 1.13.11.7 Deleted entry: 3,4-dihydroxyphenylacetate 3,4-dioxygenase (EC 1.13.11.7 created 1965 as EC 1.13.1.7, transferred 1972 to EC 1.13.11.7, deleted 1980)]
Accepted name: protocatechuate 4,5-dioxygenase
Reaction: 3,4-dihydroxybenzoate + O2 = 4-carboxy-2-hydroxymuconate semialdehyde
For diagram of reaction click here
Other name(s): protocatechuate 4,5-oxygenase; protocatechuic 4,5-dioxygenase; protocatechuic 4,5-oxygenase; protocatechuate:oxygen 4,5-oxidoreductase (ring-opening); protocatechuate:oxygen 4,5-oxidoreductase (decyclizing)
Systematic name: 3,4-dihydroxybenzoate:oxygen 4,5-oxidoreductase (ring-opening)
Comments: Requires Fe2+.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-56-5
References:
1. Trippett, S., Dagley, S. and Stopher, D.A. The bacterial oxidation of nicotinic acid Biochem. J. 76 (1960) 9P.
Accepted name: 2,5-dihydroxypyridine 5,6-dioxygenase
Reaction: 2,5-dihydroxypyridine + O2 = N-formylmaleamic acid
Other name(s): 2,5-dihydroxypyridine oxygenase; pyridine-2,5-diol dioxygenase; NicX
Systematic name: 2,5-dihydroxypyridine:oxygen 5,6-oxidoreductase
Comments: Requires Fe2+.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-57-6
References:
1. Behrman, E.J. and Stanier, R.Y. The bacterial oxidation of nicotinic acid. J. Biol. Chem. 228 (1957) 923-945. [PMID: 13475371]
2. Gauthier, J.J. and Rittenberg, S.C. The metabolism of nicotinic acid. I. Purification and properties of 2,5-dihydroxypyridine oxygenase from Pseudomonas putida N-9. J. Biol. Chem. 246 (1971) 3737-3742. [PMID: 5578917]
3. Gauthier, J.J. and Rittenberg, S.C. The metabolism of nicotinic acid. II. 2,5-Dihydroxypyridine oxidation, product formation, and oxygen 18 incorporation. J. Biol. Chem. 246 (1971) 3743-3748. [PMID: 5578918]
4. Jimenez, J.I., Canales, A., Jimenez-Barbero, J., Ginalski, K., Rychlewski, L., Garcia, J.L. and Diaz, E. Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440. Proc. Natl. Acad. Sci. USA 105 (2008) 11329-11334. [PMID: 18678916]
Accepted name: 7,8-dihydroxykynurenate 8,8a-dioxygenase
Reaction: 7,8-dihydroxykynurenate + O2 = 5-(3-carboxy-3-oxopropenyl)-4,6-dihydroxypyridine-2-carboxylate
Other name(s): 7,8-dihydroxykynurenate oxygenase; 7,8-dihydroxykynurenate 8,8α-dioxygenase; 7,8-dihydroxykynurenate:oxygen 8,8a-oxidoreductase (decyclizing)
Systematic name: 7,8-dihydroxykynurenate:oxygen 8,8a-oxidoreductase (ring-opening)
Comments: Requires Fe2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9029-58-7
References:
1. Kuno, S., Tashiro, M., Taniuchi, H., Horibata, K., Hayaishi, O., Seno, S., Tokuyama, T. and Sakan, T. Enzymatic degradation of kynurenic acid. Fed. Proc. 20 (1961) 3.
Accepted name: tryptophan 2,3-dioxygenase
Reaction: L-tryptophan + O2 = N-formyl-L-kynurenine
For diagram, click here
Other name(s): tryptophan pyrrolase (ambiguous); tryptophanase; tryptophan oxygenase; tryptamine 2,3-dioxygenase; tryptophan peroxidase; indoleamine 2,3-dioxygenase (ambiguous); indolamine 2,3-dioxygenase (ambiguous); L-tryptophan pyrrolase; TDO; L-tryptophan 2,3-dioxygenase; L-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: L-tryptophan:oxygen 2,3-oxidoreductase (ring-opening)
Comments: A protohemoprotein. In mammals, the enzyme appears to be located only in the liver. This enzyme, together with EC 1.13.11.52, indoleamine 2,3-dioxygenase, catalyses the first and rate-limiting step in the kynurenine pathway, the major pathway of tryptophan metabolism [5]. The enzyme is specific for tryptophan as substrate, but is far more active with L-tryptophan than with D-tryptophan [2].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9014-51-1
References:
1. Uchida, K., Shimizu, T., Makino, R., Sakaguchi, K., Iizuka, T., Ishimura, Y., Nozawa, T. and Hatano, M. Magnetic and natural circular dichroism of L-tryptophan 2,3-dioxygenases and indoleamine 2,3-dioxygenase. I. Spectra of ferric and ferrous high spin forms. J. Biol. Chem. 258 (1983) 2519-2525. [PMID: 6600455]
2. Ren, S., Liu, H., Licad, E. and Correia, M.A. Expression of rat liver tryptophan 2,3-dioxygenase in Escherichia coli: structural and functional characterization of the purified enzyme. Arch. Biochem. Biophys. 333 (1996) 96-102. [PMID: 8806758]
3. Leeds, J.M., Brown, P.J., McGeehan, G.M., Brown, F.K. and Wiseman, J.S. Isotope effects and alternative substrate reactivities for tryptophan 2,3-dioxygenase. J. Biol. Chem. 268 (1993) 17781-17786. [PMID: 8349662]
4. Dang, Y., Dale, W.E. and Brown, O.R. Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway. Free Radic. Biol. Med. 28 (2000) 615-624. [PMID: 10719243]
5. Littlejohn, T.K., Takikawa, O., Truscott, R.J. and Walker, M.J. Asp274 and His346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase. J. Biol. Chem. 278 (2003) 29525-29531. [PMID: 12766158]
Accepted name: linoleate 13S-lipoxygenase
Reaction: (1) linoleate + O2 = (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate
(2) α-linolenate + O2 = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
Glossary: linoleate = (9Z,12Z)-octadeca-9,12-dienoate
α-linolenate = (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
Other name(s): 13-lipoxidase; carotene oxidase; 13-lipoperoxidase; fat oxidase; 13-lipoxydase; lionoleate:O2 13-oxidoreductase
Systematic name: linoleate:oxygen 13-oxidoreductase
Comments: Contains nonheme iron. A common plant lipoxygenase that oxidizes linoleate and α-linolenate, the two most common polyunsaturated fatty acids in plants, by inserting molecular oxygen at the C-13 position with (S)-configuration. This enzyme produces precursors for several important compounds, including the plant hormone jasmonic acid. EC 1.13.11.58, linoleate 9S-lipoxygenase, catalyses a similar reaction at the second available position of these fatty acids.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-60-1
References:
1. Christopher, J., Pistorius, E. and Axelrod, B. Isolation of an enzyme of soybean lipoxidase. Biochim. Biophys. Acta 198 (1970) 12-19. [PMID: 5461103]
2. Theorell, H., Holman, R.T. and Åkesson, Å. Crystalline lipoxidase. Acta Chem. Scand. 1 (1947) 571-576. [PMID: 18907700]
3. Zimmerman, D.C. Specificity of flaxseed lipoxidase. Lipids 5 (1970) 392-397. [PMID: 5447012]
4. Royo, J., Vancanneyt, G., Perez, A.G., Sanz, C., Stormann, K., Rosahl, S. and Sanchez-Serrano, J.J. Characterization of three potato lipoxygenases with distinct enzymatic activities and different organ-specific and wound-regulated expression patterns. J. Biol. Chem. 271 (1996) 21012-21019. [PMID: 8702864]
5. Bachmann, A., Hause, B., Maucher, H., Garbe, E., Voros, K., Weichert, H., Wasternack, C. and Feussner, I. Jasmonate-induced lipid peroxidation in barley leaves initiated by distinct 13-LOX forms of chloroplasts. Biol. Chem. 383 (2002) 1645-1657. [PMID: 12452441]
[EC 1.13.11.13 Deleted entry: ascorbate 2,3-dioxygenase. The activity is the sum of several enzymatic and spontaneous reactions (EC 1.13.11.13 created 1972, deleted 2012)]
Accepted name: 2,3-dihydroxybenzoate 3,4-dioxygenase
Reaction: 2,3-dihydroxybenzoate + O2 = 3-carboxy-2-hydroxymuconate semialdehyde
Other name(s): o-pyrocatechuate oxygenase; 2,3-dihydroxybenzoate 1,2-dioxygenase; 2,3-dihydroxybenzoic oxygenase; 2,3-dihydroxybenzoate oxygenase; 2,3-dihydroxybenzoate:oxygen 3,4-oxidoreductase (decyclizing)
Systematic name: 2,3-dihydroxybenzoate:oxygen 3,4-oxidoreductase (ring-opening)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9032-31-9
References:
1. Ribbons, D.W. Bacterial oxidation of 2,3-dihydroxybenzoic acid - a new oxygenase. Biochem. J. 99 (1966) 30P-31P.
Accepted name: 3,4-dihydroxyphenylacetate 2,3-dioxygenase
Reaction: 3,4-dihydroxyphenylacetate + O2 = 2-hydroxy-5-carboxymethylmuconate semialdehyde
Other name(s): 3,4-dihydroxyphenylacetic acid 2,3-dioxygenase; HPC dioxygenase; homoprotocatechuate 2,3-dioxygenase;3,4-dihydroxyphenylacetate:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: 3,4-dihydroxyphenylacetate:oxygen 2,3-oxidoreductase (ring-opening)
Comments: An iron protein.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37256-56-7
References:
1. Adachi, K., Takeda, Y., Senoh, S. and Kita, H. Metabolism of p-hydroxyphenylacetic acid in Pseudomonas ovalis. Biochim. Biophys. Acta 93 (1964) 483-493.
2. Barbour, M.G. and Bayly, R.C. Control of meta-cleavage degradation of 4-hydroxyphenylacetate in Pseudomonas putida. J. Bacteriol. 147 (1981) 844-850. [PMID: 5891457]
3. Krishnan Kutty, R., Devi, N.A., Veeraswamy, M., Ramesh, S. and Subba Rao, P.V. Degradation of (+/-)-synephrine by Arthrobacter synephrinum. Oxidation of 3,4-dihydroxyphenylacetate to 2-hydroxy-5-carboxymethyl-muconate semialdehyde. Biochem. J. 167 (1977) 163-170. [PMID: 588248]
Accepted name: 3-carboxyethylcatechol 2,3-dioxygenase
Reaction: (1) 3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate
(2) (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 = (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate
For diagram of reaction click here or click here.
Glossary: (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate = trans-2,3-dihydroxycinnamate
Other name(s): 2,3-dihydroxy-β-phenylpropionic dioxygenase; 2,3-dihydroxy-β-phenylpropionate oxygenase; 3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase; 3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase (decyclizing)
Systematic name: 3-(2,3-dihydroxyphenyl)propanoate:oxygen 1,2-oxidoreductase (ring-opening)
Comments: An iron protein. This enzyme catalyses a step in the pathway of phenylpropanoid compounds degradation.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 105503-63-7
References:
1. Dagley, S., Chapman, P.J. and Gibson, D.T. The metabolism of β-phenylpropionic acid by an Achromobacter. Biochem. J. 97 (1965) 643-650. [PMID: 5881653]
2. Lam, W. W. Y and Bugg, T. D. H. Chemistry of extradiol aromatic ring cleavage: isolation of a stable dienol ring fission intermediate and stereochemistry of its enzymatic hydrolytic clevage. J. Chem. Soc., Chem. Commun. 10 (1994) 1163-1164.
3. Díaz, E., Ferrández, A. and García, J.L. Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12. J. Bacteriol. 180 (1998) 2915-2923. [PMID: 9603882]
Accepted name: indole 2,3-dioxygenase
Reaction: indole + O2 = 2-formylaminobenzaldehyde
Other name(s): indole oxidase; indoleamine 2,3-dioxygenase (ambiguous); indole:O2 oxidoreductase ; indole-oxygen 2,3-oxidoreductase (decyclizing); IDO (ambiguous); indole:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: indole:oxygen 2,3-oxidoreductase (ring-opening)
Comments: Enzymes from the plants Tecoma stans, Jasminum grandiflorum and Zea mays are flavoproteins containing copper. They are part of enzyme systems that form either anthranil (2,1-benzoisoxazole) (Tecoma stans), anthranilate (Jasminum grandiflorum) or both (Zea mays) as the final product. A second enzyme from Tecoma stans is not a flavoprotein, does not require copper, and is part of a system that forms anthranilate as the final product.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-57-8
References:
1. Divakar, N.G., Subramanian, V., Sugumaran, M. and Vaidyanathan, C.S. Indole oxygenase from the leaves of Jasminum grandiflorum. Plant Sci. Lett. 15 (1979) 177-181.
2. Chauhan, Y.S., Rathore, V.S., Garg, G.K. and Bhargava, A. Detection of an indole oxidizing system in maize leaves. Biochem. Biophys. Res. Commun. 83 (1978) 1237-1245. [PMID: 697856]
3. Nair, P.M. and Vaidyanathan, C.S. An indole oxidase isolated from the leaves of Tecoma stans. Biochim. Biophys. Acta 81 (1964) 496-506.
4. Kunapuli, S.P. and Vaidyanathan, C.S. Purification and characterization of a new indole oxygenase from the leaves of Tecoma stans L. Plant Physiol. 71 (1983) 19-23. [PMID: 16662784]
Accepted name: persulfide dioxygenase
Reaction: S-sulfanylglutathione + O2 + H2O = glutathione + sulfite + 2 H+ (overall reaction)
(1a) S-sulfanylglutathione + O2 = S-sulfinatoglutathione + H+
(1b) S-sulfinatoglutathione + H2O = glutathione + sulfite + H+ (spontaneous)
Other name(s): sulfur oxygenase (incorrect); sulfur:oxygen oxidoreductase (incorrect); sulfur dioxygenase (incorrect)
Systematic name: S-sulfanylglutathione:oxygen oxidoreductase
Comments: An iron protein. Perthiols, formed spontaneously by interactions between thiols and elemental sulfur or sulfide, are the only acceptable substrate to the enzyme. The sulfite that is formed by the enzyme can be further converted into sulfate, thiosulfate or S-sulfoglutathione (GSSO3-) non-enzymically [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-58-9
References:
1. Suzuki, I. and Silver, M. The initial product and properties of the sulfur-oxidizing enzyme of thiobacilli. Biochim. Biophys. Acta 122 (1966) 22-33. [PMID: 5968172]
2. Rohwerder, T. and Sand, W. The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp. Microbiology 149 (2003) 1699-1710. [PMID: 12855721]
3. Liu, H., Xin, Y. and Xun, L. Distribution, diversity, and activities of sulfur dioxygenases in heterotrophic bacteria. Appl. Environ. Microbiol. 80 (2014) 1799-1806. [PMID: 24389926]
4. Holdorf, M.M., Owen, H.A., Lieber, S.R., Yuan, L., Adams, N., Dabney-Smith, C. and Makaroff, C.A. Arabidopsis ETHE1 encodes a sulfur dioxygenase that is essential for embryo and endosperm development. Plant Physiol. 160 (2012) 226-236. [PMID: 22786886]
5. Pettinati, I., Brem, J., McDonough, M.A. and Schofield, C.J. Crystal structure of human persulfide dioxygenase: structural basis of ethylmalonic encephalopathy. Hum. Mol. Genet. 24 (2015) 2458-2469. [PMID: 25596185]
Accepted name: cysteamine dioxygenase
Reaction: 2-aminoethanethiol + O2 = hypotaurine
For diagram, click here
Other name(s): persulfurase; cysteamine oxygenase; cysteamine:oxygen oxidoreductase
Systematic name: 2-aminoethanethiol:oxygen oxidoreductase
Comments: A non-heme iron protein that is involved in the biosynthesis of taurine. Requires catalytic amounts of a cofactor-like compound, such as sulfur, sufide, selenium or methylene blue for maximal activity. 3-Aminopropanethiol (homocysteamine) and 2-sulfanylethan-1-ol (2-mercaptoethanol) can also act as substrates, but glutathione, cysteine, and cysteine ethyl- and methyl esters are not good substrates [1,3].
