An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.
Common name: UDP-N-acetylmuramate dehydrogenase
Reaction: UDP-N-acetylmuramate + NADP+ = UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + NADPH + H+
For diagram click here.
Other name(s): MurB reductase; UDP-N-acetylenolpyruvoylglucosamine reductase; UDP-N-acetylglucosamine-enoylpyruvate reductase; UDP-GlcNAc-enoylpyruvate reductase; uridine diphosphoacetylpyruvoylglucosamine reductase; uridine diphospho-N-acetylglucosamine-enolpyruvate reductase; uridine-5'-diphospho-N-acetyl-2-amino-2-deoxy-3-O-lactylglucose:NADP-oxidoreductase
Systematic name: UDP-N-acetylmuramate:NADP+ oxidoreductase
Comments: A flavoprotein (FAD). Sodium dithionite, sodium borohydride and, to a lesser extent, NADH, can replace NADPH.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 39307-28-3
References:
1. Taku, A. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. IV. Activation of uridine diphospho-N-acetylenolpyruvylglucosamine reductase by monovalent cations. J. Biol. Chem. 248 (1973) 4971-1976. [PMID: 4717533]
2. Taku, A., Gunetileke, K.G. and Anwar, R.A. Biosynthesis of uridine diphospho-N-acetylmuramic acid. 3. Purification and properties of uridine diphospho-N-acetylenolpyruvyl-glucosamine reductase. J. Biol. Chem. 245 (1970) 5012-5016. [Medline UI: 4394163]
3. van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18 (2001) 503-519. [PMID: 11699883]
Common name: dTDP-galactose 6-dehydrogenase
Reaction: dTDP-D-galactose + 2 NADP+ + H2O = dTDP-D-galacturonate + 2 NADPH + 2 H+
Other name(s): thymidine-diphosphate-galactose dehydrogenase
Systematic name: dTDP-D-galactose:NADP+ 6-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Katan, R. and Avigad, G. NADP dependent oxidation of TDP-glucose by an enzyme system from sugar beets. Biochem. Biophys. Res. Commun. 24 (1966) 18-24. [PMID: 4381717]
Common name: vellosimine dehydrogenase
Reaction: 10-deoxysarpagine + NADP+ = vellosimine + NADPH + H+
For diagram click here.
Systematic name: 10-deoxysarpagine:NADP+ oxidoreductase
Comments: Also acts on related alkaloids with an endo-aldehyde group as vellosimine (same stereochemistry at C-16) but only slight activity with exo-aldehydes. Detected in many cell suspension cultures of plants from the family Apocynaceae.
References:
1. Pfitzner, A., Krausch, B. and Stöckigt, J. Characteristics of vellosimine reductase, a specific enzyme involved in the biosynthesis of the Rauwolfia alkaloid sarpagine. Tetrahedron 40 (1984) 1691-1699.
Common name: 2,5-didehydrogluconate reductase
Reaction: 2-dehydro-D-gluconate + NADP+ = 2,5-didehydro-D-gluconate + NADPH + H+
Other name(s): 2,5-diketo-D-gluconate reductase; YqhE reductase
Systematic name: 2-dehydro-D-gluconate:NADP+ 2-oxidoreductase
Comments: This is a key enzyme in the microbial production of ascorbate. Can also reduce ethyl 2-methylacetoacetate stereoselectively to ethyl (2R)-methyl-(3S)-hydroxybutanoate and can also accept some other β-keto esters. The identification of a bacterial β-keto ester reductase as a 2,5-didehydrogluconate reductase links two previously separate areas of biocatalysis, i.e., asymmetric carbonyl reduction and microbial vitamin C production.
References:
1. Yum, D.Y., Lee, B.Y. and Pan, J.G. Identification of the yqhE and yafB genes encoding two 2,5-diketo-D-gluconate reductases in Escherichia coli. Appl. Environ. Microbiol. 65 (1999) 3341-3346. [PMID: 10427017]
2. Yum, D.Y., Lee, B.Y., Hahm, D.H. and Pan, J.G. The yiaE gene, located at 80.1 minutes on the Escherichia coli chromosome, encodes a 2-ketoaldonate reductase. J. Bacteriol. 180 (1998) 5984-5988. [PMID: 9811658]
3. Habrych, M., Rodriguez, S. and Stewart, J.D. Purification and identification of an Escherichia coli β-keto ester reductase as 2,5-diketo-D-gluconate reductase YqhE. Biotechnol. Prog. 18 (2002) 257-261. [PMID: 11934293]
[EC 1.1.3.26 Transferred entry: now EC 1.21.3.2, columbamine oxidase (EC 1.1.3.26 created 1989, deleted 2002)]
[EC 1.1.3.32 Transferred entry: now EC 1.14.21.1, (S)-stylopine synthase (EC 1.1.3.32 created 1999, deleted 2002)]
[EC 1.1.3.33 Transferred entry: now EC 1.14.21.2, (S)-cheilanthifoline synthase (EC 1.1.3.33 created 1999, deleted 2002)]
[EC 1.1.3.34 Transferred entry: now EC 1.14.21.3, berbamunine synthase (EC 1.1.3.34 created 1999, deleted 2002)]
[EC 1.1.3.35 Transferred entry: now EC 1.14.21.4, salutaridine synthase (EC 1.1.3.35 created 1999, deleted 2002)]
[EC 1.1.3.36 Transferred entry: now EC 1.14.21.5, (S)-canadine synthase (EC 1.1.3.36 created 1999, deleted 2002)]
Common name: xylitol oxidase
Reaction: xylitol + O2 = xylose + H2O2
Systematic name: xylitol:oxygen oxidoreductase
Comments: The enzyme from Streptomyces sp. IKD472 is a monomeric oxidase containing one molecule of FAD per molecule of protein. The enzyme also oxidizes D-sorbitol.
References:
1. Yamashita, M., Omura, H., Okamoto, E., Furuya, Y., Yabuuchi, M., Fukahi, K. and Murooka, Y. Isolation, characterization, and molecular cloning of a thermostable xylitol oxidase from Streptomyces sp. IKD472. J. Biosci. Bioeng. 89 (2000) 350-360.
[EC 1.1.5.1 Deleted entry: cellobiose dehydrogenase (quinone). Now known to be proteolytic product of EC 1.1.99.18, cellobiose dehydrogenase (acceptor). (EC 1.1.5.1 created 1983, deleted 2002)]
Common name: cellobiose dehydrogenase (acceptor)
Reaction: cellobiose + acceptor = cellobiono-1,5-lactone + reduced acceptor
Other name(s): cellobiose dehydrogenase
Systematic name: cellobiose:(acceptor) 1-oxidoreductase
Comments: 2,6-Dichloroindophenol can act as acceptor. Also acts, more slowly, on cello-oligosaccharides, lactose and D-glucosyl-1,4-β-D-mannose. Includes EC 1.1.5.1, cellobiose dehydrogenase (quinone), which is now known to be a proteolytic product of this enzyme.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 54576-85-1
References:
1. Coudray, M.-R., Canebascini, G. and Meier, H. Characterization of a cellobiose dehydrogenase in the cellulolytic fungus porotrichum (Chrysosporium) thermophile. Biochem. J. 203 (1982) 277-284. [PMID: 7103940]
2. Dekker, R.F.H. Induction and characterization of a cellobiose dehydrogenase produced by a species of Monilia. J. Gen. Microbiol. 120 (1980) 309-316.
3. Dekker, R.F.H. Cellobiose dehydrogenase produced by Monilia sp. Methods Enzymol. 160 (1988) 454-463.
4. Habu, N., Samejima, M., Dean, J.F. and Eriksson, K.E. Release of the FAD domain from cellobiose oxidase by proteases from cellulolytic cultures of Phanerochaete chrysosporium. FEBS Lett. 327 (1993) 161-164.
5. Baminger, U. Subramaniam, S.S., Renganathan, V. and Haltrich, D. Purification and characterization of cellobiose dehydrogenase from the plant pathogen Sclerotium (Athelia) rolfsii. Appl. Environ. Microbiol. 67 (2001) 1766-1774. [PMID: 11282631]
6. Hallberg, B.M., Henriksson, G., Pettersson, G. and Divne, C. Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase. J. Mol. Biol. 315 (2002) 421-434. [PMID: 11786022]
Common name: formaldehyde dehydrogenase (glutathione)
Reaction: formaldehyde + glutathione + NAD+ = S-formylglutathione + NADH + H+
Other name(s): NAD-linked formaldehyde dehydrogenase; formaldehyde dehydrogenase; formic dehydrogenase
Systematic name: formaldehyde:NAD+ oxidoreductase (glutathione-formylating)
Comments: Some 2-oxoaldehydes are also oxidized. In the reverse direction, NADPH can replace NADH. Also specifically reduces S-nitrosylglutathione.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, UM-BBD, WIT, CAS registry number: 9028-84-6
References:
1. Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 203-221.
2. Rose, Z.B. and Racker, E. Formaldehyde dehydrogenase. Methods Enzymol. 9 (1966) 357-360.
3. Liu, L., Hausladen, A., Zeng, M., Que, L., Heitman, J. and Stamler, J.S. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410 (2001) 490-494. [PMID: 11260719]
Common name: δ24(241)-sterol reductase
Reaction: ergosterol + NADP+ = ergosta-5,7,22,24(241)-tetraen-3β-ol + NADPH + H+
For diagram click here.
Other names: sterol δ24(28)-methylene reductase; sterol δ24(28)-reductase
Systematic name: ergosterol:NADP+ δ24(241)-oxidoreductase
Comments: Acts on a range of steroids with a 24(241)-double bond.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Neal, W.D. and Parks, L.W. Sterol 24(28) methylene reductase in Saccharomyces cerevisiae. J. Bacteriol. 129 (1977) 1375-1378. [PMID: 14922]
2. Zweytick, D., Hrastnik, C., Kohlwein. S.D. and Daum, G. Biochemical characterization and subcellular localization of the sterol C-24(28) reductase, erg4p, from the yeast Saccharomyces cerevisiae. FEBS Lett. 470 (2000) 83-87. [PMID: 10722850]
Common name: 1,2-dihydrovomilenine reductase
Reaction: 17-O-acetylnorajmaline + NADP+ = 1,2-dihydrovomilenine + NADPH + H+
For diagram click here.
Systematic name: 17-O-acetylnorajmaline:NADP+ oxidoreductase
Comments: Forms part of the ajmaline biosynthesis pathway.
References:
1. Gao, S., von Schumann, G. and Stöckigt, J. A newly-detected reductase from Rauvolfia closes a gap in the biosynthesis of the antiarrhythmic alkaloid ajmaline. Planta Med. 68 (2002) 906-911. [PMID: 12391554 ]
Common name: secologanin synthase
Reaction: loganin + NADPH + H+ + O2 = secologanin + NADP+ + 2 H2O
For diagram click here.
Systematic name: loganin:oxygen oxidoreductase (ring cleaving)
Comments: A heme-thiolate protein (P-450). Secologanin is the precursor of the monoterpenoid indole alkaloids and ipecac alkaloids.
References:
1. Yamamoto, H., Katano, N., Ooi, A. and Inoue, K. Secologanin synthase which catalyzes the oxidative cleavage of loganin into secologanin is a cytochrome P-450. Phytochemistry 53 (2000) 7-12. [PMID: 10656401]
2. Irmler, S., Schroder, G., St-Pierre, B., Crouch, N.P., Hotze, M., Schmidt, J., Strack, D., Matern, U. and Schroder, J. Indole alkaloid biosynthesis in Catharanthus roseus: new enzyme activities and identification of cytochrome P-450 CYP72A1 as secologanin synthase. Plant J. 24 (2000) 797-804. [PMID: 11135113]
3. Yamamoto, H., Katano, N., Ooi, Y. and Inoue, K. Transformation of loganin and 7-deoxyloganin into secologanin by Lonicera japonica cell suspension cultures Phytochemistry 50 (1999) 417-422.
Common name: 15,16-dihydrobiliverdin:ferredoxin oxidoreductase
Reaction: 15,16-dihydrobiliverdin + oxidized ferredoxin = biliverdin IXα + reduced ferredoxin
For diagram click here.
Other name(s): PebA
Systematic name: 15,16-dihydrobiliverdin:ferredoxin oxidoreductase
Comments: Catalyses the two-electron reduction of biliverdin IXα at the C15 methine bridge. It has been proposed that this enzyme and EC 1.3.7.3, phycoerythrobilin:ferredoxin oxidoreductase, function as a dual enzyme complex in the conversion of biliverdin IXα into phycoerythrobilin.
References:
1. Frankenberg, N., Mukougawa, K., Kohchi, T. and Lagarias, J.C. Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms. Plant Cell 13 (2001) 965-978. [PMID: 11283349]
Common name: phycoerythrobilin:ferredoxin oxidoreductase
Reaction: (3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + reduced ferredoxin
For diagram click here.
Other name(s): PebB
Systematic name: (3Z)-phycoerythrobilin:ferredoxin oxidoreductase
Comments: Catalyses the two-electron reduction of the C2 and C31 diene system of 15,16-dihydrobiliverdin. Specific for 15,16-dihydrobiliverdin. It has been proposed that this enzyme and EC 1.3.7.2, 15,16-dihydrobiliverdin:ferredoxin oxidoreductase, function as a dual enzyme complex in the conversion of biliverdin IXα to phycoerythrobilin.
References:
1. Frankenberg, N., Mukougawa, K., Kohchi, T. and Lagarias, J.C. Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms. Plant Cell 13 (2001) 965-978. [PMID: 11283349]
Common name: phytochromobilin:ferredoxin oxidoreductase
Reaction: (3Z)-phytochromobilin + oxidized ferredoxin = biliverdin IXα + reduced ferredoxin
For diagram click here.