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9033-41-4
References:
1. Cavallini, D., de Marco, C., Scandurra, R., Duprè, S. and Graziani, M.T. The enzymatic oxidation of cysteamine to hypotaurine. Purification and properties of the enzyme. J. Biol. Chem. 241 (1966) 3189-3196. [PMID: 5912113]
2. Wood, J.L. and Cavallini, D. Enzymic oxidation of cysteamine to hypotaurine in the absence of a cofactor. Arch. Biochem. Biophys. 119 (1967) 368-372. [PMID: 6052430]
3. Cavallini, D., Federici, G., Ricci, G., Duprè, S. and Antonucci, A. The specificity of cysteamine oxygenase. FEBS Lett. 56 (1975) 348-351. [PMID: 1157952]
4. Richerson, R.B. and Ziegler, D.M. Cysteamine dioxygenase. Methods Enzymol. 143 (1987) 410-415. [PMID: 3657558]
Accepted name: cysteine dioxygenase
Reaction: L-cysteine + O2 = 3-sulfinoalanine
For diagram click here.
Other name(s): cysteine oxidase
Systematic name: L-cysteine:oxygen oxidoreductase
Comments: Requires Fe2+ and NAD(P)H.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37256-59-0
References:
1. Lombardini, J.B., Singer, T.P. and Boyer, P.D. Cystein oxygenase. II. Studies on the mechanism of the reaction with 18oxygen. J. Biol. Chem. 244 (1969) 1172-1175. [PMID: 5767301]
[EC 1.13.11.21 Transferred entry: now EC 1.14.99.36, β-carotene 15,15'-monooxygenase (EC 1.13.11.21 created 1972, deleted 2001)]
Accepted name: caffeate 3,4-dioxygenase
Reaction: 3,4-dihydroxy-trans-cinnamate + O2 = 3-(2-carboxyethenyl)-cis,cis-muconate
Other name(s): 3,4-dihydroxy-trans-cinnamate:oxygen 3,4-oxidoreductase (decyclizing)
Systematic name: 3,4-dihydroxy-trans-cinnamate:oxygen 3,4-oxidoreductase (ring-opening)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-61-4
References:
1. Seidman, M.M., Toms, A. and Wood, J.M. Influence of side-chain substituents on the position of cleavage of the benzene ring by Pseudomonas fluorescens. J. Bacteriol. 97 (1969) 1192-1197. [PMID: 5776526]
Accepted name: 2,3-dihydroxyindole 2,3-dioxygenase
Reaction: 2,3-dihydroxyindole + O2 = anthranilate + CO2
Other name(s): 2,3-dihydroxyindole:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: 2,3-dihydroxyindole:oxygen 2,3-oxidoreductase (ring-opening)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-62-5
References:
1. Fujioka, M. and Wada, H. The bacterial oxidation of indole. Biochim. Biophys. Acta 158 (1968) 70-78. [PMID: 5652436]
Accepted name: quercetin 2,3-dioxygenase
Reaction: quercetin + O2 = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO + H+
For diagram of reaction click here
Other name(s): quercetinase; flavonol 2,4-oxygenase; quercetin:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: quercetin:oxygen 2,3-oxidoreductase (ring-opening)
Comments: The enzyme from Aspergillus sp. is a copper protein whereas that from Bacillus subtilis contains iron. Quercetin is a flavonol (5,7,3',4'-tetrahydroxyflavonol).
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9075-67-6
References:
1. Oka, T. and Simpson, F.J. Quercetinase, a dioxygenase containing copper. Biochem. Biophys. Res. Commun. 43 (1971) 1-5. [PMID: 5579942]
2. Steiner, R.A., Kalk, K.H. and Dijkstra, B.W. Anaerobic enzyme·substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase. Proc. Natl. Acad. Sci. USA 99 (2002) 16625-16630. [PMID: 12486225]
3. Bowater, L., Fairhurst, S.A., Just, V.J., and Bornemann, S. Bacillus subtilis YxaG is a novel Fe-containing quercetin 2,3-dioxygenase. FEBS Lett. 557 (2004) 45-48. [PMID: 14741339]
Accepted name: 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase
Reaction: 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + O2 = 3-hydroxy-5,9,17-trioxo-4,5:9,10-disecoandrosta-1(10),2-dien-4-oate
Other name(s): steroid 4,5-dioxygenase; 3-alkylcatechol 2,3-dioxygenase; 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione:oxygen 4,5-oxidoreductase (decyclizing)
Systematic name: 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione:oxygen 4,5-oxidoreductase (ring-opening)
Comments: Requires Fe2+. Also acts on 3-isopropylcatechol and 3-tert-butyl-5-methylcatechol.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 37256-63-6
References:
1. Gibson, D.T., Wang, K.C., Sih, C.J. and Whitlock, J.H. Mechanisms of steroid oxidation by microorganisms. IX. On the mechanism of ring A cleavage in the degradation of 9,10-seco steroids by microorganisms. J. Biol. Chem. 241 (1966) 551-559. [PMID: 5908121]
Accepted name: peptide-tryptophan 2,3-dioxygenase
Reaction: [protein]-L-tryptophan + O2 = [protein]-N-formyl-L-kynurenine
Glossary: N-formyl-L-kynurenine = (2S)-2-amino-4-[2-(formamido)phenyl]-4-oxobutanoic acid
Other name(s): pyrrolooxygenase; peptidyltryptophan 2,3-dioxygenase; tryptophan pyrrolooxygenase; [protein]-L-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: [protein]-L-tryptophan:oxygen 2,3-oxidoreductase (ring-opening)
Comments: Also acts on tryptophan.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 37256-64-7
References:
1. Frydman, R.B., Tomaro, M.L. and Frydman, B. Pyrrolooxygenase: its action on tryptophan-containing enzymes and peptides. Biochim. Biophys. Acta 284 (1972) 80-89. [PMID: 4403729]
2. Camoretti-Mercado, B. and Frydman, R.B. Separation of tryptophan pyrrolooxygenase into three molecular forms. A study of their substrate specificities using tryptophyl-containing peptides and proteins. Eur. J. Biochem. 156 (1986) 317-325. [PMID: 3699018]
Accepted name: 4-hydroxyphenylpyruvate dioxygenase
Reaction: 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2
For diagram of reaction click here or click here.
Other name(s): p-hydroxyphenylpyruvic hydroxylase; p-hydroxyphenylpyruvate hydroxylase; p-hydroxyphenylpyruvate oxidase; p-hydroxyphenylpyruvic oxidase; p-hydroxyphenylpyruvate dioxygenase; p-hydroxyphenylpyruvic acid hydroxylase; 4-hydroxyphenylpyruvic acid dioxygenase
Systematic name: 4-hydroxyphenylpyruvate:oxygen oxidoreductase (hydroxylating, decarboxylating)
Comments: The Pseudomonas enzyme contains one Fe3+ per mole of enzyme; the enzymes from other sources may contain essential iron or copper. Formerly EC 1.14.2.2 and EC 1.99.1.14.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9029-72-5
References:
1. Lindstedt, S. and Rundgren, M. Blue color, metal content, and substrate binding in 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874. J. Biol. Chem. 257 (1982) 11922-11931. [PMID: 7118918]
2. Roche, P.A., Moorehead, T.J. and Hamilton, G.A. Purification and properties of hog liver 4-hydroxyphenylpyruvate dioxygenase. Arch. Biochem. Biophys. 216 (1982) 62-73. [PMID: 7103516]
Accepted name: 2,3-dihydroxybenzoate 2,3-dioxygenase
Reaction: 2,3-dihydroxybenzoate + O2 = 2-carboxy-cis,cis-muconate
Other name(s): 2,3-dihydroxybenzoate 2,3-oxygenase; 2,3-dihydroxybenzoate:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: 2,3-dihydroxybenzoate:oxygen 2,3-oxidoreductase (ring-opening)
Comments: Also acts, more slowly, with 2,3-dihydroxy-4-methylbenzoate and 2,3-dihydroxy-4-isopropylbenzoate.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 56802-97-2
References:
1. La Du, B.N. and Zannoni, V.G. The tyrosine oxidation system of liver. III. Further studies on the oxidation of p-hydroxyphenylpyruvic acid. J. Biol. Chem. 219 (1956) 273-281.
2. Sharma, H.K. and Vaidyanathan, C.S. A new mode of ring cleavage of 2,3-dihydroxybenzoic acid in Tecoma stans (L.). Partial purification and properties of 2,3-dihydroxybenzoate 2,3-oxygenase. Eur. J. Biochem. 56 (1975) 163-171. [PMID: 1175620]
Accepted name: stizolobate synthase
Reaction: L-dopa + O2 = 4-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde
Systematic name: 3,4-dihydroxy-L-phenylalanine:oxygen 4,5-oxidoreductase (recyclizing)
Glossary: L-dopa = 3,4-dihydroxy-L-phenylalanine
Comments: The intermediate product undergoes ring closure and oxidation, with NAD(P)+ as acceptor, to stizolobic acid. The enzyme requires Zn2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 65979-39-7
References:
1. Saito, K. and Komamine, A. Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. An enzyme system(s) catalyzing the conversion of dihydroxyphenylalanine into stizolobinic acid and stizolobic acid from etiolated seedlings of Stizolobium hassjoo. Eur. J. Biochem. 68 (1976) 237-243. [PMID: 9285]
2. Saito, K. and Komamine, A. Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. Eur. J. Biochem. 82 (1978) 385-392. [PMID: 624278]
Accepted name: stizolobinate synthase
Reaction: L-dopa + O2 = 5-(L-alanin-3-yl)-2-hydroxy-cis,cis-muconate 6-semialdehyde
Glossary: L-dopa = 3,4-dihydroxy-L-phenylalanine
Systematic name: 3,4-dihydroxy-L-phenylalanine:oxygen 2,3-oxidoreductase (recyclizing)
Comments: The intermediate product undergoes ring closure and oxidation, with NAD(P)+ as acceptor, to stizolobinic acid. The enzyme requires Zn2+.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 65979-38-6
References:
1. Saito, K. and Komamine, A. Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. An enzyme system(s) catalyzing the conversion of dihydroxyphenylalanine into stizolobinic acid and stizolobic acid from etiolated seedlings of Stizolobium hassjoo. Eur. J. Biochem. 68 (1976) 237-243. [PMID: 9285]
2. Saito, K. and Komamine, A. Biosynthesis of stizolobinic acid and stizolobic acid in higher plants. Eur. J. Biochem. 82 (1978) 385-392. [PMID: 624278]
Accepted name: arachidonate 12-lipoxygenase
Reaction: arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
Other name(s): δ12-lipoxygenase; 12-lipoxygenase; 12δ-lipoxygenase; C-12 lipoxygenase; 12S-lipoxygenase; leukotriene A4 synthase; LTA4 synthase
Systematic name: arachidonate:oxygen 12-oxidoreductase
Comments: The product is rapidly reduced to the corresponding 12S-hydroxy compound.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 82391-43-3
References:
1. Hamberg, M. and Samuelsson, B. Prostaglandin endoperoxides. Novel transformations of arachidonic acid in human platelets. Proc. Natl. Acad. Sci. USA 71 (1974) 3400-3404. [PMID: 4215079]
2. Nugteren, D.H. Arachidonate lipoxygenase in blood platelets. Biochim. Biophys. Acta 380 (1975) 299-307. [PMID: 804329]
3. Wallach, D.P. and Brown, V.R. A novel preparation of human platelet lipoxygenase. Characteristics and inhibition by a variety of phenyl hydrazones and comparisons with other lipoxygenases. Biochim. Biophys. Acta 663 (1981) 361-372. [PMID: 6783111]
[EC 1.13.11.32 Transferred entry: 2-nitropropane dioxygenase. Now EC 1.13.12.16, nitronate monooxygenase. (EC 1.13.11.32 created 1984, modified 2006, deleted 2009)]
Accepted name: arachidonate 15-lipoxygenase
Reaction: arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
Other name(s): 15-lipoxygenase; linoleic acid ω6-lipoxygenase; ω6 lipoxygenase
Systematic name: arachidonate:oxygen 15-oxidoreductase
Comments: The product is rapidly reduced to the corresponding 15S-hydroxy compound.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 82249-77-2
References:
1. Bryant, R.W., Bailey, J.M., Schewqe, T. and Rapoport, S.M. Positional specificity of a reticulocyte lipoxygenase. Conversion of arachidonic acid to 15-S-hydroperoxy-eicosatetraenoic acid. J. Biol. Chem. 257 (1982) 6050-6055. [PMID: 6804460]
2. Narumiya, S. and Salmon, J.A. Arachidonic acid-15-lipoxygenase from rabbit peritoneal polymorphonuclear leukocytes. Methods Enzymol. 86 (1982) 45-48. [PMID: 6813644]
3. Oliw, E.H. and Sprecher, H. Metabolism of polyunsaturated fatty acids by an (n-6)-lipoxygenase associated with human ejaculates. Biochim. Biophys. Acta 1002 (1989) 283-291. [PMID: 2496760]
4. Shibata, D., Steczko, J., Dixon, F.E., Hermodson, M., Yasdanparast, R. and Axelrod, B. Primary structure of soybean lipoxygenase-1. J. Biol. Chem. 262 (1987) 10080-10085. [PMID: 3112136]
Accepted name: arachidonate 5-lipoxygenase
Reaction: arachidonate + O2 = (5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O (overall reaction)
(1a) arachidonate + O2 = (5S,6E,8Z,11Z,14Z)-5-hydroperoxyicosa-6,8,11,14-tetraenoate
(1b) (5S,6E,8Z,11Z,14Z)-5-hydroperoxyicosa-6,8,11,14-tetraenoate = (5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate + H2O
For diagram of reaction click here
Glossary: leukotriene A4 = (5S,6S,7E,9E,11Z,14Z)-5,6-epoxyicosa-7,9,11,14-tetraenoate
Other name(s): leukotriene-A4 synthase; δ5-lipoxygenase; 5δ-lipoxygenase; arachidonic 5-lipoxygenase; arachidonic acid 5-lipoxygenase; C-5-lipoxygenase; LTA synthase; leukotriene A4 synthase
Systematic name: arachidonate:oxygen 5-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 80619-02-9
References:
1. Matsumoto, T., Funk, C.D., Radmark, O., Hoog, J.-O., Jornvall, H. and Samuelsson, B. Molecular cloning and amino acid sequence of human 5-lipoxygenase. Proc. Natl. Acad. Sci. USA 85 (1988) 26-30. [PMID: 2829172]
2. Ohishi, N., Izumi, T., Minami, M., Kitamura, S., Seyama, Y., Ohkawa, S., Terao, S., Yotsumoto, H., Takaku, F. and Shimizu, T. Leukotriene A4 hydrolase in the human lung. Inactivation of the enzyme with leukotriene A4 isomers. J. Biol. Chem. 262 (1987) 10200-10205. [PMID: 3038871]
3. Shimizu, T., Izumi, T., Seyama, Y., Tadokoro, K., Rädmark, O. and Samuelsson, B. Characterization of leukotriene A4 synthase from murine mast cells: evidence for its identity to arachidonate 5-lipoxygenase. Proc. Natl. Acad. Sci. USA 83 (1986) 4175-4179. [PMID: 3012557]
4. Shimizu, T., Rädmark, O. and Samuelssohn, B. Enzyme with dual lipoxygenase activities catalyzes leukotriene A4 synthesis from arachidonic acid. Proc. Natl. Acad. Sci. USA 81 (1984) 689-693. [PMID: 6322165]
Accepted name: pyrogallol 1,2-oxygenase
Reaction: 1,2,3-trihydroxybenzene + O2 = (2Z,4E)-2-hydroxyhexa-2,4-dienedioate
Glossary: (2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (2Z,4E)-2-hydroxymuconate
1,2,3-trihydroxybenzene = pyrogallol
Other name(s): pyrogallol 1,2-dioxygenase; 1,2,3-trihydroxybenzene:oxygen 1,2-oxidoreductase (decyclizing)
Systematic name: 1,2,3-trihydroxybenzene:oxygen 1,2-oxidoreductase (ring-opening)
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 78310-68-6
References:
1. Groseclose, E.E. and Ribbons, D.W. Metabolism of resorcinylic compounds by bacteria: new pathway for resorcinol catabolism in Azotobacter vinelandii. J. Bacteriol. 146 (1981) 460-466. [PMID: 7217008]
Accepted name: chloridazon-catechol dioxygenase
Reaction: 5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O2 = 5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone
Other name(s): 5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone 1,2-oxidoreductase (decyclizing)
Systematic name: 5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone 1,2-oxidoreductase (ring-opening)
Comments: An iron protein, requiring additional Fe2+. Not identical with EC 1.13.11.1 (catechol 1,2-dioxygenase), EC 1.13.11.2 (catechol 2,3-dioxygenase) or EC 1.13.11.5 (homogentisate 1,2-dioxygenase). Involved in the breakdown of the herbicide chloridazon.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 82869-32-7
References:
1. Müller, R, Haug, S., Eberspächer, J. and Lingens, F. Catechol-2,3-Dioxygenase aus Pyrazon-abbauenden Bakterien. Hoppe-Seyler's Z. Physiol. Chem. 358 (1977) 797-805. [PMID: 19349]
2. Müller, R., Schmitt, S. and Lingens, F. A novel non-heme iron-containing dioxygenase. Chloridazon-catechol dioxygenase from Phenylobacterium immobilis DSM 1986. Eur. J. Biochem. 125 (1982) 579-584. [PMID: 6811270]
Accepted name: hydroxyquinol 1,2-dioxygenase
Reaction: hydroxyquinol + O2 = maleylacetate
For diagram of reaction click here.