Other name(s): HY2; PΦB synthase; phytochromobilin synthase
Systematic name: (3Z)-phytochromobilin:ferredoxin oxidoreductase
Comments: Catalyses the two-electron reduction of biliverdin IXα. Can use 2Fe-2S ferredoxins from a number of sources as acceptor but not the 4Fe-4S ferredoxin from Clostridium pasteurianum. The isomerization of (3Z)-phytochromobilin to (3E)-phytochromobilin is thought to occur prior to covalent attachment to apophytochrome in the plant cell cytoplasm. Flavodoxins can be used instead of ferredoxin.
References:
1. Frankenberg, N., Mukougawa, K., Kohchi, T. and Lagarias, J.C. Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms. Plant Cell 13 (2001) 965-978. [PMID: 11283349]
2. McDowell, M.T. and Lagarias, J.C. Purification and biochemical properties of phytochromobilin synthase from etiolated oat seedlings. Plant Physiol. 126 (2001) 1546-1554. [PMID: 11500553]
3. Terry, M.J., Wahleithner, J.A. and Lagarias, J.C. Biosynthesis of the plant photoreceptor phytochrome. Arch. Biochem. Biophys. 306 (1993) 1-15. [PMID: 8215388]
Common name: phycocyanobilin:ferredoxin oxidoreductase
Reaction: (3Z)-phycocyanobilin + oxidized ferredoxin = biliverdin IXα + reduced ferredoxin
For diagram click here.
Systematic name: (3Z)-phycocyanobilin:ferredoxin oxidoreductase
Comments: Catalyses the four-electron reduction of biliverdin IXα (2-electron reduction at both the A and D rings). Reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin. Flavodoxins can be used instead of ferredoxin.The direct conversion of biliverdin IXα (BV) to (3Z)-phycocyanolbilin (PCB) in the cyanobacteria Synechocystis sp PCC 6803, Anabaena sp PCC7120 and Nostoc punctiforme is in contrast to the proposed pathways of PCB biosynthesis in the red alga Cyanidium caldarium, which involves (3Z)-phycoerythrobilin (PEB) as an intermediate [2] and in the green alga Mesotaenium caldariorum, in which PCB is an isolable intermediate.
References:
1. Frankenberg, N., Mukougawa, K., Kohchi, T. and Lagarias, J.C. Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms. Plant Cell 13 (2001) 965-978. [PMID: 11283349]
2. Beale, SI.I. Biosynthesis of phycobilins. Chem. Rev. 93 (1993) 785-802.
3. Wu. S.-H., McDowell, M.T. and Lagarias, J.C. Phycocyanobilin is the natural chromophore precursor of phytochrome from the green alga Mesotaenium caldariorum. J. Biol. Chem. 272 (1997) 25700-25705. [PMID: 9325294]
[EC 1.3.99.9 Transferred entry: now EC 1.21.99.1, β-cyclopiazonate dehydrogenase (EC 1.3.99.9 created 1976, deleted 2002)]
Common name: glycine oxidase
Reaction: (1) glycine + H2O + O2 = glyoxylate + NH3 + H2O2
(2) D-alanine + H2O + O2 = pyruvate + NH3 + H2O2
(3) sarcosine + H2O + O2 = glyoxylate + methylamine + H2O2
(4) N-ethylglycine + H2O + O2 = glyoxylate + ethylamine + H2O2
Systematic name: glycine:oxygen oxidoreductase (deaminating)
Comments: A flavoenzyme containing non-covalently bound FAD. The enzyme from Bacillus subtilis is active with glycine, sarcosine, N-ethylglycine, D-alanine, D-α-aminobutyrate, D-proline, D-pipecolate and N-methyl-D-alanine. It differs from EC 1.4.3.3, D-amino acid oxidase, due to its activity on sarcosine and D-pipecolate.
References:
1. Job, V., Marcone, G.L., Pilone, M.S. and Pollegioni, L. Glycine oxidase from Bacillus subtilis. Characterization of a new flavoprotein. J. Biol. Chem. 277 (2002) 6985-6993. [PMID: 11744710]
2. Nishiya, Y. and Imanaka, T. Purification and characterization of a novel glycine oxidase from Bacillus subtilis. FEBS Lett. 438 (1998) 263-266. [PMID: 9827558]
Common name: FMN reductase
Reaction: FMNH2 + NAD(P)+ = FMN + NAD(P)H + H+
Other name(s): NAD(P)H-FMN reductase; NAD(P)H-dependent FMN reductase; NAD(P)H:FMN oxidoreductase; NAD(P)H:flavin oxidoreductase; NAD(P)H2 dehydrogenase (FMN); NAD(P)H2:FMN oxidoreductase; SsuE ; riboflavin mononucleotide reductase; flavine mononucleotide reductase; riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide (phosphate)) reductase; flavin mononucleotide reductase; riboflavine mononucleotide reductase
Systematic name: FMNH2:NAD(P)+ oxidoreductase
Comments: The enzyme from luminescent bacteria and the SsuE enzyme from Escherichia coli also reduce riboflavin and FAD, but more slowly. In E. coli, this enzyme, in conjunction with EC 1.14.14.5, alkanesulfonate monooxygenase, forms a two-component alkanesulfonate monooxygenase, which allows for utilization of alkanesulfonates as sulfur sources under conditions of sulfate and cysteine starvation.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 64295-83-6
References:
1. Duane, W. and Hastings, J.W. Flavin mononucleotide reductase of luminous bacteria. Mol. Cell. Biochem. 6 (1975) 53-64. [PMID: 47604]
2. Fisher, J., Spencer, R. and Walsh, C. Enzyme-catalyzed redox reactions with the flavin analogues 5-deazariboflavin, 5-deazariboflavin 5'-phosphate, and 5-deazariboflavin 5'-diphosphate, 5' leads to 5'-adenosine ester. Biochemistry 15 (1976) 1054-1064. [PMID: 3207]
3. Tu, S.-C., Becvar, J.E. and Hastings, J.W. Kinetic studies on the mechanism of bacterial NAD(P)H:flavin oxidoreductase. Arch. Biochem. Biophys. 193 (1979) 110-116. [PMID: 222213]
4. Liu, M., Lei, B., Ding, Q., Lee, J.C. and Tu, S.C. Vibrio harveyi NADPH:FMN oxidoreductase: preparation and characterization of the apoenzyme and monomer-dimer equilibrium. Arch. Biochem. Biophys. 337 (1997) 89-95. [PMID: 8990272]
5. Lei, B. and Tu, S.C. Mechanism of reduced flavin transfer from Vibrio harveyi NADPH-FMN oxidoreductase to luciferase. Biochemistry 37 (1998) 14623-14629. [PMID: 9772191]
6. Tang, C.K., Jeffers, C.E., Nichols, J.C. and Tu, S.C. Flavin specificity and subunit interaction of Vibrio fischeri general NAD(P)H-flavin oxidoreductase FRG/FRase I. Arch. Biochem. Biophys. 392 (2001) 110-116. [PMID: 11469801]
7. Ingelman, M., Ramaswamy, S., Nivière, V., Fontecave, M. and Eklund, H. Crystal structure of NAD(P)H:flavin oxidoreductase from Escherichia coli. Biochemistry 38 (1999) 7040-7049. [PMID: 10353815]
8. Eichhorn, E., van der Ploeg, J.R. and Leisinger, T. Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli. J. Biol. Chem. 274 (1999) 26639-26646. [PMID: 10480865]
Common name: berberine reductase
Reaction: (R)-canadine + 2 NADP+ = berberine + 2 NADPH + H+
For diagram click here.
Other name(s): (R)-canadine synthase
Systematic name: (R)-tetrahydroberberine:NADP+ oxidoreductase
Comments: Involved in alkaloid biosynthesis in Corydalis cava to give (R)-canadine with the opposite configuration to the precursor of berberine (see EC 1.3.3.8 tetrahydroberberine oxidase). Also acts on 7,8-dihydroberberine.
References:
1. Bauer, W. and Zenk, M.H. Formation of (R)-configurated tetrahydroprotoberberine alkaloids in vivo and in vitro. Tetrahedron Lett. 32 (1991) 487-490.
Common name: vomilenine reductase
Reaction: 1,2-dihydrovomilenine + NADP+ = vomilenine + NADPH + H+
For diagram click here.
Systematic name: 1,2-dihydrovomilenine:NADP+ oxidoreductase
Comments: Forms part of the ajmaline biosynthesis pathway.
References:
1. von Schumann, G., Gao, S. and Stöckigt, J. Vomilenine reductase - a novel enzyme catalyzing a crucial step in the biosynthesis of the therapeutically applied antiarrhythmic alkaloid ajmaline. J. Bioorg. Med. Chem. 10 (2002) 1913-1918. [PMID: 11937349]
[EC 1.5.3.9 Transferred entry: now EC 1.21.3.3, reticuline oxidase (EC 1.5.3.9 created 1989, modified 1999, deleted 2002)]
EC 1.5.8 With a flavin as acceptor
Common name: dimethylamine dehydrogenase
Reaction: dimethylamine + H2O + electron-transferring flavoprotein = methylamine + formaldehyde + reduced electron-transferring flavoprotein
Systematic name: dimethylamine:electron-transferring flavoprotein oxidoreductase
Comments: Contains FAD and a [4Fe-4S] cluster.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 68247-64-3 (172522-63-3, 172522-64-4)
References:
1. Yang, C.C., Packman, L.C. and Scrutton, N.S. The primary structure of Hyphomicrobium X dimethylamine dehydrogenase. Relationship to trimethylamine dehydrogenase and implications for substrate recognition. Eur. J. Biochem. 232 (1995) 264-271. [PMID: 7556160]
Common name: trimethylamine dehydrogenase
Reaction: trimethylamine + H2O + electron-transferring flavoprotein = dimethylamine + formaldehyde + reduced electron-transferring flavoprotein
Systematic name: trimethylamine:electron-transferring flavoprotein oxidoreductase (demethylating)
Comments: A number of alkyl-substituted derivatives of trimethylamine can also act as electron donors; phenazine methosulfate and 2,6-dichloroindophenol can act as electron acceptors. Contains FAD and a [4Fe-4S] cluster.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 39307-09-0
References:
1. Colby, J. and Zatman, L.J. The purification and properties of a bacterial trimethylamine dehydrogenase. Biochem. J. 121 (1971) 9P-10P.
2. Steenkamp, D.J. and Singer, T.P. Participation of the iron-sulphur cluster and of the covalently bound coenzyme of trimethylamine dehydrogenase in catalysis. Biochem. J. 169 (1978) 361-369. [PMID: 204297]
3. Huang, L.X., Rohlfs, R.J. and Hille, R. The reaction of trimethylamine dehydrogenase with electron transferring flavoprotein. J. Biol. Chem. 270 (1995) 23958-23965. [PMID: 7592591]
4. Jones, M., Talfournier, F., Bobrov, A., Grossmann, J.G., Vekshin, N., Sutcliffe, M.J. and Scrutton, N.S. Electron transfer and conformational change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein. J. Biol. Chem. 277 (2002) 8457-8465. [PMID: 11756429]
5. Scrutton, N.S. and Sutcliffe, M.J. Trimethylamine dehydrogenase and electron transferring flavoprotein. Subcell. Biochem. 35 (2000) 145-181. [PMID: 11192721]
[EC 1.5.99.7 Transferred entry: now EC 1.5.8.2, trimethylamine dehydrogenase (EC 1.5.99.7 created 1976, deleted 2002)]
[EC 1.5.99.10 Transferred entry: now EC 1.5.8.1, dimethylamine dehydrogenase (EC 1.5.99.10 created 1999, deleted 2002)]
Common name: nitrite reductase (NO-forming)
Reaction: nitric oxide + H2O + ferricytochrome c = nitrite + ferrocytochrome c + 2 H+
Other name(s): cd-cytochrome nitrite reductase; [nitrite reductase (cytochrome)] [misleading, see comments.]; cytochrome c-551:O2, NO2+ oxidoreductase; cytochrome cd; cytochrome cd1; hydroxylamine (acceptor) reductase; methyl viologen-nitrite reductase; nitrite reductase (cytochrome; NO-forming)
Systematic name: nitric-oxide:ferricytochrome-c oxidoreductase
Comments: The reaction is catalysed by two types of enzymes, found in the perimplasm of denitrifying bacteria. One type comprises proteins containing multiple copper centres, the other a heme protein, cytochrome cd1. Acceptors include c-type cytochromes such as cytochrome c-550 or cytochrome c-551 from Paracoccus denitrificans or Pseudomonas aeruginosa, and small blue copper proteins such as azurin and pseudoazurin. Cytochrome cd1 also has oxidase and hydroxylamine reductase activities. May also catalyse the reaction of hydroxylamine reductase (EC 1.7.99.1) since this is a well-known activity of cytochrome cd1.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37256-41-0
References:
1. Miyata, M. and Mori, T. Studies on denitrification. X. The "denitrifying enzyme" as a nitrite reductase and the electron donating system for denitrification. J. Biochem. (Tokyo) 66 (1969) 463-471. [PMID: 5354021]
2. Chung, C.W. and Najjar, V.A. Cofactor requirements for enzymatic denitrification. I. Nitrite reductase. J. Biol. Chem. 218 (1956) 617-625.
3. Walker, G.C. and Nicholas, D.J.D. Nitrite reductase from Pseudomonas aeruginosa. Biochim. Biophys. Acta 49 (1961) 350-360.
4. Singh, J. Cytochrome oxidase from Pseudomonas aeruginosa. III. Reduction of hydroxylamine. Biochim. Biophys. Acta 333 (1974) 28-36.
5. Michalski, W.P. and Nicholas, D.J.D. Molecular characterization of a copper-containing nitrite reductase from Rhodopseudomonas sphaeriodes forma sp. Denitrificans. Biochim. Biophys. Acta 828 (1985) 130-137.