Glossary: hydroxyquinol = 1,2,4-trihydroxybenzene
maleylacetate = (2Z)-4-oxohex-2-enedioate
Other name(s): hydroxyquinol dioxygenase; benzene-1,2,4-triol:oxygen 1,2-oxidoreductase (decyclizing)
Systematic name: benzene-1,2,4-triol:oxygen 1,2-oxidoreductase (ring-opening)
Comments: An iron protein. Highly specific; catechol and pyrogallol are acted on at less than 1% of the rate at which hydroxyquinol is oxidized.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 91847-14-2
References:
1. Sze, I.S.-Y. and Dagley, S. Properties of salicylate hydroxylase and hydroxyquinol 1,2-dioxygenase purified from Trichosporon cutaneum. J. Bacteriol. 159 (1984) 353-359. [PMID: 6539772]
2. Ferraroni, M., Seifert, J., Travkin, V.M., Thiel, M., Kaschabek, S., Scozzafava, A., Golovleva, L., Schlomann, M. and Briganti, F. Crystal structure of the hydroxyquinol 1,2-dioxygenase from Nocardioides simplex 3E, a key enzyme involved in polychlorinated aromatics biodegradation. J. Biol. Chem. 280 (2005) 21144-21154. [PMID: 15772073]
3. Hatta, T., Nakano, O., Imai, N., Takizawa, N. and Kiyohara, H. Cloning and sequence analysis of hydroxyquinol 1,2-dioxygenase gene in 2,4,6-trichlorophenol-degrading Ralstonia pickettii DTP0602 and characterization of its product. J. Biosci. Bioeng. 87 (1999) 267-272. [PMID: 16232466]
Accepted name: 1-hydroxy-2-naphthoate 1,2-dioxygenase
Reaction: 1-hydroxy-2-naphthoate + O2 = (3Z)-4-(2-carboxyphenyl)-2-oxobut-3-enoate
For diagram of reaction click here
Other name(s): 1-hydroxy-2-naphthoate dioxygenase; 1-hydroxy-2-naphthoate-degrading enzyme; 1-hydroxy-2-naphthoic acid dioxygenase; 1-hydroxy-2-naphthoate:oxygen 1,2-oxidoreductase (decyclizing)
Systematic name: 1-hydroxy-2-naphthoate:oxygen 1,2-oxidoreductase (ring-opening)
Comments: Requires Fe2+. Involved, with EC 4.1.2.34 4-(2-carboxyphenyl)-2-oxobut-3-enoate aldolase, in the metabolism of phenanthrene in bacteria.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, CAS registry number: 85941-64-6
References:
1. Barnsley, E.A. Phthalate pathway of phenanthrene metabolism: formation of 2'-carboxybenzalpyruvate. J. Bacteriol. 154 (1983) 113-117. [PMID: 6833175]
Accepted name: biphenyl-2,3-diol 1,2-dioxygenase
Reaction: biphenyl-2,3-diol + O2 = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
Other name(s): 2,3-dihydroxybiphenyl dioxygenase; biphenyl-2,3-diol dioxygenase; bphC (gene name); biphenyl-2,3-diol:oxygen 1,2-oxidoreductase (decyclizing)
Systematic name: biphenyl-2,3-diol:oxygen 1,2-oxidoreductase (ring-opening)
Comments: Contains Fe2+ or Mn2+ [3]. This enzyme participates in the degradation pathway of biphenyl and PCB (polychlorinated biphenyls), and catalyses the first ring cleavage step by incorporating two atomic oxygens into the catechol ring formed by EC 1.3.1.56, cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase. The enzyme from the bacterium Burkholderia xenovorans LB400 can also process catechol, 3-methylcatechol, and 4-methylcatechol, but less efficiently [1]. The enzyme from the carbazole-degrader Pseudomonas resinovorans strain CA10 also accepts 2'-aminobiphenyl-2,3-diol [5]. The enzyme from the bacterium Ralstonia sp. SBUG 290 can also accept 1,2-dihydroxydibenzofuran and 1,2-dihydroxynaphthalene [4]. The enzyme is strongly inhibited by the substrate [1]. Not identical with EC 1.13.11.2 catechol 2,3-dioxygenase.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 103679-58-9
References:
1. Eltis, L.D., Hofmann, B., Hecht, H.J., Lunsdorf, H. and Timmis, K.N. Purification and crystallization of 2,3-dihydroxybiphenyl 1,2-dioxygenase. J. Biol. Chem. 268 (1993) 2727-2732. [PMID: 8428946]
2. Uragami, Y., Senda, T., Sugimoto, K., Sato, N., Nagarajan, V., Masai, E., Fukuda, M. and Mitsu, Y. Crystal structures of substrate free and complex forms of reactivated BphC, an extradiol type ring-cleavage dioxygenase. J. Inorg. Biochem. 83 (2001) 269-279. [PMID: 11293547]
3. Hatta, T., Mukerjee-Dhar, G., Damborsky, J., Kiyohara, H. and Kimbara, K. Characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a polychlorinated biphenyl- and naphthalene-degrading Bacillus sp. JF8. J. Biol. Chem. 278 (2003) 21483-21492. [PMID: 12672826]
4. Wesche, J., Hammer, E., Becher, D., Burchhardt, G. and Schauer, F. The bphC gene-encoded 2,3-dihydroxybiphenyl-1,2-dioxygenase is involved in complete degradation of dibenzofuran by the biphenyl-degrading bacterium Ralstonia sp. SBUG 290. J Appl Microbiol 98 (2005) 635-645. [PMID: 15715866]
5. Iwata, K., Nojiri, H., Shimizu, K., Yoshida, T., Habe, H. and Omori, T. Expression, purification, and characterization of 2'-aminobiphenyl-2,3-diol 1,2-dioxygenase from carbazole-degrader Pseudomonas resinovorans strain CA10. Biosci. Biotechnol. Biochem. 67 (2003) 300-307. [PMID: 12728990]
Accepted name: arachidonate 8-lipoxygenase
Reaction: arachidonate + O2 = (5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14-tetraenoate
Other name(s): 8-lipoxygenase; 8(R)-lipoxygenase
Systematic name: arachidonate:oxygen 8-oxidoreductase
Comments: From the coral Pseudoplexaura porosa.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 100900-72-9
References:
1. Bundy, G.L., Nidy, E.G., Epps, D.E., Mizsak, S.A. and Wnuk, R.J. Discovery of an arachidonic acid C-8 lipoxygenase in the gorgonian coral Pseudoplexaura porosa. J. Biol. Chem. 261 (1986) 747-751. [PMID: 2867091]
Accepted name: 2,4'-dihydroxyacetophenone dioxygenase
Reaction: 2,4'-dihydroxyacetophenone + O2 = 4-hydroxybenzoate + formate
Other name(s): (4-hydroxybenzoyl)methanol oxygenase
Systematic name: 2,4'-dihydroxyacetophenone oxidoreductase (C-C-bond-cleaving)
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 257617-97-3
References:
1. Hopper, D.J. Oxygenase properties of the (4-hydroxybenzoyl)methanol-cleavage enzyme from an Alcaligenes sp. Biochem. J. 239 (1986) 469-472. [PMID: 3814084]
[EC 1.13.11.42 Deleted entry: indoleamine-pyrrole 2,3-dioxygenase (EC 1.13.11.42 created 1992, deleted 2006)]
Accepted name: lignostilbene αβ-dioxygenase
Reaction: 1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene + O2 = 2 vanillin
Systematic name: 1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene:oxygen oxidoreductase (αβ-bond-cleaving)
Comments: An iron protein. The enzyme catalyses oxidative cleavage of the interphenyl double bond in the synthetic substrate and lignin-derived stilbenes. It is responsible for the degradation of a diarylpropane-type structure in lignin.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 124834-28-2
References:
1. Kamoda, S., Habu, N., Samejima, M. and Yoshimoto, T. Purification and some properties of lignostilbene-αβ- dioxygenase responsible for the Cα-Cβ cleavage of a diarylpropane type lignin model-compound from Pseudomonas sp TMY1009. Agric. Biol. Chem. 53 (1989) 2757-2761.
[EC 1.13.11.44 Deleted entry: linoleate diol synthase. Activity is covered by EC 1.13.11.60, linoleate 8R-lipoxygenase and EC 5.4.4.6, 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase. (EC 1.13.11.44 created 2000, deleted 2011)]
Accepted name: linoleate 11-lipoxygenase
Reaction: linoleate + O2 = (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
Glossary:
Other name(s): linoleate dioxygenase; manganese lipoxygenase
Systematic name: linoleate:oxygen 11S-oxidoreductase
Comments: The product (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate, is converted, more slowly, into (9Z,11E)-(13R)-13-hydroperoxyoctadeca-9,11-dienoate. The enzyme from the fungus Gaeumannomyces graminis requires Mn2+. It also acts on α-linolenate, whereas γ-linolenate is a poor substrate. Oleate and arachidonate are not substrates.
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CAS registry number:
References:
1. Hamberg, M., Su, C. and Oliw, E.H. Manganese lipoxygenase: Discovery of bis-allylic hydroperoxide as product and intermediate in a lipoxygenase reaction. J. Biol. Chem. 273 (1998) 13080-13088. [PMID: 9582346]
2. Oliw, E.H., Su, C., Skogstrom, T. and Benthin, G. Analysis of novel hydroperoxides and other metabolites of oleic, linoleic, and linolenic acids by liquid chromatography-mass spectrometry with ion trap MSn. Lipids 33 (1998) 843-852. [PMID: 9778131]
3. Su, C. and Oliw, E.H. Manganese lipoxygenase: Purification and characterization. J. Biol. Chem. 273 (1998) 13072-13079. [PMID: 9582345]
Accepted name: 4-hydroxymandelate synthase
Reaction: 4-hydroxyphenylpyruvate + O2 = (S)-4-hydroxymandelate + CO2
For diagram of reaction click here.
Glossary: (S)-4-hydroxymandelate = (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate
Other name(s): 4-hydroxyphenylpyruvate dioxygenase II
Systematic name: (S)-4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating)
Comments: Requires Fe2+. Involved in the biosynthesis of the vancomycin group of glycopeptide antibiotics.
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CAS registry number: 280566-04-3
References:
1. Hubbard, B.K., Thomas, M.G. and Walsh, C.T. Biosynthesis of L-p-hydroxyphenylglycine, a non-proteinogenic amino acid constituent of peptide antibiotics. Chem. Biol. 7 (2000) 931-942. [PMID: 11137816]
2. Choroba, O.W., Williams, D.H. and Spencer, J.B. Biosynthesis of the vancomycin group of antibiotics: involvement of an unusual dioxygenase in the pathway to (S)-4-hydroxyphenylglycine. J. Am. Chem. Soc. 122 (2000) 5389-5390.
Accepted name: 3-hydroxy-4-oxoquinoline 2,4-dioxygenase
Reaction: 3-hydroxy-1H-quinolin-4-one + O2 = N-formylanthranilate + CO
For diagram click here.
Other name(s): (1H)-3-hydroxy-4-oxoquinoline 2,4-dioxygenase; 3-hydroxy-4-oxo-1,4-dihydroquinoline 2,4-dioxygenase; 3-hydroxy-4(1H)-one, 2,4-dioxygenase; quinoline-3,4-diol 2,4-dioxygenase
Systematic name: 3-hydroxy-1H-quinolin-4-one 2,4-dioxygenase (CO-forming)
Comments: Does not contain a metal centre or organic cofactor. Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of carbon monoxide. The enzyme from Pseudomonas putida is highly specific for this substrate.
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CAS registry number: 238093-32-8
References:
1. Bauer, I., De Beyer, A., Tsisuaka, B., Fetzner, S. and Lingens, F. A novel type of oxygenolytic ring cleavage: 2,4-Oxygenation and decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline. FEMS Microbiol. Lett. 117 (1994) 299-304.
2. Bauer, I., Max, N., Fetzner, S. and Lingens, F. 2,4-Dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Ru61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1. Eur. J. Biochem. 240 (1996) 576-583. [PMID: 8856057]
3. Fischer, F., Kunne, S. and Fetzner, S. Bacterial 2,4-dioxygenases: new members of the α/β hydrolase-fold superfamily of enzymes functionally related to serine hydrolases. J. Bacteriol. 181 (1999) 5725-5733. [PMID: 10482514]
Accepted name: 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase
Reaction: 3-hydroxy-2-methyl-1H-quinolin-4-one + O2 = N-acetylanthranilate + CO
For diagram click here.
Other name(s): (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase
Systematic name: 3-hydroxy-2-methyl-1H-quinolin-4-one 2,4-dioxygenase (CO-forming)
Comments: Does not contain a metal centre or organic cofactor. Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of carbon monoxide. The enzyme from Arthrobacter sp. can also act on 3-hydroxy-4-oxoquinoline, forming N-formylanthranilate and CO (cf. EC 1.13.11.47, 3-hydroxy-4-oxoquinoline 2,4-dioxygenase), but more slowly.
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CAS registry number: 160995-63-1
References:
1. Bauer, I., De Beyer, A., Tsisuaka, B., Fetzner, S. and Lingens, F. A novel type of oxygenolytic ring cleavage: 2,4-Oxygenation and decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline. FEMS Microbiol. Lett. 117 (1994) 299-304.
2. Bauer, I., Max, N., Fetzner, S. and Lingens, F. 2,4-Dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Ru61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1. Eur. J. Biochem. 240 (1996) 576-583. [PMID: 8856057]
3. Fischer, F., Kunne, S. and Fetzner, S. Bacterial 2,4-dioxygenases: new members of the α/β hydrolase-fold superfamily of enzymes functionally related to serine hydrolases. J. Bacteriol. 181 (1999) 5725-5733. [PMID: 10482514]
Accepted name: chlorite O2-lyase
Reaction: chloride + O2 = chlorite
Other name(s): [chlorite dismutase]
Comments: Reaction occurs in the reverse direction in chlorate- and perchlorate-reducing bacteria. There is no activity when chlorite is replaced by hydrogen peroxide, perchlorate, chlorate or nitrite. The term 'chlorite dismutase' is misleading as the reaction does not involve dismutation/disproportionation. Contains iron and protoheme IX.
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References:
1. van Ginkel, C.G., Rikken, G.B., Kron, A.G.M. and Kengen, S.W.M. Purification and characterization of chlorite dismutase: a novel oxygen-generating enzyme. Arch. Microbiol. 166 (1996) 321-326. [PMID: 8929278]
2. Stenklo, K., Thorell, H.D., Bergius, H., Aasa, R. and Nilsson, T. Chlorite dismutase from Ideonella dechloratans. J. Biol. Inorg. Chem. 6 (2001) 601-607. [PMID: 11472023]
Accepted name: acetylacetone-cleaving enzyme
Reaction: pentane-2,4-dione + O2 = acetate + methylglyoxal
Glossary: methylglyoxal = 2-oxopropanal
Other name(s): Dke1; acetylacetone dioxygenase; diketone cleaving dioxygenase; diketone cleaving enzyme
Systematic name: acetylacetone:oxygen oxidoreductase
Comments: An iron(II)-dependent enzyme. Forms the first step in the acetylacetone degradation pathway of Acinetobacter johnsonii. While acetylacetone is by far the best substrate, heptane-3,5-dione, octane-2,4-dione, 2-acetylcyclohexanone and ethyl acetoacetate can also act as substrates.
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CAS registry number: 524047-53-8
References:
1. Straganz, G.D., Glieder, A., Brecker, L., Ribbons, D.W. and Steiner, W. Acetylacetone-cleaving enzyme Dke1: a novel C-C-bond-cleaving enzyme from Acinetobacter johnsonii. Biochem. J. 369 (2003) 573-581. [PMID: 12379146]
Accepted name: 9-cis-epoxycarotenoid dioxygenase
Reaction: (1) a 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a 12'-apo-carotenal
(2) 9-cis-violaxanthin + O2 = 2-cis,4-trans-xanthoxin + (3S,5R,6S)-5,6-epoxy-3-hydroxy-5,6-dihydro-12'-apo-β-caroten-12'-al
(3) 9'-cis-neoxanthin + O2 = 2-cis,4-trans-xanthoxin + (3S,5R,6R)-3,5-dihydroxy-6,7-didehydro-5,6-dihydro-12'-apo-β-caroten-12'-al
For diagram click here.
Other name(s): nine-cis-epoxycarotenoid dioxygenase; NCED; AtNCED3; PvNCED1; VP14
Systematic name: 9-cis-epoxycarotenoid 11,12-dioxygenase
Comments: Requires iron(II). Acts on 9-cis-violaxanthin and 9'-cis-neoxanthin but not on the all-trans isomers [2,3]. In vitro, it will cleave 9-cis-zeaxanthin. Catalyses the first step of abscisic-acid biosynthesis from carotenoids in chloroplasts, in response to water stress. The other enzymes involved in the abscisic-acid biosynthesis pathway are EC 1.1.1.288 (xanthoxin dehydrogenase), EC 1.2.3.14 (abscisic aldehyde oxidase) and EC 1.14.13.93 [(+)-abscisic acid 8'-hydroxylase].
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CAS registry number: 199877-10-6
References:
1. Schwartz, S.H., Tan, B.C., Gage, D.A., Zeevaart, J.A. and McCarty, D.R. Specific oxidative cleavage of carotenoids by VP14 of maize. Science 276 (1997) 1872-1874. [PMID: 9188535]
2. Tan, B.C., Schwartz, S.H., Zeevaart, J.A. and McCarty, D.R. Genetic control of abscisic acid biosynthesis in maize. Proc. Natl. Acad. Sci. USA 94 (1997) 12235-12240. [PMID: 9342392]
3. Qin, X. and Zeevaart, J.A. The 9-cis-epoxycarotenoid cleavage reaction is the key regulatory step of abscisic acid biosynthesis in water-stressed bean. Proc. Natl. Acad. Sci. USA 96 (1999) 15354-15361. [PMID: 10611388]
4. Thompson, A.J., Jackson, A.C., Symonds, R.C., Mulholland, B.J., Dadswell, A.R., Blake, P.S., Burbidge, A. and Taylor, I.B. Ectopic expression of a tomato 9-cis-epoxycarotenoid dioxygenase gene causes over-production of abscisic acid. Plant J. 23 (2000) 363-374. [PMID: 10929129]
5. Iuchi, S., Kobayashi, M., Taji, T., Naramoto, M., Seki, M., Kato, T., Tabata, S., Kakubari, Y., Yamaguchi-Shinozaki, K. and Shinozaki, K. Regulation of drought tolerance by gene manipulation of 9-cis-epoxycarotenoid dioxygenase, a key enzyme in abscisic acid biosynthesis in Arabidopsis. Plant J. 27 (2001) 325-333. [PMID: 11532178]
6. Iuchi, S., Kobayashi, M., Taji, T., Naramoto, M., Seki, M., Kato, T., Tabata, S., Kakubari, Y., Yamaguchi-Shinozaki, K. and Shinozaki, K. Regulation of drought tolerance by gene manipulation of 9-cis-epoxycarotenoid dioxygenase, a key enzyme in abscisic acid biosynthesis in Arabidopsis. Erratum. Plant J. 30 (2002) 611. [PMID: 11532178]
Accepted name: indoleamine 2,3-dioxygenase
Reaction: (1) D-tryptophan + O2 = N-formyl-D-kynurenine
(2) L-tryptophan + O2 = N-formyl-L-kynurenine
For diagram, click here
Other name(s): IDO (ambiguous); tryptophan pyrrolase (ambiguous); D-tryptophan:oxygen 2,3-oxidoreductase (decyclizing)
Systematic name: D-tryptophan:oxygen 2,3-oxidoreductase (ring-opening)
Comments: A protohemoprotein. Requires ascorbic acid and methylene blue for activity. This enzyme has broader substrate specificity than EC 1.13.11.11, tryptophan 2,3-dioxygenase [1]. It is induced in response to pathological conditions and host-defense mechanisms and its distribution in mammals is not confined to the liver [2]. While the enzyme is more active with D-tryptophan than L-tryptophan, its only known function to date is in the metabolism of L-tryptophan [2,6]. Superoxide radicals can replace O2 as oxygen donor [4,7].
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CAS registry number: 9014-51-1
References:
1. Yamamoto, S. and Hayaishi, O. Tryptophan pyrrolase of rabbit intestine. D- and L-tryptophan-cleaving enzyme or enzymes. J. Biol. Chem. 242 (1967) 5260-5266. [PMID: 6065097]
2. Yasui, H., Takai, K., Yoshida, R. and Hayaishi, O. Interferon enhances tryptophan metabolism by inducing pulmonary indoleamine 2,3-dioxygenase: its possible occurrence in cancer patients. Proc. Natl. Acad. Sci. USA 83 (1986) 6622-6626. [PMID: 2428037]
3. Takikawa, O., Yoshida, R., Kido, R. and Hayaishi, O. Tryptophan degradation in mice initiated by indoleamine 2,3-dioxygenase. J. Biol. Chem. 261 (1986) 3648-3653. [PMID: 2419335]
4. Hirata, F., Ohnishi, T. and Hayaishi, O. Indoleamine 2,3-dioxygenase. Characterization and properties of enzyme. O2- complex. J. Biol. Chem. 252 (1977) 4637-4642. [PMID: 194886]
5. Dang, Y., Dale, W.E. and Brown, O.R. Comparative effects of oxygen on indoleamine 2,3-dioxygenase and tryptophan 2,3-dioxygenase of the kynurenine pathway. Free Radic. Biol. Med. 28 (2000) 615-624. [PMID: 10719243]
6. Littlejohn, T.K., Takikawa, O., Truscott, R.J. and Walker, M.J. Asp274 and His346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase. J. Biol. Chem. 278 (2003) 29525-29531. [PMID: 12766158]
7. Thomas, S.R. and Stocker, R. Redox reactions related to indoleamine 2,3-dioxygenase and tryptophan metabolism along the kynurenine pathway. Redox Rep. 4 (1999) 199-220. [PMID: 10731095]
8. Sono, M. Spectroscopic and equilibrium studies of ligand and organic substrate binding to indolamine 2,3-dioxygenase. Biochemistry 29 (1990) 1451-1460. [PMID: 2334706]
Accepted name: acireductone dioxygenase (Ni2+-requiring)
Reaction: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-(methylsulfanylo)propanoate + formate + CO
For diagram click here or mechanism click here
Glossary: acireductone = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one
Other name(s): ARD; 2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase (ambiguous); acireductone dioxygenase (ambiguous); E-2; 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one:oxygen oxidoreductase (formate- and CO-forming)
Systematic name: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one:oxygen oxidoreductase (formate- and CO-forming)
Comments: Requires Ni2+. If iron(II) is bound instead of Ni2+, the reaction catalysed by EC 1.13.11.54, acireductone dioxygenase [iron(II)-requiring], occurs instead [1]. The enzyme from Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC strain 8724 is involved in the methionine salvage pathway.
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References:
1. Wray, J.W. and Abeles, R.H. A bacterial enzyme that catalyzes formation of carbon monoxide. J. Biol. Chem. 268 (1993) 21466-21469. [PMID: 8407993]
2. Wray, J.W. and Abeles, R.H. The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases. J. Biol. Chem. 270 (1995) 3147-3153. [PMID: 7852397]
3. Furfine, E.S. and Abeles, R.H. Intermediates in the conversion of 5'-S-methylthioadenosine to methionine in Klebsiella pneumoniae. J. Biol. Chem. 263 (1988) 9598-9606. [PMID: 2838472]
4. Dai, Y., Wensink, P.C. and Abeles, R.H. One protein, two enzymes. J. Biol. Chem. 274 (1999) 1193-1195. [PMID: 9880484]
5. Mo, H., Dai, Y., Pochapsky, S.S. and Pochapsky, T.C. 1H, 13C and 15N NMR assignments for a carbon monoxide generating metalloenzyme from Klebsiella pneumoniae. J. Biomol. NMR 14 (1999) 287-288. [PMID: 10481280]
6. Dai, Y., Pochapsky, T.C. and Abeles, R.H. Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae. Biochemistry 40 (2001) 6379-6387. [PMID: 11371200]
7. Al-Mjeni, F., Ju, T., Pochapsky, T.C. and Maroney, M.J. XAS investigation of the structure and function of Ni in acireductone dioxygenase. Biochemistry 41 (2002) 6761-6769. [PMID: 12022880]
8. Pochapsky, T.C., Pochapsky, S.S., Ju, T., Mo, H., Al-Mjeni, F. and Maroney, M.J. Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae. Nat. Struct. Biol. 9 (2002) 966-972. [PMID: 12402029]
Accepted name: acireductone dioxygenase [iron(II)-requiring]
Reaction: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-(methylsulfanyl)-2-oxobutanoate + formate
For diagram click here or mechanism click here
Other name(s): ARD'; 2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase (ambiguous); acireductone dioxygenase (ambiguous); E-2'; E-3 dioxygenase; 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one:oxygen oxidoreductase (formate-forming)
Systematic name: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one:oxygen oxidoreductase (formate-forming)
Comments: Requires iron(II). If Ni2+ is bound instead of iron(II), the reaction catalysed by EC 1.13.11.53, acireductone dioxygenase (Ni2+-requiring), occurs instead. The enzyme from Klebsiella oxytoca (formerly Klebsiella pneumoniae) ATCC strain 8724 is involved in the methionine salvage pathway.
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BRENDA,
EXPASY,
KEGG,
Metacyc,
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CAS registry number:
References:
1. Wray, J.W. and Abeles, R.H. A bacterial enzyme that catalyzes formation of carbon monoxide. J. Biol. Chem. 268 (1993) 21466-21469. [PMID: 8407993]
2. Wray, J.W. and Abeles, R.H. The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases. J. Biol. Chem. 270 (1995) 3147-3153. [PMID: 7852397]
3. Furfine, E.S. and Abeles, R.H. Intermediates in the conversion of 5'-S-methylthioadenosine to methionine in Klebsiella pneumoniae. J. Biol. Chem. 263 (1988) 9598-9606. [PMID: 2838472]
4. Dai, Y., Wensink, P.C. and Abeles, R.H. One protein, two enzymes. J. Biol. Chem. 274 (1999) 1193-1195. [PMID: 9880484]
5. Mo, H., Dai, Y., Pochapsky, S.S. and Pochapsky, T.C. 1H, 13C and 15N NMR assignments for a carbon monoxide generating metalloenzyme from Klebsiella pneumoniae. J. Biomol. NMR 14 (1999) 287-288. [PMID: 10481280]
6. Dai, Y., Pochapsky, T.C. and Abeles, R.H. Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae. Biochemistry 40 (2001) 6379-6387. [PMID: 11371200]
7. Al-Mjeni, F., Ju, T., Pochapsky, T.C. and Maroney, M.J. XAS investigation of the structure and function of Ni in acireductone dioxygenase. Biochemistry 41 (2002) 6761-6769. [PMID: 12022880]
8. Pochapsky, T.C., Pochapsky, S.S., Ju, T., Mo, H., Al-Mjeni, F. and Maroney, M.J. Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae. Nat. Struct. Biol. 9 (2002) 966-972. [PMID: 12402029]
Accepted name: sulfur oxygenase/reductase
Reaction: 4 sulfur + 4 H2O + O2 = 2 hydrogen sulfide + 2 HSO3– + 2 H+
Glossary: bisulfite = HSO3–
Other name(s): SOR; sulfur oxygenase; sulfur oxygenase reductase
Systematic name: sulfur:oxygen oxidoreductase (hydrogen-sulfide- and sulfite-forming)
Comments: This enzyme, which is found in thermophilic microorganisms, contains one mononuclear none-heme iron centre per subunit. Elemental sulfur is both the electron donor and one of the two known acceptors, the other being oxygen. Another reaction product is thiosulfate, but this is probably formed non-enzymically at elevated temperature from sulfite and sulfur [1]. This enzyme differs from EC 1.13.11.18, sulfur dioxygenase and EC 1.12.98.4, sulfur reductase, in that both activities are found together.
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CAS registry number: 120598-92-7
References:
1. Kletzin, A. Coupled enzymatic production of sulfite, thiosulfate, and hydrogen sulfide from sulfur: purification and properties of a sulfur oxygenase reductase from the facultatively anaerobic archaebacterium Desulfurolobus ambivalens. J. Bacteriol. 171 (1989) 1638-1643. [PMID: 2493451]
2. Kletzin, A. Molecular characterization of the sor gene, which encodes the sulfur oxygenase/reductase of the thermoacidophilic Archaeum Desulfurolobus ambivalens. J. Bacteriol. 174 (1992) 5854-5859. [PMID: 1522063]
3. Sun, C.W., Chen, Z.W., He, Z.G., Zhou, P.J. and Liu, S.J. Purification and properties of the sulfur oxygenase/reductase from the acidothermophilic archaeon, Acidianus strain S5. Extremophiles 7 (2003) 131-134. [PMID: 12664265]
4. Urich, T., Bandeiras, T.M., Leal, S.S., Rachel, R., Albrecht, T., Zimmermann, P., Scholz, C., Teixeira, M., Gomes, C.M. and Kletzin, A. The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre. Biochem. J. 381 (2004) 137-146. [PMID: 15030315]
Accepted name: 1,2-dihydroxynaphthalene dioxygenase
Reaction: naphthalene-1,2-diol + O2 = 2-hydroxy-2H-chromene-2-carboxylate
For diagram of reaction, click here
Other name(s): 1,2-DHN dioxygenase; DHNDO; 1,2-dihydroxynaphthalene oxygenase; 1,2-dihydroxynaphthalene:oxygen oxidoreductase
Systematic name: naphthalene-1,2-diol:oxygen oxidoreductase
Comments: This enzyme is involved in naphthalene degradation. Requires Fe2+.