6. Godden, J.W., Turley, S., Teller, D.C., Adman, E.T., Liu, M.Y., Payne, W.J. and Legall, J. The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes. Science 253 (1991) 438-442. [PMID: 1862344]
7. Williams, P.A., Fulop, V., Leung, Y.C., Chan, C., Moir, J.W.B., Howlett, G., Ferguson, S.J., Radford, S.E. and Hajdu, J. Pseudospecific docking surfaces on electron transfer proteins as illustrated by pseudoazurin, cytochrome c-550 and cytochrome cd1 nitrite reductase. Nat. Struct. Biol. 2 (1995) 975-982. [PMID: 7583671]
8. Hole, U.H., Vollack, K.U., Zumft, W.G., Eisenmann, E., Siddiqui, R.A., Friedrich, B. and Kroneck, P.M.H. Characterization of the membranous denitrification enzymes nitrite reductase (cytochrome cd1) and copper-containing nitrous oxide reductase from Thiobacillus denitrificans. Arch. Microbiol. 165 (1996) 55-61. [PMID: 8639023]
9. Zumft, W.G. Cell biology and molecular basis of denitrification. Microbiol. Mol. Biol. Rev. 61 (1997) 533-616. [PMID: 9409151]
10. Ferguson, S.J. Nitrogen cycle enzymology. Curr. Opin. Chem. Biol. 2 (1998) 182-193. [PMID: 9667932]
11. Vijgenboom, E., Busch, J.E. and Canters, G.W. In vitro studies disprove the obligatory role of azurin in denitrification in Pseudomonas aeruginosa and show that azu expression is under the control of RpoS and ANR. Microbiology 143 (1997) 2853-2863. [PMID: 9308169]
Common name: trimethylamine-N-oxide reductase (cytochrome c)
Reaction: trimethylamine + 2 (ferricytochrome c)-subunit + H2O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+
Other name(s): TMAO reductase; TOR
Systematic name: trimethylamine:cytochrome c oxidoreductase
Comments: The cytochrome c involved in photosynthetic bacteria is a pentahaem protein. Contains bis(molybdopterin guanine dinucleotide)molybdenum cofactor. The reductant is a membrane-bound multiheme cytochrome c. Also reduces dimethyl sulfoxide to dimethyl sulfide.
References:
1. Arata, H., Shimizu, M. and Takamiya, K. Purification and properties of trimethylamine N-oxide reductase from aerobic photosynthetic bacterium Roseobacter denitrificans. J. Biochem. (Tokyo) 112 (1992) 470-475. [PMID: 1337081]
2. Knablein, J., Dobbek, H., Ehlert, S. and Schneider, F. Isolation, cloning, sequence analysis and X-ray structure of dimethyl sulfoxide trimethylamine N-oxide reductase from Rhodobacter capsulatus. Biol. Chem. 378 (1997) 293-302. [PMID: 9165084]
3. Czjzek, M., Dos Santos, J.P., Pommier, J., Giordano, G., Méjean, V. and Haser, R. Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 Å resolution. J. Mol. Biol. 284 (1998) 435-447. [PMID: 9813128]
4. Gon, S., Giudici-Orticoni, M.T., Mejean, V. and Iobbi-Nivol, C. Electron transfer and binding of the c-type cytochrome TorC to the trimethylamine N-oxide reductase in Escherichia coli. J. Biol. Chem. 276 (2001) 11545-11551. [PMID: 11056172]
Common name: urate oxidase
Reaction: urate + O2 = 5-hydroxyisourate + H2O2
Other name(s): uric acid oxidase; uricase; uricase II
For diagram click here.
Systematic name: urate:oxygen oxidoreductase
Comments: A copper protein. The 5-hydroxyisourate formed decomposes to form allantoin and CO2
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9002-12-4
References:
1. London, M. and Hudson, P.B. Purification and properties of solubilized uricase. Biochim. Biophys. Acta 21 (1956) 290-298.
2. Mahler, H.R., Hübscher, G. and Baum, H. Studies on uricase. I. Preparation, purification, and properties of a cuproprotein. J. Biol. Chem. 216 (1955) 625-641.
3. Robbins, K.C., Barnett, E.L. and Grant, N.H. Partial purification of porcine liver uricase. J. Biol. Chem. 216 (1955) 27-35.
4. Kahn, K. and Tipton, P.A. Spectroscopic characterization of intermediates in the urate oxidase reaction. Biochemistry 37 (1998) 11651-11659. [PMID: 9709003]
5. Colloc'h, N., el Hajji, M., Bachet, B., L'Hermite, G., Schiltz, M., Prange, T., Castro, B. and Mornon, J.-P. Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05 Å resolution. Nat. Struct. Biol. 4 (1997) 947-952. [PMID: 9360612]
Common name: hydroxylamine reductase
Reaction: ammonia + H2O + acceptor = hydroxylamine + reduced acceptor
Other name(s): hydroxylamine (acceptor) reductase
Systematic name: ammonia:(acceptor) oxidoreductase
Comments: A flavoprotein. Reduced pyocyanine, methylene blue and flavins act as donors for the reduction of hydroxylamine. May be identical to EC 1.7.2.1, nitrite reductase (NO-forming).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37256-42-1
References:
1. Taniguchi, H., Mitsui, H., Nakamura, K. and Egami, F. Hydoxylamine reductase. Ann. Acad. Sci. Fenn. Ser. A II 60 (1955) 200-215.
2. Walker, G.C. and Nicholas, D.J.D. Hydroxylamine reductase from Pseudomonas aeruginosa. Biochim. Biophys. Acta 49 (1961) 361-368.