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CAS registry number:
References:
1. Kuhm, A.E., Stolz, A., Ngai, K.L. and Knackmuss, H.J. Purification and characterization of a 1,2-dihydroxynaphthalene dioxygenase from a bacterium that degrades naphthalenesulfonic acids. J. Bacteriol. 173 (1991) 3795-3802. [PMID: 2050635]
2. Keck, A., Conradt, D., Mahler, A., Stolz, A., Mattes, R. and Klein, J. Identification and functional analysis of the genes for naphthalenesulfonate catabolism by Sphingomonas xenophaga BN6. Microbiology 152 (2006) 1929-1940. [PMID: 16804169]
3. Patel, T.R. and Barnsley, E.A. Naphthalene metabolism by pseudomonads: purification and properties of 1,2-dihydroxynaphthalene oxygenase. J. Bacteriol. 143 (1980) 668-673. [PMID: 7204331]
Accepted name: gallate dioxygenase
Reaction: 3,4,5-trihydroxybenzoate + O2 = (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate
For diagram of reaction click here
Other name(s): GalA; gallate:oxygen oxidoreductase
Systematic name: 3,4,5-trihydroxybenzoate:oxygen oxidoreductase
Comments: Contains non-heme Fe2+. The enzyme is a ring-cleavage dioxygenase that acts specifically on 3,4,5-trihydroxybenzoate to produce the keto-tautomer of 4-oxalomesaconate [1,2].
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References:
1. Nogales, J., Canales, A., JimŽnez-Barbero, J., García, J.L. and Díaz, E. Molecular characterization of the gallate dioxygenase from Pseudomonas putida KT2440. The prototype of a new subgroup of extradiol dioxygenases. J. Biol. Chem. 280 (2005) 35382-35390. [PMID: 16030014]
2. Nogales, J., Canales, A., Jimenez-Barbero, J., Serra, B., Pingarron, J.M., Garcia, J.L. and Diaz, E. Unravelling the gallic acid degradation pathway in bacteria: the gal cluster from Pseudomonas putida. Mol. Microbiol. 79 (2011) 359-374. [PMID: 21219457]
Accepted name: linoleate 9S-lipoxygenase
Reaction: linoleate + O2 = (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoate
Glossary: linoleate = (9Z,12Z)-octadeca-9,12-dienoate
Other name(s): 9-lipoxygenase; 9S-lipoxygenase; linoleate 9-lipoxygenase; LOX1 (gene name); 9S-LOX
Systematic name: linoleate:oxygen 9S-oxidoreductase
Comments: Contains nonheme iron. A common plant lipoxygenase that oxidizes linoleate and α-linolenate, the two most common polyunsaturated fatty acids in plants, by inserting molecular oxygen at the C9 position with (S)-configuration. The enzyme plays a physiological role during the early stages of seedling growth. The enzyme from Arabidopsis thaliana shows comparable activity towards linoleate and linolenate [4]. EC 1.13.11.12 (linoleate 13S-lipoxygenase) catalyses a similar reaction at another position of these fatty acids.
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References:
1. Vellosillo, T., Martinez, M., Lopez, M.A., Vicente, J., Cascon, T., Dolan, L., Hamberg, M. and Castresana, C. Oxylipins produced by the 9-lipoxygenase pathway in Arabidopsis regulate lateral root development and defense responses through a specific signaling cascade. Plant Cell 19 (2007) 831-846. [PMID: 17369372]
2. Boeglin, W.E., Itoh, A., Zheng, Y., Coffa, G., Howe, G.A. and Brash, A.R. Investigation of substrate binding and product stereochemistry issues in two linoleate 9-lipoxygenases. Lipids 43 (2008) 979-987. [PMID: 18795358]
3. Andreou, A.Z., Hornung, E., Kunze, S., Rosahl, S. and Feussner, I. On the substrate binding of linoleate 9-lipoxygenases. Lipids 44 (2009) 207-215. [PMID: 19037675]
4. Bannenberg, G., Martinez, M., Hamberg, M. and Castresana, C. Diversity of the enzymatic activity in the lipoxygenase gene family of Arabidopsis thaliana. Lipids 44 (2009) 85-95. [PMID: 18949503]
Accepted name: torulene dioxygenase
Reaction: torulene + O2 = 4'-apo-β,ψ-caroten-4'-al + 3-methylbut-2-enal
For diagram of reaction click here
Glossary: torulene = 3',4'-didehydro-β,ψ-carotene
Other name(s): CAO-2; CarT
Systematic name: torulene:oxygen oxidoreductase
Comments: It is assumed that 3-methylbut-2-enal is formed. The enzyme cannot cleave the saturated 3',4'-bond of γ-carotene which implies that a 3',4'-double bond is neccessary for this reaction.
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References:
1. Prado-Cabrero, A., Estrada, A.F., Al-Babili, S. and Avalos, J. Identification and biochemical characterization of a novel carotenoid oxygenase: elucidation of the cleavage step in the Fusarium carotenoid pathway. Mol. Microbiol. 64 (2007) 448-460. [PMID: 17493127]
2. Saelices, L., Youssar, L., Holdermann, I., Al-Babili, S. and Avalos, J. Identification of the gene responsible for torulene cleavage in the Neurospora carotenoid pathway. Mol. Genet. Genomics 278 (2007) 527-537. [PMID: 17610084]
3. Estrada, A.F., Maier, D., Scherzinger, D., Avalos, J. and Al-Babili, S. Novel apocarotenoid intermediates in Neurospora crassa mutants imply a new biosynthetic reaction sequence leading to neurosporaxanthin formation. Fungal Genet. Biol. 45 (2008) 1497-1505. [PMID: 18812228]
Accepted name: linoleate 8R-lipoxygenase
Reaction: linoleate + O2 = (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate
Glossary: linoleate = (9Z,12Z)-octadeca-9,12-dienoate
Other name(s): linoleic acid 8R-dioxygenase; 5,8-LDS (bifunctional enzyme); 7,8-LDS (bifunctional enzyme); 5,8-linoleate diol synthase (bifunctional enzyme); 7,8-linoleate diol synthase (bifunktional enzyme); PpoA
Systematic name: linoleate:oxygen (8R)-oxidoreductase
Comments: The enzyme contains heme [1,4]. The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyse two separate reactions. Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, which is subsequently isomerized by the C-terminal P450 heme thiolate domain to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.5, 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase) [1]. The bifunctional enzyme from Gaeumannomyces graminis also catalyses the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, but its second domain isomerizes it to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.6, 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase) [4].
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References:
1. Brodhun, F., Gobel, C., Hornung, E. and Feussner, I. Identification of PpoA from Aspergillus nidulans as a fusion protein of a fatty acid heme dioxygenase/peroxidase and a cytochrome P450. J. Biol. Chem. 284 (2009) 11792-11805. [PMID: 19286665]
2. Hamberg, M., Zhang, L.-Y., Brodowsky, I.D. and Oliw, E.H. Sequential oxygenation of linoleic acid in the fungus Gaeumannomyces graminis: stereochemistry of dioxygenase and hydroperoxide isomerase reactions. Arch. Biochem. Biophys. 309 (1994) 77-80. [PMID: 8117115]
3. Garscha, U. and Oliw, E. Pichia expression and mutagenesis of 7,8-linoleate diol synthase change the dioxygenase and hydroperoxide isomerase. Biochem. Biophys. Res. Commun. 373 (2008) 579-583. [PMID: 18586008]
4. Su, C. and Oliw, E.H. Purification and characterization of linoleate 8-dioxygenase from the fungus Gaeumannomyces graminis as a novel hemoprotein. J. Biol. Chem. 271 (1996) 14112-14118. [PMID: 8662736]
Accepted name: linolenate 9R-lipoxygenase
Reaction: α-linolenate + O2 = (9R,10E,12Z,15Z)-9-hydroperoxyoctadeca-10,12,15-trienoate
Glossary: linoleate = (9Z,12Z)-octadeca-9,12-dienoate
Other name(s): NspLOX; (9R)-LOX; linoleate 9R-dioxygenase
Systematic name: α-linolenate:oxygen (9R)-oxidoreductase
Comments: In cyanobacteria the enzyme is involved in oxylipin biosynthesis. The enzyme also converts linoleate to (9R,10E,12Z)-9-hydroperoxyoctadeca-10,12-dienoate.
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References:
1. Jerneren, F., Hoffmann, I. and Oliw, E.H. Linoleate 9R-dioxygenase and allene oxide synthase activities of Aspergillus terreus. Arch. Biochem. Biophys. 495 (2010) 67-73. [PMID: 20043865]
2. Andreou, A.Z., Vanko, M., Bezakova, L. and Feussner, I. Properties of a mini 9R-lipoxygenase from Nostoc sp. PCC 7120 and its mutant forms. Phytochemistry 69 (2008) 1832-1837. [PMID: 18439634]
3. Lang, I., Gobel, C., Porzel, A., Heilmann, I. and Feussner, I. A lipoxygenase with linoleate diol synthase activity from Nostoc sp. PCC 7120. Biochem. J. 410 (2008) 347-357. [PMID: 18031288]
Accepted name: linoleate 10R-lipoxygenase
Reaction: linoleate + O2 = (8E,10R,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
Glossary: linoleate = (9Z,12Z)-octadeca-9,12-dienoate
Other name(s): 10R-DOX; (10R)-dioxygenase; 10R-dioxygenase
Systematic name: linoleate:oxygen (10R)-oxidoreductase
Comments: The enzyme is involved in biosynthesis of oxylipins, which affect sporulation, development, and pathogenicity of Aspergillus spp.
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References:
1. Garscha, U. and Oliw, E.H. Leucine/valine residues direct oxygenation of linoleic acid by (10R)- and (8R)-dioxygenases: expression and site-directed mutagenesis of (10R)-dioxygenase with epoxyalcohol synthase activity. J. Biol. Chem. 284 (2009) 13755-13765. [PMID: 19289462]
2. Jerneren, F., Garscha, U., Hoffmann, I., Hamberg, M. and Oliw, E.H. Reaction mechanism of 5,8-linoleate diol synthase, 10R-dioxygenase, and 8,11-hydroperoxide isomerase of Aspergillus clavatus. Biochim. Biophys. Acta 1801 (2010) 503-507. [PMID: 20045744]
Accepted name: β-carotene 15,15'-dioxygenase
Reaction: β-carotene + O2 = 2 all-trans-retinal
For diagram of reaction click here.
Other name(s): blh (gene name); BCO1 (gene name); BCDO (gene name); carotene dioxygenase; carotene 15,15'-dioxygenase; BCMO1 (misleading); β-carotene 15,15'-monooxygenase (incorrect)
Systematic name: β-carotene:oxygen 15,15'-dioxygenase (bond-cleaving)
Comments: Requires Fe2+. The enzyme cleaves β-carotene symmetrically, producing two molecules of all-trans-retinal. Both atoms of the oxygen molecule are incorporated into the products [8]. The enzyme can also process β-cryptoxanthin, 8'-apo-β-carotenal, 4'-apo-β-carotenal, α-carotene and γ-carotene in decreasing order. The presence of at least one unsubstituted β-ionone ring in a substrate greater than C30 is mandatory [5]. A prokaryotic enzyme has been reported from the uncultured marine bacterium 66A03, where it is involved in the proteorhodopsin system, which uses retinal as its chromophore [6,7].
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References:
1. Goodman, D.S., Huang, H.S. and Shiratori, T. Mechanism of the biosynthesis of vitamin A from β-carotene. J. Biol. Chem. 241 (1966) 1929-1932. [PMID: 5946623]
2. Goodman, D.S., Huang, H.S., Kanai, M. and Shiratori, T. The enzymatic conversion of all-trans β-carotene into retinal. J. Biol. Chem. 242 (1967) 3543-3554.
3. Yan, W., Jang, G.F., Haeseleer, F., Esumi, N., Chang, J., Kerrigan, M., Campochiaro, M., Campochiaro, P., Palczewski, K. and Zack, D.J. Cloning and characterization of a human β,β-carotene-15,15'-dioxygenase that is highly expressed in the retinal pigment epithelium. Genomics 72 (2001) 193-202. [PMID: 11401432]
4. Leuenberger, M.G., Engeloch-Jarret, C. and Woggon, W.D. The reaction mechanism of the enzyme-catalysed central cleavage of β-carotene to retinal. Angew. Chem. 40 (2001) 2614-2616. [PMID: 11458349]
5. Kim, Y.S. and Oh, D.K. Substrate specificity of a recombinant chicken β-carotene 15,15'-monooxygenase that converts β-carotene into retinal. Biotechnol. Lett. 31 (2009) 403-408. [PMID: 18979213]
6. Kim, Y.S., Kim, N.H., Yeom, S.J., Kim, S.W. and Oh, D.K. In vitro characterization of a recombinant Blh protein from an uncultured marine bacterium as a β-carotene 15,15'-dioxygenase. J. Biol. Chem. 284 (2009) 15781-15793. [PMID: 19366683]
7. Kim, Y.S., Park, C.S. and Oh, D.K. Retinal production from β-carotene by β-carotene 15,15'-dioxygenase from an unculturable marine bacterium. Biotechnol. Lett. 32 (2010) 957-961. [PMID: 20229064]
8. dela Seña, C., Riedl, K.M., Narayanasamy, S., Curley, R.W., Jr., Schwartz, S.J. and Harrison, E.H. The human enzyme that converts dietary provitamin A carotenoids to vitamin A is a dioxygenase. J. Biol. Chem. 289 (2014) 13661-13666. [PMID: 24668807]
Accepted name: 5-nitrosalicylate dioxygenase
Reaction: 5-nitrosalicylate + O2 = 2-oxo-3-(5-oxofuran-2-ylidene)propanoate + nitrite (overall reaction)
Other name(s): naaB (gene name); 5-nitrosalicylate:oxygen 1,2-oxidoreductase (decyclizing)
Systematic name: 5-nitrosalicylate:oxygen 1,2-oxidoreductase (ring-opening)
Comments: The enzyme, characterized from the soil bacterium Bradyrhizobium sp. JS329, is involved in the pathway of 5-nitroanthranilate degradation. It is unusual in being able to catalyse the ring fission without the requirement for prior removal of the nitro group. The product undergoes spontaneous lactonization, with concurrent elimination of the nitro group.
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References:
1. Qu, Y. and Spain, J.C. Biodegradation of 5-nitroanthranilic acid by Bradyrhizobium sp. strain JS329. Appl. Environ. Microbiol. 76 (2010) 1417-1422. [PMID: 20081004]
2. Qu, Y. and Spain, J.C. Molecular and biochemical characterization of the 5-nitroanthranilic acid degradation pathway in Bradyrhizobium sp. strain JS329. J. Bacteriol. 193 (2011) 3057-3063. [PMID: 21498645]
Accepted name: carotenoid isomerooxygenase
Reaction: zeaxanthin + O2 = (3R)-11-cis-3-hydroxyretinal + (3R)-all-trans-3-hydroxyretinal
For diagram of reaction click here.
Other name(s): ninaB (gene name)
Systematic name: zeaxanthin:oxygen 15,15'-oxidoreductase (bond-cleaving, cis-isomerizing)
Comments: The enzyme, characterized from the moth Galleria mellonella and the fruit fly Drosophila melanogaster, is involved in the synthesis of retinal from dietary caroteoids in insects. The enzyme accepts different all-trans carotenoids, including β-carotene, α-carotene and lutein, and catalyses the symmetrical cleavage of the carotenoid and the simultaneous isomerization of only one of the products to a cis configuration. When the substrate is hydroxylated only in one side (as in cryptoxanthin), the enzyme preferentially isomerizes the hydroxylated part of the molecule.
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References:
1. Oberhauser, V., Voolstra, O., Bangert, A., von Lintig, J. and Vogt, K. NinaB combines carotenoid oxygenase and retinoid isomerase activity in a single polypeptide. Proc. Natl. Acad. Sci. USA 105 (2008) 19000-19005. [PMID: 19020100]
Accepted name: hydroquinone 1,2-dioxygenase
Reaction: benzene-1,4-diol + O2 = (2E,4Z)-4-hydroxy-6-oxohexa-2,4-dienoate
For diagram of reaction click here.
Glossary: benzene-1,4-diol = hydroquinone
Other name(s): hydroquinone dioxygenase; benzene-1,4-diol:oxygen 1,2-oxidoreductase (decyclizing)
Systematic name: benzene-1,4-diol:oxygen 1,2-oxidoreductase (ring-opening)
Comments: The enzyme is an extradiol-type dioxygenase, and is a member of the nonheme-iron(II)-dependent dioxygenase family. It catalyses the ring cleavage of a wide range of hydroquinone substrates to produce the corresponding 4-hydroxymuconic semialdehydes.
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References:
1. Miyauchi, K., Adachi, Y., Nagata, Y. and Takagi, M. Cloning and sequencing of a novel meta-cleavage dioxygenase gene whose product is involved in degradation of γ-hexachlorocyclohexane in Sphingomonas paucimobilis. J. Bacteriol. 181 (1999) 6712-6719. [PMID: 10542173]
2. Moonen, M.J., Synowsky, S.A., van den Berg, W.A., Westphal, A.H., Heck, A.J., van den Heuvel, R.H., Fraaije, M.W. and van Berkel, W.J. Hydroquinone dioxygenase from pseudomonas fluorescens ACB: a novel member of the family of nonheme-iron(II)-dependent dioxygenases. J. Bacteriol. 190 (2008) 5199-5209. [PMID: 18502867]
3. Shen, W., Liu, W., Zhang, J., Tao, J., Deng, H., Cao, H. and Cui, Z. Cloning and characterization of a gene cluster involved in the catabolism of p-nitrophenol from Pseudomonas putida DLL-E4. Bioresour. Technol. 101 (2010) 7516-7522. [PMID: 20466541]
Accepted name: 8'-apo-β-carotenoid 14',13'-cleaving dioxygenase
Reaction: 8'-apo-β-carotenol + O2 = 14'-apo-β-carotenal + an uncharacterized product
For diagram of reaction click here.
Other names: 8'-apo-β-carotenol:O2 oxidoreductase (14',13'-cleaving)
Systematic name(s): 8'-apo-β-carotenol:oxygen oxidoreductase (14',13'-cleaving)
Comments: A thiol-dependent enzyme isolated from rat and rabbit. Unlike EC 1.13.11.63, β-carotene-15,15'-monooxygenase, it is not active towards β-carotene. The secondary product has not been characterized, but may be (3E,5E)-7-hydroxy-6-methylhepta-3,5-dien-2-one.
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CAS registry number: 198028-39-6
References:
1. Dmitrovskii, A.A., Gessler, N.N., Gomboeva, S.B., Ershov, Yu.V. and Bykhovsky, V.Ya. Enzymatic oxidation of β-apo-8'-carotenol to β-apo-14'-carotenal by an enzyme different from β-carotene-15,15'-dioxygenase. Biochemistry (Mosc) 62 (1997) 787-792. [PMID: 9331970]
Accepted name: 9-cis-β-carotene 9',10'-cleaving dioxygenase
Reaction: 9-cis-β-carotene + O2 = 9-cis-10'-apo-β-carotenal + β-ionone
For diagram of reaction click here.
Glossary: β-ionone = (3E)-4-(2,6,6-trimethylcyclohex-1-en-1-yl)but-3-en-2-one
Other name(s): CCD7 (gene name); MAX3 (gene name); NCED7 (gene name); 9-cis-β-carotene:O2 oxidoreductase (9',10'-cleaving)
Systematic name: 9-cis-β-carotene:oxygen oxidoreductase (9',10'-cleaving)
Comments: Requires Fe2+. The enzyme participates in a pathway leading to biosynthesis of strigolactones, plant hormones involved in promotion of symbiotic associations known as arbuscular mycorrhiza.
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References:
1. Booker, J., Auldridge, M., Wills, S., McCarty, D., Klee, H. and Leyser, O. MAX3/CCD7 is a carotenoid cleavage dioxygenase required for the synthesis of a novel plant signaling molecule. Curr. Biol. 14 (2004) 1232-1238. [PMID: 15268852]
2. Alder, A., Jamil, M., Marzorati, M., Bruno, M., Vermathen, M., Bigler, P., Ghisla, S., Bouwmeester, H., Beyer, P. and Al-Babili, S. The path from β-carotene to carlactone, a strigolactone-like plant hormone. Science 335 (2012) 1348-1351. [PMID: 22422982]
Accepted name: carlactone synthase
Reaction: 9-cis-10'-apo-β-carotenal + 2 O2 = carlactone + (2E,4E,6E)-7-hydroxy-4-methylhepta-2,4,6-trienal
For diagram of reaction click here and mechanism click here.
Glossary: carlactone = 3-methyl-5-{[(1Z,3E)-2-methyl-4-(2,6,6-trimethylcyclohex-1-en-1-yl)buta-1,3-dien-1-yl]oxy}-5H-furan-2-one
Other name(s): CCD8 (gene name); MAX4 (gene name); NCED8 (gene name); 9-cis-10'-apo-β-carotenal:O2 oxidoreductase (14,15-cleaving, carlactone-forming)
Systematic name: 9-cis-10'-apo-β-carotenal:oxygen oxidoreductase (14,15-cleaving, carlactone-forming)
Comments: Requires Fe2+. The enzyme participates in a pathway leading to biosynthesis of strigolactones, plant hormones involved in promotion of symbiotic associations known as arbuscular mycorrhiza. Also catalyses EC 1.13.11.70, all-trans-10'-apo-β-carotenal 13,14-cleaving dioxygenase, but 10-fold slower. The secondary product has not been characterized, but may be (2E,4E,6E)-7-hydroxy-4-methylhepta-2,4,6-trienal or one of its tautomers. The preferred tautomeric form is not known.
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References:
1. Sorefan, K., Booker, J., Haurogne, K., Goussot, M., Bainbridge, K., Foo, E., Chatfield, S., Ward, S., Beveridge, C., Rameau, C. and Leyser, O. MAX4 and RMS1 are orthologous dioxygenase-like genes that regulate shoot branching in Arabidopsis and pea. Genes Dev. 17 (2003) 1469-1474. [PMID: 12815068]
2. Schwartz, S.H., Qin, X. and Loewen, M.C. The biochemical characterization of two carotenoid cleavage enzymes from Arabidopsis indicates that a carotenoid-derived compound inhibits lateral branching. J. Biol. Chem. 279 (2004) 46940-46945. [PMID: 15342640]
3. Alder, A., Jamil, M., Marzorati, M., Bruno, M., Vermathen, M., Bigler, P., Ghisla, S., Bouwmeester, H., Beyer, P. and Al-Babili, S. The path from β-carotene to carlactone, a strigolactone-like plant hormone. Science 335 (2012) 1348-1351. [PMID: 22422982]
Accepted name: all-trans-10'-apo-β-carotenal 13,14-cleaving dioxygenase
Reaction: all-trans-10'-apo-β-carotenal + O2 = 13-apo-β-carotenone + (2E,4E,6E)-4-methylocta-2,4,6-trienedial
For diagram of reaction click here.
Other name(s): CCD8 (gene name); MAX4 (gene name); NCED8 (gene name); all-trans-10'-apo-β-carotenal:O2 oxidoreductase (13,14-cleaving)
Systematic name: all-trans-10'-apo-β-carotenal:oxygen oxidoreductase (13,14-cleaving)
Comments: Requires Fe2+. The enzyme from the plant Arabidopsis thaliana also catalyses EC 1.13.11.69, carlactone synthase, 10-fold faster.
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References:
1. Schwartz, S.H., Qin, X. and Loewen, M.C. The biochemical characterization of two carotenoid cleavage enzymes from Arabidopsis indicates that a carotenoid-derived compound inhibits lateral branching. J. Biol. Chem. 279 (2004) 46940-46945. [PMID: 15342640]
Accepted name: carotenoid-9',10'-cleaving dioxygenase
Reaction: all-trans-β-carotene + O2 = all-trans-10'-apo-β-carotenal + β-ionone
For diagram of reaction click here.
Other name(s): BCO2 (gene name); β-carotene 9',10'-monooxygenase (misleading); all-trans-β-carotene:O2 oxidoreductase (9',10'-cleaving)
Systematic name: all-trans-β-carotene:oxygen oxidoreductase (9',10'-cleaving)
Comments: Requires Fe2+. The enzyme catalyses the asymmetric oxidative cleavage of carotenoids. The mammalian enzyme can also cleave all-trans-lycopene.
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References:
1. Kiefer, C., Hessel, S., Lampert, J.M., Vogt, K., Lederer, M.O., Breithaupt, D.E. and von Lintig, J. Identification and characterization of a mammalian enzyme catalyzing the asymmetric oxidative cleavage of provitamin A. J. Biol. Chem. 276 (2001) 14110-14116. [PMID: 11278918]
2. Lindqvist, A., He, Y.G. and Andersson, S. Cell type-specific expression of β-carotene 9',10'-monooxygenase in human tissues. J. Histochem. Cytochem. 53 (2005) 1403-1412. [PMID: 15983114]
Accepted name: 2-hydroxyethylphosphonate dioxygenase
Reaction: 2-hydroxyethylphosphonate + O2 = hydroxymethylphosphonate + formate
For diagram of reaction click here.
Other name(s): HEPD; phpD (gene name); 2-hydroxyethylphosphonate:O2 1,2-oxidoreductase (hydroxymethylphosphonate forming)
Systematic name: 2-hydroxyethylphosphonate:oxygen1,2-oxidoreductase (hydroxymethylphosphonate forming)
Comments: Requires non-heme-iron(II). Isolated from some bacteria including Streptomyces hygroscopicus and Streptomyces viridochromogenes. The pro-R hydrogen at C-2 of the ethyl group is retained by the formate ion. Any stereochemistry at C-1 of the ethyl group is lost. One atom from dioxygen is present in each product. Involved in phosphinothricin biosynthesis.
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References:
1. Cicchillo, R.M., Zhang, H., Blodgett, J.A., Whitteck, J.T., Li, G., Nair, S.K., van der Donk, W.A. and Metcalf, W.W. An unusual carbon-carbon bond cleavage reaction during phosphinothricin biosynthesis. Nature 459 (2009) 871-874. [PMID: 19516340]
2. Whitteck, J.T., Malova, P., Peck, S.C., Cicchillo, R.M., Hammerschmidt, F. and van der Donk, W.A. On the stereochemistry of 2-hydroxyethylphosphonate dioxygenase. J. Am. Chem. Soc. 133 (2011) 4236-4239. [PMID: 21381767]
3. Peck, S.C., Cooke, H.A., Cicchillo, R.M., Malova, P., Hammerschmidt, F., Nair, S.K. and van der Donk, W.A. Mechanism and substrate recognition of 2-hydroxyethylphosphonate dioxygenase. Biochemistry 50 (2011) 6598-6605. [PMID: 21711001]
Accepted name: methylphosphonate synthase
Reaction: 2-hydroxyethylphosphonate + O2 = methylphosphonate + HCO3-
For diagram of reaction click here.
Systematic name: 2-hydroxyethylphosphonate:oxygen 1,2-oxidoreductase (methylphosphonate forming)
Comments: Isolated from the marine archaeon Nitrosopumilus maritimus.
Comments: Isolated from the marine archaeon Nitrosopumilus maritimus.
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References:
1. Metcalf, W.W., Griffin, B.M., Cicchillo, R.M., Gao, J., Janga, S.C., Cooke, H.A., Circello, B.T., Evans, B.S., Martens-Habbena, W., Stahl, D.A. and van der Donk, W.A. Synthesis of methylphosphonic acid by marine microbes: a source for methane in the aerobic ocean. Science 337 (2012) 1104-1107. [PMID: 22936780]
Accepted name: 2-aminophenol 1,6-dioxygenase
Reaction: 2-aminophenol + O2 = 2-aminomuconate 6-semialdehyde
Other name(s): amnA (gene name); amnB (gene name); 2-aminophenol:oxygen 1,6-oxidoreductase (decyclizing)
Systematic name: 2-aminophenol:oxygen 1,6-oxidoreductase (ring-opening)
Comments: The enzyme, a member of the nonheme-iron(II)-dependent dioxygenase family, is an extradiol-type dioxygenase that utilizes a non-heme ferrous iron to cleave the aromatic ring at the meta position (relative to the hydroxyl substituent). The enzyme also has some activity with 2-amino-5-methylphenol and 2-amino-4-methylphenol [1]. The enzyme from the bacterium Comamonas testosteroni CNB-1 also has the activity of EC 1.3.1.105, 2-amino-5-chlorophenol 1,6-dioxygenase [2].
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References:
1. Takenaka, S., Murakami, S., Shinke, R., Hatakeyama, K., Yukawa, H. and Aoki, K. Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme. J. Biol. Chem. 272 (1997) 14727-14732. [PMID: 9169437]
2. Wu, J.F., Sun, C.W., Jiang, C.Y., Liu, Z.P. and Liu, S.J. A novel 2-aminophenol 1,6-dioxygenase involved in the degradation of p-chloronitrobenzene by Comamonas strain CNB-1: purification, properties, genetic cloning and expression in Escherichia coli. Arch. Microbiol. 183 (2005) 1-8. [PMID: 15580337]
3. Li, D.F., Zhang, J.Y., Hou, Y., Liu, L., Liu, S.J. and Liu, W. Crystallization and preliminary crystallographic analysis of 2-aminophenol 1,6-dioxygenase complexed with substrate and with an inhibitor. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68 (2012) 1337-1340. [PMID: 23143244]
Accepted name: all-trans-8'-apo-β-carotenal 15,15'-oxygenase
Reaction: all-trans-8'-apo-β-carotenal + O2 = all-trans-retinal + (2E,4E,6E)-2,6-dimethylocta-2,4,6-trienedial
For diagram of reaction click here.
Other name(s): Diox1; ACO; 8'-apo-β-carotenal 15,15'-oxygenase
Systematic name: all-trans-8'-apo-β-carotenal:oxygen 15,15'-oxidoreductase (bond-cleaving)
Comments: Contains an Fe2+-4His arrangement. The enzyme is involved in retinal biosynthesis in bacteria [2].
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References:
1. Ruch, S., Beyer, P., Ernst, H. and Al-Babili, S. Retinal biosynthesis in Eubacteria: in vitro characterization of a novel carotenoid oxygenase from Synechocystis sp. PCC 6803. Mol. Microbiol. 55 (2005) 1015-1024. [PMID: 15686550]
2. Kloer, D.P., Ruch, S., Al-Babili, S., Beyer, P. and Schulz, G.E. The structure of a retinal-forming carotenoid oxygenase. Science 308 (2005) 267-269. [PMID: 15821095]
Accepted name: 2-amino-5-chlorophenol 1,6-dioxygenase
Reaction: 2-amino-5-chlorophenol + O2 = 2-amino-5-chloromuconate 6-semialdehyde
Other name(s): cnbC (gene name); 2-amino-5-chlorophenol:oxygen 1,6-oxidoreductase (decyclizing)
Systematic name: 2-amino-5-chlorophenol:oxygen 1,6-oxidoreductase (ring-opening)
Comments: The enzyme, a member of the nonheme-iron(II)-dependent dioxygenase family, is an extradiol-type dioxygenase that utilizes a non-heme ferrous iron to cleave the aromatic ring at the meta position (relative to the hydroxyl substituent). The enzyme from the bacterium Comamonas testosteroni CNB-1 also has the activity of EC 1.3.11.74, 2-aminophenol 1,6-dioxygenase.