3. Richter, C.D., Allen, J.W., Higham, C.W., Koppenhofer, A., Zajicek, R.S., Watmough, N.J. and Ferguson, S.J. Cytochrome cd1, reductive activation and kinetic analysis of a multifunctional respiratory enzyme. J. Biol. Chem. 277 (2002) 3093-3100.[PMID: 11709555]
[EC 1.7.99.3 Transferred entry: now included with EC 1.7.2.1, nitrite reductase (NO-forming) (EC 1.7.99.3 created 1961 as EC 1.6.6.5, transferred 1964 to EC 1.7.99.3, modified 1976, deleted 2002)]
Common name: prenylcysteine oxidase
Reaction: an S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2
Other name(s): prenylcysteine lyase
Systematic name: a prenyl-L-cysteine:oxygen oxidoreductase
Comments: A flavoprotein (FAD). Cleaves the thioether bond of S-prenyl-L-cysteines, such as S-farnesylcysteine and S-geranylgeranylcysteine. N-Acetyl-prenylcysteine and prenylcysteinyl peptides are not substrates. May represent the final step in the degradation of prenylated proteins in mammalian tissues. Originally thought to be a simple lyase, EC 4.4.1.18.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Zhang, L., Tschantz, W.R. and Casey, P.J. Isolation and characterization of a prenylcysteine lyase from bovine brain. J. Biol. Chem. 272 (1997) 23354-23359. [PMID: 9287348]
2. Tschantz, W.R., Digits, J.A., Pyun, H.J., Coates, R.M. and Casey, P.J. Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase. J. Biol. Chem. 276 (2001) 2321-2324. [PMID: 11078725]
Common name: enzyme-thiol transhydrogenase (glutathione-disulfide)
Reaction: [xanthine dehydrogenase] + glutathione disulfide = [xanthine oxidase] + 2 glutathione
Other name(s): [xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase; enzyme-thiol transhydrogenase (oxidized-glutathione); glutathione-dependent thiol:disulfide oxidoreductase; thiol:disulphide oxidoreductase
Systematic name: [xanthine-dehydrogenase]:glutathione-disulfide S-oxidoreductase
Comments: Converts EC 1.1.1.204 xanthine dehydrogenase into EC 1.1.3.22 xanthine oxidase in the presence of glutathione disulfide; also reduces the disulfide bond of ricin. Not inhibited by Cu2+ or thiol reagents.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 85030-79-1
References:
1. Battelli, M.G. and Lorenzoni, E. Purification and properties of a new glutathione-dependent thiol:disulphide oxidoreductase from rat liver. Biochem. J. 207 (1982) 133-138. [PMID: 6960894]
Common name: adenylyl-sulfate reductase (glutathione)
Reation: AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2 glutathione
Other name(s): 5'-adenylylsulfate reductase (also used for EC 1.8.99.2); AMP,sulfite:oxidized-glutathione oxidoreductase (adenosine-5'-phosphosulfate-forming); plant-type 5'-adenylylsulfate reductase
Systematic name: AMP,sulfite:glutathione-disulfide oxidoreductase (adenosine-5'-phosphosulfate-forming)
Comments: This enzyme differs from EC 1.8.99.2, adenylyl-sulfate reductase (acceptor), in using glutathione as the reductant. Glutathione can be replaced by γ-glutamylcysteine or dithiothreitol, but not by thioredoxin, glutaredoxin or mercaptoethanol. The enzyme from the mouseear cress, Arabidopsis thaliana, contains a glutaredoxin-like domain. The enzyme is also found in other photosynthetic eukaryotes, e.g., the Madagascar periwinkle, Catharanthus roseus and the hollow green seaweed, Enteromorpha intestinalis.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:
References:
1. Gutierrez-Marcos, J.F., Roberts, M.A., Campbell, E.I. and Wray, J.L. Three members of a novel small gene-family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and 'APS reductase' activity. Proc. Natl. Acad. Sci. USA 93 (1996) 13377-13382. [PMID: 8917599]
2. Setya, A., Murillo, M. and Leustek, T. Sulfate reduction in higher plants: Molecular evidence for a novel 5-adenylylphosphosulfate (APS) reductase. Proc. Natl. Acad. Sci. USA 93 (1996) 13383-13388. [PMID: 8917600]
3. Bick, J.A., Aslund, F., Cen, Y. and Leustek, T. Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5'-adenylylsulfate reductase. Proc. Natl. Acad. Sci. USA 95 (1998) 8404-8409. [PMID: 9653199]
[EC 1.9.3.2 Transferred entry: now included with EC 1.7.2.1, nitrite reductase (NO-forming) (EC 1.9.3.2 created 1965, deleted 2002)]
[EC 1.10.3.7 Transferred entry: now EC 1.21.3.4, sulochrin oxidase [(+)-bisdechlorogeodin-forming] (EC 1.10.3.7 created 1986, deleted 2002)]
[EC 1.10.3.8 Transferred entry: now EC 1.21.3.5, sulochrin oxidase [(-)-bisdechlorogeodin-forming] (EC 1.10.3.8 created 1986, deleted 2002)]
Common name: hydrogen dehydrogenase
Reaction: H2 + NAD+ = H+ + NADH
Other name(s): H2:NAD+ oxidoreductase; NAD-linked hydrogenase; bidirectional hydrogenase; hydrogenase
Systematic name: hydrogen:NAD+ oxidoreductase
Comments: An iron-sulfur flavoprotein (FMN or FAD). Some forms of this enzyme contain nickel.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, WIT, CAS registry number: 9027-05-8
References:
1. Bone, D.H., Bernstein, S. and Vishniac, W. Purification and some properties of different forms of hydrogen dehydrogenase. Biochim. Biophys. Acta 67 (1963) 581-588.
2. Schneider, K. and Schlegel, H.G. Purification and properties of soluble hydrogenase from Alcaligenes eutrophus H 16. Biochim. Biophys. Acta 452 (1976) 66-80. [PMID: 186126]
Common name: hydrogen dehydrogenase (NADP)
Reaction: H2 + NADP+ = H+ + NADPH
Other name(s): NADP-linked hydrogenase; NADP-reducing hydrogenase; hydrogenase [ambiguous]
Systematic name: hydrogen:NADP+ oxidoreductase
Comments: An iron-sulfur flavoprotein.
References:
1. de Luca, G., de Philip, P., Rousset, M., Belaich, J.P. and Dermoun, Z. The NADP-reducing hydrogenase of Desulfovibrio fructosovorans: Evidence for a native complex with hydrogen-dependent methyl-viologen-reducing activity. Biochem. Biophys. Res. Commun. 248 (1998) 591-596. [PMID: 9703971]
Common name: cytochrome-c3 hydrogenase
Reaction: 2 H2 + ferricytochrome c3 = 4 H+ + ferrocytochrome c3
Other name(s): H2:ferricytochrome c3 oxidoreductase; cytochrome c3 reductase; cytochrome hydrogenase; hydrogenase [ambiguous]
Systematic name: hydrogen:ferricytochrome-c3 oxidoreductase
Comments: An iron-sulfur protein. Some forms of the enzyme contain nickel ([NiFe]-hydrogenases) and, of these, some contain selenocysteine ([NiFeSe]-hydrogenases). Methylene blue and other acceptors can also be reduced.
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD , WIT, CAS registry number: 9027-05-8
References:
1. DerVartanian, D.V. and Le Gall, J. A monomolecular electron transfer chain: structure and function of cytochrome c3. Biochim. Biophys. Acta 346 (1974) 79-99.
2. Higuchi, Y., Yasuoka, N., Kakudo, M., Katsube, Y., Yagi, T. and Inokuchi, H. Single crystals of hydrogenase from Desulfovibrio vulgaris Miyazaki F. J. Biol. Chem. 262 (1987) 2823-2825. [PMID: 3546297]
3. Rilkis, E. and Rittenberg, D. Some observations on the enzyme, hydrogenase. J. Biol. Chem. 236 (1961) 2526-2529.
4. Sadana, J.C. and Morey, A.V. Purification and properties of the hydrogenase of Desulfovibrio desulfuricans. Biochim. Biophys. Acta 50 (1961) 153-163.
5. Volbeda, A., Charon, M.H., Piras, C., Hatchikian, E.C., Frey, M. and Fontecillacamps, J.C. Crystal-structure of the nickel-iron hydrogenase from Desulfovibrio gigas. Nature 373 (1995) 580-587. [PMID: 7854413]
6. Garcin, E., Vernede, X., Hatchikian, E.C., Volbeda, A., Frey, M. and Fontecilla-Camps, J.C. The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center. Structure Fold. Des. 7 (1999) 557-566. [PMID: 10378275]
EC 1.12.5 With a quinone or similar compound as acceptor
Common name: hydrogen:quinone oxidoreductase
Reaction: H2 + menaquinone = menaquinol
Other name(s): hydrogen-ubiquinone oxidoreductase; hydrogen:menaquinone oxidoreductase; membrane-bound hydrogenase; quinone-reactive Ni/Fe-hydrogenase
Systematic name: hydrogen:quinone oxidoreductase
Comments: Contains nickel, iron-sulfur clusters and cytochrome b. Also catalyses the reduction of water-soluble quinones (e.g. 2,3-dimethylnaphthoquinone) or viologen dyes (benzyl viologen or methyl viologen).