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References:
1. Wu, J.F., Sun, C.W., Jiang, C.Y., Liu, Z.P. and Liu, S.J. A novel 2-aminophenol 1,6-dioxygenase involved in the degradation of p-chloronitrobenzene by Comamonas strain CNB-1: purification, properties, genetic cloning and expression in Escherichia coli. Arch. Microbiol. 183 (2005) 1-8. [PMID: 15580337]
Accepted name: oleate 10S-lipoxygenase
Reaction: (1) oleate + O2 = (8E,10S)-10-hydroperoxyoctadeca-8-enoate
Other name(s): 10S-DOX; (10S)-dioxygenase; 10S-dioxygenase
Systematic name: oleate:oxygen (10S)-oxidoreductase
Comments: Binds Fe2+. The enzyme isolated from the bacterium Pseudomonas sp. 42A2 has similar activity with all the three Δ9 fatty acids. cf. EC 1.13.11.62, linoleate 10R-lipoxygenase.
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References:
1. Busquets, M., Deroncele, V., Vidal-Mas, J., Rodriguez, E., Guerrero, A. and Manresa, A. Isolation and characterization of a lipoxygenase from Pseudomonas 42A2 responsible for the biotransformation of oleic acid into (S)-(E)-10-hydroxy-8-octadecenoic acid. Antonie Van Leeuwenhoek 85 (2004) 129-139. [PMID: 15028873]
Accepted name: 2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming)
Reaction: (2-amino-1-hydroxyethyl)phosphonate + O2 = glycine + phosphate
Other name(s): phnZ (gene name)
Systematic name: 2-amino-1-hydroxyethylphosphonate:oxygen 1-oxidoreductase (glycine-forming)
Comments: Requires Fe2+. The enzyme, characterized from a marine bacterium, is involved in a 2-aminoethylphosphonate degradation pathway.
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References:
1. McSorley, F.R., Wyatt, P.B., Martinez, A., DeLong, E.F., Hove-Jensen, B. and Zechel, D.L. PhnY and PhnZ comprise a new oxidative pathway for enzymatic cleavage of a carbon-phosphorus bond. J. Am. Chem. Soc. 134 (2012) 8364-8367. [PMID: 22564006]
2. Worsdorfer, B., Lingaraju, M., Yennawar, N.H., Boal, A.K., Krebs, C., Bollinger, J.M., Jr. and Pandelia, M.E. Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases. Proc. Natl. Acad. Sci. USA 110 (2013) 18874-18879. [PMID: 24198335]
Accepted name: aerobic 5,6-dimethylbenzimidazole synthase
Reaction: FMNH2 + O2 = 5,6-dimethylbenzimidazole + D-erythrose 4-phosphate + other product(s)
For diagram of reaction click here
Other name(s): BluB; flavin destructase
Systematic name: FMNH2 oxidoreductase (5,6-dimethylbenzimidazole-forming)
Comments: The enzyme catalyses a complex oxygen-dependent conversion of reduced flavin mononucleotide to form 5,6-dimethylbenzimidazole, the lower ligand of vitamin B12. This conversion involves many sequential steps in two distinct stages, and an alloxan intermediate that acts as a proton donor, a proton acceptor, and a hydride acceptor [4]. The C-2 of 5,6-dimethylbenzimidazole is derived from C-1' of the ribityl group of FMNH2 and 2-H from the ribityl 1'-pro-S hydrogen. While D-erythrose 4-phosphate has been shown to be one of the byproducts, the nature of the other product(s) has not been verified yet.
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1. Gray, M.J. and Escalante-Semerena, J.C. Single-enzyme conversion of FMNH2 to 5,6-dimethylbenzimidazole, the lower ligand of B12. Proc. Natl. Acad. Sci. USA 104 (2007) 2921-2926. [PMID: 17301238]
2. Ealick, S.E. and Begley, T.P. Biochemistry: molecular cannibalism. Nature 446 (2007) 387-388. [PMID: 17377573]
3. Taga, M.E., Larsen, N.A., Howard-Jones, A.R., Walsh, C.T. and Walker, G.C. BluB cannibalizes flavin to form the lower ligand of vitamin B12. Nature 446 (2007) 449. [PMID: 17377583]
4. Wang, X.L. and Quan, J.M. Intermediate-assisted multifunctional catalysis in the conversion of flavin to 5,6-dimethylbenzimidazole by BluB: a density functional theory study. J. Am. Chem. Soc. 133 (2011) 4079-4091. [PMID: 21344938]
5. Collins, H.F., Biedendieck, R., Leech, H.K., Gray, M., Escalante-Semerena, J.C., McLean, K.J., Munro, A.W., Rigby, S.E., Warren, M.J. and Lawrence, A.D. Bacillus megaterium has both a functional BluB protein required for DMB synthesis and a related flavoprotein that forms a stable radical species. PLoS One 8 (2013) e55708. [PMID: 23457476]
Accepted name: (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase
Reaction: (3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA
Glossary: (3,5-dihydroxyphenyl)acetyl-CoA = 2-(3,5-dihydroxyphenyl)acetyl-CoA
Other name(s): DpgC
Systematic name: (3,5-dihydroxyphenyl)acetyl-CoA:oxygen oxidoreductase
Comments: The enzyme, characterized from bacteria Streptomyces toyocaensis and Amycolatopsis orientalis, is involved in the biosynthesis of (3,5-dihydroxyphenyl)glycine, a component of the glycopeptide antibiotic vancomycin.
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References:
1. Chen, H., Tseng, C.C., Hubbard, B.K. and Walsh, C.T. Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine. Proc. Natl. Acad. Sci. USA 98 (2001) 14901-14906. [PMID: 11752437]
2. Widboom, P.F., Fielding, E.N., Liu, Y. and Bruner, S.D. Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis. Nature 447 (2007) 342-345. [PMID: 17507985]
3. Fielding, E.N., Widboom, P.F. and Bruner, S.D. Substrate recognition and catalysis by the cofactor-independent dioxygenase DpgC. Biochemistry 46 (2007) 13994-14000. [PMID: 18004875]
Accepted name: 7,8-dihydroneopterin oxygenase
Reaction: 7,8-dihydroneopterin + O2 = 7,8-dihydroxanthopterin + formate + glycolaldehyde
For diagram of reaction click here.
Glossary: 7,8-dihydroneopterin = 2-amino-6-[(1S,2R)-1,2,3-trihydroxypropyl]-7,8-dihydropteridin-4(3H)-one
Systematic name: 7,8-dihydroneopterin:oxygen oxidoreductase
Comments: The enzyme from the bacterium Mycobacterium tuberculosis is multifunctional and also catalyses the epimerisation of the 2'-hydroxy group of 7,8-dihydroneopterin (EC 5.1.99.8, 7,8-dihydroneopterin epimerase) and the reaction of EC 4.1.2.25 (dihydroneopterin aldolase).
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References:
1. Czekster, C.M. and Blanchard, J.S. One substrate, five products: reactions catalyzed by the dihydroneopterin aldolase from Mycobacterium tuberculosis. J. Am. Chem. Soc. 134 (2012) 19758-19771. [PMID: 23150985]
Accepted name: 8'-apo-carotenoid 13,14-cleaving dioxygenase
Reaction: 8'-apo-β-carotenal + O2 = 13-apo-β-carotenone + 2,6-dimethyldeca-2,4,6,8-tetraenedial
For diagram of reaction click here.
Other name(s): NACOX1 (gene name)
Systematic name: 8'-apo-β-carotenal:oxygen 13,14-dioxygenase (bond-cleaving)
Comments: Isolated from the bacterium Novosphingobium aromaticivorans. It is less active with 4'-apo-β-carotenal and γ-carotene.
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References:
1. Kim, Y.S., Seo, E.S. and Oh, D.K. Characterization of an apo-carotenoid 13,14-dioxygenase from Novosphingobium aromaticivorans that converts β-apo-8'-carotenal to β-apo-13-carotenone. Biotechnol. Lett. 34 (2012) 1851-1856. [PMID: 22711425]
Accepted name: 4-hydroxy-3-prenylphenylpyruvate oxygenase
Reaction: 3(4-hydroxy-3-prenylphenyl)pyruvate + O2 = 4-hydroxy-3-prenylmandelate + CO2
For diagram of reaction, click here
Glossary: 3-(4-hydroxy-3-prenylphenyl)pyruvate = 3-(4-hydroxy-3-prenylphenyl)-2-oxopropanoate
Other name(s): CloR
Systematic name: 4-hydroxy-3-prenylphenylpyruvate:oxygen 1,2-oxidoreductase (4-hydroxy-3-prenylmandelate forming)
Comments: Requires non-heme-Fe(II). Isolated from the bacterium Streptomyces roseochromogenes DS 12976. A bifunctional enzyme involved in clorobiocin biosynthesis that also catalyses the activity of EC 1.13.12.23, 4-hydroxy-3-prenylbenzoate synthase.
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References:
1. Pojer, F., Kahlich, R., Kammerer, B., Li, S.M. and Heide, L. CloR, a bifunctional non-heme iron oxygenase involved in clorobiocin biosynthesis. J. Biol. Chem. 278 (2003) 30661-30668. [PMID: 12777382]
Accepted name: crocetin dialdehyde synthase
Reaction: zeaxanthin + 2 O2 = crocetin dialdehyde + 2 3β-hydroxy-β-cyclocitral (overall reaction)
For diagram of reaction click here.
Glossary: crocetin dialdehyde = 8,8'-diapocarotene-8,8'-dial
Other name(s): CCD2; zeaxanthin 7,8-dioxygenase
Systematic name: zeaxanthin:oxygen 7',8'-oxidoreductase (bond-cleaving)
Comments: The enzyme, characterized from the plant Crocus sativus (saffron), acts twice, cleaving 3β-hydroxy-β-cyclocitral off each 3-hydroxy end group. It is part of the zeaxanthin degradation pathway in that plant, leading to the different compounds that impart the color, flavor and aroma of the saffron spice. The enzyme can similarly cleave the 7-8 double bond of other carotenoids with a 3-hydroxy-β-carotenoid end group.
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1. Frusciante, S., Diretto, G., Bruno, M., Ferrante, P., Pietrella, M., Prado-Cabrero, A., Rubio-Moraga, A., Beyer, P., Gomez-Gomez, L., Al-Babili, S. and Giuliano, G. Novel carotenoid cleavage dioxygenase catalyzes the first dedicated step in saffron crocin biosynthesis. Proc. Natl. Acad. Sci. USA 111 (2014) 12246-12251. [PMID: 25097262]
2. Ahrazem, O., Rubio-Moraga, A., Berman, J., Capell, T., Christou, P., Zhu, C. and Gomez-Gomez, L. The carotenoid cleavage dioxygenase CCD2 catalysing the synthesis of crocetin in spring crocuses and saffron is a plastidial enzyme. New Phytol. 209 (2016) 650-663. [PMID: 26377696]
3. Ahrazem, O., Diretto, G., Argandona, J., Rubio-Moraga, A., Julve, J.M., Orzaez, D., Granell, A. and Gomez-Gomez, L. Evolutionarily distinct carotenoid cleavage dioxygenases are responsible for crocetin production in Buddleja davidii. J. Exp. Bot. 68 (2017) 4663-4677. [PMID: 28981773]
Accepted name: exo-cleaving rubber dioxygenase
Reaction: cis-1,4-polyisoprene + n O2 = n (4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal
For diagram of reaction click here.
Other name(s): roxA (gene name); heme-dependent rubber oxygenase (ambiguous)
Systematic name: cis-1,4-polyisoprene:oxygen dioxygenase [(4Z,8Z)-4,8-dimethyl-12-oxotrideca-4,8-dienal-forming]
Comments: The enzyme, studied mainly from the bacterium Xanthomonas sp. 35Y, catalyses the cleavage of the double bonds in natural and synthetic rubber (cis-1,4-polyisoprene polymers), generating ends that contain ketone and aldehyde groups. The enzyme from Xanthomonas sp. 35Y contains two c-type cytochromes. It attacks the substrate from its end, producing a single product of 15 carbons.
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1. Tsuchii, A. and Takeda, K. Rubber-degrading enzyme from a bacterial culture. Appl. Environ. Microbiol. 56 (1990) 269-274. [PMID: 16348100]
2. Jendrossek, D. and Reinhardt, S. Sequence analysis of a gene product synthesized by Xanthomonas sp. during growth on natural rubber latex. FEMS Microbiol. Lett. 224 (2003) 61-65. [PMID: 12855168]
3. Braaz, R., Fischer, P. and Jendrossek, D. Novel type of heme-dependent oxygenase catalyzes oxidative cleavage of rubber (poly-cis-1,4-isoprene). Appl. Environ. Microbiol. 70 (2004) 7388-7395. [PMID: 15574940]
4. Braaz, R., Armbruster, W. and Jendrossek, D. Heme-dependent rubber oxygenase RoxA of Xanthomonas sp. cleaves the carbon backbone of poly(cis-1,4-Isoprene) by a dioxygenase mechanism. Appl. Environ. Microbiol. 71 (2005) 2473-2478. [PMID: 15870336]
5. Seidel, J., Schmitt, G., Hoffmann, M., Jendrossek, D. and Einsle, O. Structure of the processive rubber oxygenase RoxA from Xanthomonas sp. Proc. Natl Acad. Sci. USA 110 (2013) 13833-13838. [PMID: 23922395]
6. Birke, J. and Jendrossek, D. Rubber oxygenase and latex clearing protein cleave rubber to different products and use different cleavage mechanisms. Appl. Environ. Microbiol. 80 (2014) 5012-5020. [PMID: 24907333]
Accepted name: 5-aminosalicylate 1,2-dioxygenase
Reaction: 5-aminosalicylate + O2 = (2Z,4E)-4-amino-6-oxohepta-2,4-dienedioate
Glossary: 5-aminosalicylate = 5-amino-2-hydroxybenzoate
Other name(s): mabB (gene name)
Systematic name: 5-aminosalicylate:oxygen 1,2-oxidoreductase (ring-opening)
Comments: Requires iron(II). The enzyme, characterized from different bacteria, is a nonheme iron dioxygenase in the bicupin family.
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References:
1. Stolz, A., Nortemann, B. and Knackmuss, H.J. Bacterial metabolism of 5-aminosalicylic acid. Initial ring cleavage. Biochem. J. 282 (1992) 675-680. [PMID: 1554350]
2. Yu, H., Zhao, S. and Guo, L. Novel gene encoding 5-aminosalicylate 1,2-dioxygenase from Comamonas sp. strain QT12 and catalytic properties of the purified enzyme. J. Bacteriol. 200 (2018) . [PMID: 29038259]
Accepted name: endo-cleaving rubber dioxygenase
Reaction: Cleavage of cis-1,4-polyisoprene polymers into a mixture of compounds, including a C20 compound ((4Z,8Z,12Z,16Z,20Z,24Z)-4,8,12,16,20,24-hexamethyl-28-oxononacosa-4,8,12,16,20,24-hexaenal), a C25 compound ((4Z,8Z,12Z,16Z,20Z)-4,8,12,16,20-pentamethyl-24-oxopentacosa-4,8,12,16,20-pentaenal), a C30 compound ((4Z,8Z,12Z,16Z)-4,8,12,16-tetramethyl-20-oxohenicosa-4,8,12,16-tetraenal), and larger isoprenologes such as C35, C40, C45, and higher analogues.
For diagram of reaction click here.
Other name(s): latex clearing protein; lcp (gene name); roxB (gene name)
Systematic name: cis-1,4-polyisoprene:oxygen dioxygenase (endo-cleaving)
Comments: The enzyme catalyses the cleavage of the double bonds in natural and synthetic rubber, producing a mixture of C20, C25, C30, and higher oligo-isoprenoids with ketone and aldehyde groups at their ends. Two unrelated bacterial enzymes are known to possess this activity - the enzyme from Streptomyces sp. K30 (Lcp) contains a b-type cytochrome, while the enzyme from Xanthomonas sp. 35Y, (RoxB) contains two c-type cytochromes. Both enzymes attack the substrate at random locations, and are not able to cleave the C35 or smaller products into shorter fragments.
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References:
1. Tsuchii, A. and Takeda, K. Rubber-degrading enzyme from a bacterial culture. Appl. Environ. Microbiol. 56 (1990) 269-274. [PMID: 16348100]
2. Jendrossek, D. and Reinhardt, S. Sequence analysis of a gene product synthesized by Xanthomonas sp. during growth on natural rubber latex. FEMS Microbiol. Lett. 224 (2003) 61-65. [PMID: 12855168]
3. Braaz, R., Fischer, P. and Jendrossek, D. Novel type of heme-dependent oxygenase catalyzes oxidative cleavage of rubber (poly-cis-1,4-isoprene). Appl. Environ. Microbiol. 70 (2004) 7388-7395. [PMID: 15574940]
4. Braaz, R., Armbruster, W. and Jendrossek, D. Heme-dependent rubber oxygenase RoxA of Xanthomonas sp. cleaves the carbon backbone of poly(cis-1,4-Isoprene) by a dioxygenase mechanism. Appl. Environ. Microbiol. 71 (2005) 2473-2478. [PMID: 15870336]
5. Seidel, J., Schmitt, G., Hoffmann, M., Jendrossek, D. and Einsle, O. Structure of the processive rubber oxygenase RoxA from Xanthomonas sp. Proc. Natl Acad. Sci. USA 110 (2013) 13833-13838. [PMID: 23922395]
6. Birke, J. and Jendrossek, D. Rubber oxygenase and latex clearing protein cleave rubber to different products and use different cleavage mechanisms. Appl. Environ. Microbiol. 80 (2014) 5012-5020. [PMID: 24907333]
7. Birke, J., Röther, W. and Jendrossek, D. RoxB is a novel type of rubber oxygenase that combines properties of rubber oxygenase RoxA and latex clearing protein (Lcp). Appl. Environ. Microbiol. 83 (2017) e00721-17. [PMID: 28500046]
Accepted name: isoeugenol monooxygenase
Reaction: isoeugenol + O2 = vanillin + acetaldehyde
For diagram of reaction click here.
Glossary: isoeugenol = 2-methoxy-4-(prop-1-en-1-yl)phenol
Other name(s): iem (gene name)
Systematic name: isoeugenol:oxygen 7,8-oxidoreductase (bond-cleaving)
Comments: Contains iron(II). The enzyme, charcterised from the bacteria Pseudomonas putida and Pseudomonas nitroreducens, catalyses the epoxidation of the double bond in the side chain of isoeugenol, followed by a second oxygenation and cleavage of the side chain in the form of acetaldehyde.
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References:
1. Shimoni, E., Ravid, U. and Shoham, Y. Isolation of a Bacillus sp. capable of transforming isoeugenol to vanillin. J. Biotechnol. 78 (2000) 1-9. [PMID: 10702906]
2. Yamada, M., Okada, Y., Yoshida, T. and Nagasawa, T. Biotransformation of isoeugenol to vanillin by Pseudomonas putida IE27 cells. Appl. Microbiol. Biotechnol. 73 (2007) 1025-1030. [PMID: 16944125]
3. Yamada, M., Okada, Y., Yoshida, T. and Nagasawa, T. Purification, characterization and gene cloning of isoeugenol-degrading enzyme from Pseudomonas putida IE27. Arch. Microbiol. 187 (2007) 511-517. [PMID: 17516050]
4. Ryu, J.Y., Seo, J., Unno, T., Ahn, J.H., Yan, T., Sadowsky, M.J. and Hur, H.G. Isoeugenol monooxygenase and its putative regulatory gene are located in the eugenol metabolic gene cluster in Pseudomonas nitroreducens Jin1. Arch. Microbiol. 192 (2010) 201-209. [PMID: 20091296]
5. Ryu, J.Y., Seo, J., Park, S., Ahn, J.H., Chong, Y., Sadowsky, M.J. and Hur, H.G. Characterization of an isoeugenol monooxygenase (iem) from Pseudomonas nitroreducens Jin1 that transforms isoeugenol to vanillin. Biosci. Biotechnol. Biochem. 77 (2013) 289-294. [PMID: 23391906]
Accepted name: hydroxymethylphosphonate dioxygenase
Reaction: (hydroxymethyl)phosphonate + O2 = formate + phosphate
Other name(s): phnZ1 (gene name)
Systematic name: hydroxymethylphosphonate:oxygen 1-oxidoreductase (formate-forming)
Comments: Requires iron(II). The enzyme, characterized from the marine bacterium Gimesia maris, participates in a methylphosphonate degradation pathway. It also has the activity of EC 1.13.11.78, (2-amino-1-hydroxyethyl)phosphonate dioxygenase (glycine-forming).
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EXPASY,
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References:
1. Gama, S.R., Vogt, M., Kalina, T., Hupp, K., Hammerschmidt, F., Pallitsch, K. and Zechel, D.L. An oxidative pathway for microbial utilization of methylphosphonic acid as a phosphate source. ACS Chem. Biol. 14 (2019) 735-741. [PMID: 30810303]
Accepted name: [1-hydroxy-2-(trimethylamino)ethyl]phosphonate dioxygenase (glycine-betaine-forming)
Reaction: [(1R)-1-hydroxy-2-(trimethylamino)ethyl]phosphonate + O2 = glycine betaine + phosphate
Other name(s): tmpB (gene name)
Systematic name: [(1R)-1-hydroxy-2-(trimethylamino)ethyl]phosphonate:oxygen 1R-oxidoreductase (glycine-betaine-forming)
Comments: Requires Fe2+. This bacterial enzyme is involved in a degradation pathway for [2-(trimethylamino)ethyl]phosphonate.
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EXPASY,
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Metacyc,
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References:
1. Rajakovich, L.J., Pandelia, M.E., Mitchell, A.J., Chang, W.C., Zhang, B., Boal, A.K., Krebs, C. and Bollinger, J.M., Jr. A new microbial pathway for organophosphonate degradation catalyzed by two previously misannotated non-heme-iron oxygenases. Biochemistry 58 (2019) 1627-1647. [PMID: 30789718]
Accepted name: 3-mercaptopropionate dioxygenase
Reaction: 3-sulfanylpropanoate + O2 = 3-sulfinopropanoate
Other name(s): mdo (gene name); 3-mercaptopropionic acid dioxygenase; 3-sulfanylpropanoate dioxygenase
Systematic name: 3-sulfanylpropanoate:oxygen oxidoreductase
Comments: This bacterial enzyme contains an iron(2+) atom coordinated by three protein-derived histidines and a Ser-His-Tyr motif. It is similar to EC 1.13.11.20, cysteine dioxygenase, and can act on L-cysteine, but has a much higher activity with its native substrate, 3-sulfanylpropanoate.
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BRENDA,
EXPASY,
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References:
1. Bruland, N., Wubbeler, J.H. and Steinbuchel, A. 3-Mercaptopropionate dioxygenase, a cysteine dioxygenase homologue, catalyzes the initial step of 3-mercaptopropionate catabolism in the 3,3-thiodipropionic acid-degrading bacterium Variovorax paradoxus. J. Biol. Chem. 284 (2009) 660-672. [PMID: 19001372]
2. Driggers, C.M., Hartman, S.J. and Karplus, P.A. Structures of Arg- and Gln-type bacterial cysteine dioxygenase homologs. Protein Sci. 24 (2015) 154-161. [PMID: 25307852]
3. Pierce, B.S., Subedi, B.P., Sardar, S. and Crowell, J.K. The ’Gln-type’ thiol dioxygenase from Azotobacter vinelandii is a 3-mercaptopropionic acid dioxygenase. Biochemistry 54 (2015) 7477-7490. [PMID: 26624219]
4. Tchesnokov, E.P., Fellner, M., Siakkou, E., Kleffmann, T., Martin, L.W., Aloi, S., Lamont, I.L., Wilbanks, S.M. and Jameson, G.N. The cysteine dioxygenase homologue from Pseudomonas aeruginosa is a 3-mercaptopropionate dioxygenase. J. Biol. Chem. 290 (2015) 24424-24437. [PMID: 26272617]
5. Fellner, M., Aloi, S., Tchesnokov, E.P., Wilbanks, S.M. and Jameson, G.N. Substrate and pH-dependent kinetic profile of 3-mercaptopropionate dioxygenase from Pseudomonas aeruginosa. Biochemistry 55 (2016) 1362-1371. [PMID: 26878277]
6. Crowell, J.K., Sardar, S., Hossain, M.S., Foss, F.W., Jr. and Pierce, B.S. Non-chemical proton-dependent steps prior to O2-activation limit Azotobacter vinelandii 3-mercaptopropionic acid dioxygenase (MDO) catalysis. Arch. Biochem. Biophys. 604 (2016) 86-94. [PMID: 27311613]
7. Aloi, S., Davies, C.G., Karplus, P.A., Wilbanks, S.M. and Jameson, G.NL. Substrate specificity in thiol dioxygenases. Biochemistry 58 (2019) 2398-2407. [PMID: 31045343]
8. Sardar, S., Weitz, A., Hendrich, M.P. and Pierce, B.S. Outer-sphere tyrosine 159 within the 3-mercaptopropionic acid dioxygenase S-H-Y motif gates substrate-coordination denticity at the non-heme iron active site. Biochemistry 58 (2019) 5135-5150. [PMID: 31750652]
Accepted name: fatty acid α-dioxygenase
Reaction: a fatty acid + O2 = a (2R)-2-hydroperoxyfatty acid
Other name(s): DOX1 (gene name)
Systematic name: fatty acid:oxygen 2-oxidoreductase [(2R)-2-hydroperoxyfatty acid-forming]
Comments: Contains heme. This plant enzyme catalyses the (2R)-hydroperoxidation of fatty acids. It differs from lipoxygenases and cyclooxygenases in that the oxygen addition does not target an unsaturated region in the fatty acid. In vitro the product undergoes spontaneous decarboxylation, resulting in formation of a chain-shortened aldehyde. In vivo the product may be reduced to a (2R)-2-hydroxyfatty acid. The enzyme, which is involved in responses to different abiotic and biotic stresses, has a wide substrate range that includes both saturated and unsaturated fatty acids.
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EXPASY,
KEGG,
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CAS registry number:
References:
1. Akakabe, Y., Matsui, K., and Kajiwara, T. Enantioselective α-hydroperoxylation of long-chain fatty acids with crude enzyme of marine green alga Ulva pertusa. Tetrahedron Lett. 40 (1999) 1137-1140.
2. Hamberg, M., Sanz, A. and Castresana, C. α-oxidation of fatty acids in higher plants. Identification of a pathogen-inducible oxygenase (piox) as an α-dioxygenase and biosynthesis of 2-hydroperoxylinolenic acid. J. Biol. Chem. 274 (1999) 24503-24513. [PMID: 10455113]
3. Saffert, A., Hartmann-Schreier, J., Schon, A. and Schreier, P. A dual function α-dioxygenase-peroxidase and NAD(+) oxidoreductase active enzyme from germinating pea rationalizing α-oxidation of fatty acids in plants. Plant Physiol. 123 (2000) 1545-1552. [PMID: 10938370]
4. Koeduka, T., Matsui, K., Akakabe, Y. and Kajiwara, T. Catalytic properties of rice α-oxygenase. A comparison with mammalian prostaglandin H synthases. J. Biol. Chem. 277 (2002) 22648-22655. [PMID: 11909851]
5. Liu, W., Rogge, C.E., Bambai, B., Palmer, G., Tsai, A.L. and Kulmacz, R.J. Characterization of the heme environment in Arabidopsis thaliana fatty acid α-dioxygenase-1. J. Biol. Chem. 279 (2004) 29805-29815. [PMID: 15100225]
6. Meisner, A.K., Saffert, A., Schreier, P. and Schon, A. Fatty acid α-dioxygenase from Pisum sativum: temporal and spatial regulation during germination and plant development. J. Plant Physiol. 166 (2009) 333-343. [PMID: 18760499]
Accepted name: 2-oxoadipate dioxygenase/decarboxylase
Reaction: 2-oxoadipate + O2 = (R)-2-hydroxyglutarate + CO2
Other name(s): ydcJ (gene name)
Systematic name: 2-oxoadipate dioxygenase/carboxy lyase
Comments: The enzyme, characterized from the bacterium Pseudomonas putida, is involved in an L-lysine catabolic pathway. Contains Fe(II).
Links to other databases:
BRENDA,
EXPASY,
KEGG,
MetaCyc,
CAS registry number:
References:
1. Thompson, M.G., Blake-Hedges, J.M., Cruz-Morales, P., Barajas, J.F., Curran, S.C., Eiben, C.B., Harris, N.C., Benites, V.T., Gin, J.W., Sharpless, W.A., Twigg, F.F., Skyrud, W., Krishna, R.N., Pereira, J.H., Baidoo, E.EK., Petzold, C.J., Adams, P.D., Arkin, A.P., Deutschbauer, A.M. and Keasling, J.D. Massively parallel fitness profiling reveals multiple novel enzymes in Pseudomonas putida lysine metabolism. mBio 10 (2019) . [PMID: 31064836]
arachidonate: (all-Z)-icosa-5,8,11,14-tetraenoate
linoleate: (9Z,12Z)-octadeca-9,12-dienoate
α-linolenate: (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
γ-linolenate: (6Z,9Z,12Z)-octadeca-6,9,12-trienoate
oleate: (Z)-octadec-9-enoate
α-linolenate = (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
(1a) 5-nitrosalicylate + O2 = 4-nitro-6-oxohepta-2,4-dienedioate
(1b) 4-nitro-6-oxohepta-2,4-dienedioate = 2-oxo-3-(5-oxofuran-2-ylidene)propanoate + nitrite (spontaneous)
(2E,4Z)-4-hydroxy-6-oxohexa-2,4-dienoate = 4-hydroxymuconic semialdehyde
(2) linoleate + O2 = (8E,10S,12Z)-10-hydroperoxyoctadeca-8,12-dienoate
(3) α-linolenate + O2 = (8E,10S,12Z,15Z)-10-hydroperoxyoctadeca-8,12,15-trienoate
7,8-dihydroxanthopterin = 2-amino-3,5,7,8-tetrahydropteridin-4,6-dione
4-hydroxy-3-prenylmandelate = 2-hydroxy-2-(4-hydroxy-3-prenylphenyl)acetate
prenyl = 3-methylbut-2-en-1-yl
(1a) zeaxanthin + O2 = 3β-hydroxy-8'-apo-β-carotenal + 3β-hydroxy-β-cyclocitral
(1b) 3β-hydroxy-8'-apo-β-carotenal + O2 = crocetin dialdehyde + 3β-hydroxy-β-cyclocitral
zeaxanthin = (3R,3'R)-β,β-carotene-3,3'-diol
3β-hydroxy-β-cyclocitral = (4R)-4-hydroxy-2,6,6-trimethylcyclohex-1-en-1-carboxaldehyde
Continued with EC 1.13.12 to EC 1.14.11
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