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 147097-29-8, 147097-28-7 and 147097-27-6
References:
1. Dross, F., Geisler, V., Lenger, R., Theis, F., Krafft, T., Fahrenholz, F., Kojro, E., Duchêne, A., Tripier, D., Juvenal, K. and Kröger, A. The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes. Eur. J. Biochem. 206 (1992) 93-102. [PMID: 1587288]
2. Dross, F., Geisler, V., Lenger, R., Theis, F., Krafft, T., Fahrenholz, F., Kojro, E., Duchêne, A., Tripier, D., Juvenal, K. and Kröger, A. The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes. Eur. J. Biochem. 206 (1992) 93-102. [Medline UI: 92267032] [An erratum appears in Eur. J. Biochem. 214 (1993) 949-050 [PMID: 8319698].
3. Gross, R., Simon, J., Lancaster, C.R.D. and Kroger, A. Identification of histidine residues in Wolinella succinogenes hydrogenase that are essential for menaquinone reduction by H-2. Mol. Microbiol. 30 (1998) 639-646. [PMID: 9822828]
4. Bernhard, M., Benelli, B., Hochkoeppler, A., Zannoni, D. and Friedrich, B. Functional and structural role of the cytochrome b subunit of the membrane-bound hydrogenase complex of Alcaligenes eutrophus H16. Eur. J. Biochem. 248 (1997) 179-186. [PMID: 9310376]
5. Ferber, D.M. and Maier, R.J. Hydrogen-ubiquinone oxidoreductase activity by the Bradyrhizobium japonicum membrane-bound hydrogenase. FEMS Microbiol. Lett. 110 (1993) 257-264. [PMID: 8354459]
6. Ishii, M., Omori, T., Igarashi, Y., Adachi, O., Ameyama, M. and Kodama, T. Methionaquinone is a direct natural electron-acceptor for the membrane-bound hydrogenase in Hydrogenobacter thermophilus strain TK-6. Agric. Biol. Chem. 55 (1991) 3011-3016.
Common name: ferredoxin hydrogenase
Reaction: H2 + oxidized ferredoxin = reduced ferredoxin + 2 H+
Other name(s): H2 oxidizing hydrogenase; H2 producing hydrogenase [ambiguous]; bidirectional hydrogenase; hydrogen-lyase [ambiguous]; hydrogenase (ferredoxin); hydrogenase I; hydrogenase II; hydrogenlyase [ambiguous]; uptake hydrogenase [ambiguous]
Systematic name: hydrogen:ferredoxin oxidoreductase
Comments: Contains iron-sulfur clusters. The enzymes from some sources contains nickel. Can use molecular hydrogen for the reduction of a variety of substances. Formerly EC 1.12.1.1, EC 1.12.7.1, EC 1.98.1.1, EC 1.18.3.1 and EC 1.18.99.1.
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, WIT, CAS registry number: 9080-02-8
References:
1. Shug, A.L., Wilson, P.W., Green, D.E. and Mahler, H.R. The role of molybdenum and flavin in hydrogenase. J. Am. Chem. Soc. 76 (1954) 3355-3356.
2. Tagawa, K. and Arnon, D.I. Ferredoxin as electron carriers in photosynthesis and in the bioogical production and consumption of hydrogen gas. Nature (Lond.) 195 (1962) 537-543.
3. Valentine, R.C., Mortenson, L.E. and Carnahan, J.E. The hydrogenase system of Clostridium pasteurianum. J. Biol. Chem. 238 (1963) 1141-1144.
4. Zumft, W.G. and Mortenson, L.E. The nitrogen-fixing complex of bacteria. Biochim. Biophys. Acta 416 (1975) 1-52. [PMID: 164247]
5. Adams, M.W.W. The structure and mechanism of iron-hydrogenases. Biochim. Biophys. Acta 1020 (1990) 115-145. [PMID: 2173950]
6. Peters, J.W., Lanzilotta, W.N., Lemon, B.J. and Seefeldt, L.C. X-ray crystal structure of the Fe-only hydrogenase (Cpl) from Clostridium pasteurianum to 1.8 Angstrom resolution. Science 282 (1998) 1853-1858. [PMID: 9836629]
EC 1.12.98 With other known acceptors
Common name: coenzyme F420 hydrogenase
Reaction: H2 + coenzyme F420 = reduced coenzyme F420
Other name(s): 8-hydroxy-5-deazaflavin-reducing hydrogenase; F420-reducing hydrogenase; coenzyme F420-dependent hydrogenase
Systematic name: hydrogen:coenzyme F420 oxidoreductase
Comments: An iron-sulfur flavoprotein (FAD) containing nickel. The enzyme from some sources contains selenocysteine. The enzyme also reduces the riboflavin analogue of F420, flavins and methylviologen, but to a lesser extent. The hydrogen acceptor coenzyme F420 is a deazaflavin derivative.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9027-05-8
References:
1. Adams, M.W.W., Mortenson, L.E. and Chen, J.-S. Hydrogenase. Biochim. Biophys. Acta 594 (1981) 105-176.
2. Yamazaki, S. A selenium-containing hydrogenase from Methanococcus vannielii. Identification of the selenium moiety as a selenocysteine residue. J. Biol. Chem. 257 (1982) 7926-7929. [PMID: 6211447]
3. Fox, J.A., Livingston, D.J., Orme-Johnson, W.H. and Walsh, C.T. 8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 1. Purification and characterization. Biochemistry 26 (1987) 4219-4228. [PMID: 62114473663585]
4. Muth, E., Morschel, E. and Klein, A. Purification and characterization of an 8-hydroxy-5-deazaflavin-reducing hydrogenase from the archaebacterium Methanococcus voltae. Eur. J. Biochem. 169 (1987) 571-577. [PMID: 3121317]
5. Baron, S.F. and Ferry, J.G. Purification and properties of the membrane-associated coenzyme F420-reducing hydrogenase from Methanobacterium formicicum. J. Bacteriol. 171 (1989) 3846-3853. [PMID: 2738024]
Common name: N5,N10-methenyltetrahydromethanopterin hydrogenase
Reaction: H2 + N5,N10-methenyltetrahydromethanopterin = H+ + N5,N10-methylenetetrahydromethanopterin
Other name(s): H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase; nonmetal hydrogenase
Systematic name: hydrogen:N5,N10-methenyltetrahydromethanopterin oxidoreductase
Comments: Does not catalyse the reduction of artificial dyes. Does not by itself catalyse a H2/H+ exchange reaction. Does not contain nickel or iron-sulfur clusters.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 100357-01-5
References:
1. Zirngibl, C., Hedderich, R. and Thauer, R.K. N5,N10-Methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum has hydrogenase activity. FEBS Lett. 261 (1990) 112-116.
2. Klein, A., Fernandez, V.M. and Thauer, R.K. H2-Forming N5,N10-methylenetetrahydromethanopterin dehydrogenase: mechanism of H2-formation analyzed using hydrogen isotopes. FEBS Lett. 368 (1995) 203-206. [PMID: 7628605]
Common name: Methanosarcina-phenazine hydrogenase
Reaction: H2 + 2-(2,3-dihydropentaprenyloxy)phenazine = 2-dihydropentaprenyloxyphenazine
Other name(s): methanophenazine hydrogenase; methylviologen-reducing hydrogenase
Systematic name: hydrogen:2-(2,3-dihydropentaprenyloxy)phenazine oxidoreductase
Comments: Contains nickel, iron-sulfur clusters and cytochrome b. The enzyme from some sources contains selenocysteine.
References:
1. Abken, H.J., Tietze, M., Brodersen, J., Baumer, S., Beifuss, U. and Deppenmeier, U. Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Gö1. J. Bacteriol. 180 (1998) 2027-2032. [PMID: 9555882]
2. Deppenmeier, U., Lienard, T. and Gottschalk, G. Novel reactions involved in energy conservation by methanogenic archaea. FEBS Lett. 457 (1999) 291-297. [PMID: 10471795]
3. Beifuss, U., Tietze, M., Baumer, S. and Deppenmeier, U. Methanophenazine: structure, total synthesis, and function of a new cofactor from methanogenic Archaea. Angew. Chem. Int. Ed. Engl. 39 (2000) 2470-2472. [PMID: 10941105]
[EC 1.12.99.1 Transferred entry: now EC 1.12.98.1, coenzyme F420 hydrogenase (EC 1.12.99.1 created 1989, deleted 2002)]
[EC 1.12.99.2 Deleted entry: coenzyme-M-7-mercaptoheptanoylthreonine-phosphate-heterodisulfide hydrogenase. This was a system comprising two enzymes and not a single enzyme, as was thought. (EC 1.12.99.2 created 1992, deleted 2002)]
[EC 1.12.99.3 Transferred entry: now EC 1.12.5.1, hydrogen:quinone oxidoreductase (EC 1.12.99.3 created 1999, deleted 2002)]
[EC 1.12.99.4 Transferred entry: now EC 1.12.98.2, N5,N10-methenyltetrahydromethanopterin hydrogenase (EC 1.12.99.4 created 1999, deleted 2002)]
Common name: hydrogenase (acceptor)
Reaction: H2 + acceptor = 2 H+ + reduced acceptor
Other name(s): H2 producing hydrogenase; [ambiguous]; hydrogen-lyase [ambiguous]; hydrogenlyase [ambiguous]; uptake hydrogenase [ambiguous]
Systematic name: hydrogen:(acceptor) oxidoreductase
Comments: Uses molecular hydrogen for the reduction of a variety of substances. Contains iron-sulfur clusters. The enzyme from some sources contains nickel.
References:
1. Shug, A.L., Wilson, P.W., Green, D.E. and Mahler, H.R. The role of molybdenum and flavin in hydrogenase. J. Am. Chem. Soc. 76 (1954) 3355-3356.
2. Adams, M.W.W., Mortenson, L.E. and Chen, J.S. Hydrogenase. Biochim. Biophys. Acta 594 (1981) 105-176.
3. Vignais, P.M., Billoud, B. and Meyer, J. Classification and phylogeny of hydrogenases. FEMS Microbiol. Rev. 25 (2001) 455-501. [PMID: 11524134]
Common name: pyrimidine-deoxynucleoside 2'-dioxygenase
Reaction: 2'-deoxyuridine + 2-oxoglutarate + O2 = uridine + succinate + CO2
Other name(s): deoxyuridine 2'-dioxygenase; deoxyuridine 2'-hydroxylase; pyrimidine deoxyribonucleoside 2'-hydroxylase; thymidine 2'-dioxygenase; thymidine 2'-hydroxylase; thymidine 2-oxoglutarate dioxygenase; thymidine dioxygenase
Systematic name: 2'-deoxyuridine,2-oxoglutarate:oxygen oxidoreductase (2'-hydroxylating)
Comments: Requires Fe(II) and ascorbate. Also acts on thymidine. cf. EC 1.14.11.10, pyrimidine-deoxynucleoside 1'-dioxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9076-89-5
References:
1. Bankel, L., Lindstedt, G. and Lindstedt, S. Thymidine 2'-hydroxylation in Neurospora crassa. J. Biol. Chem. 247 (1972) 6128-6134. [PMID: 4265566]
2. Stubbe, J. Identification of two α-ketoglutarate-dependent dioxygenases in extracts of Rhodotorula glutinis catalyzing deoxyuridine hydroxylation. J. Biol. Chem. 260 (1985) 9972-9975. [PMID: 4040518]
3. Warn-Cramer, B.J., Macrander, L.A. and Abbott, M.T. Markedly different ascorbate dependencies of the sequential α-ketoglutarate dioxygenase reactions catalyzed by an essentially homogeneous thymine 7-hydroxylase from Rhodotorula glutinis. J. Biol. Chem. 258 (1983) 10551-10557. [PMID: 6684117]
Common name: pyrimidine-deoxynucleoside 1'-dioxygenase
Reaction: 2'-deoxyuridine + 2-oxoglutarate + O2 = uracil + 2-deoxyribonolactone + succinate + CO2
Other name(s): deoxyuridine-uridine 1'-dioxygenase
Systematic name: 2'-deoxyuridine,2-oxoglutarate:oxygen oxidoreductase (1'-hydroxylating)
Comments: Requires Fe(II) and ascorbate. cf. EC 1.14.11.3, pyrimidine-deoxynucleoside 2'-dioxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 98865-52-2
References:
1. Stubbe, J. Identification of two α-ketoglutarate-dependent dioxygenases in extracts of Rhodotorula glutinis catalyzing deoxyuridine hydroxylation. J. Biol. Chem. 260 (1985) 9972-9975. [PMID: 4040518]
Common name: desacetoxyvindoline 4-hydroxylase
Reaction: desacetoxyvindoline + 2-oxoglutarate + O2 = desacetylvindoline + succinate + CO2
For reaction pathway click here.
Systematic name: desacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase (4β-hydroxylating)
Comments: Requires Fe2+ and ascorbate. Also acts on 16-methoxy-2,3-dihydro-3-hydroxytabersonine and to a lesser extent on 16-methoxy-2,3-dihydrotabersonine.
References:
1. De Carolis, E., Chan, F., Balsevich, J. and De Luca, V. Isolation and characterization of a 2-oxoglutarate dependent dioxygenase involved in the 2nd-to-last step in vindoline biosynthesis Plant Physiol. 94 (1990) 1323-1329.
2. De Carolis, E. and De Luca, V. Purification, characterization, and kinetic analysis of a 2-oxoglutarate-dependent dioxygenase involved in vindoline biosynthesis from Catharanthus roseus. J. Biol. Chem. 268 (1993) 5504-5511. [PMID: 8449913]
3. Vazquez-Flota, F.A. and De Luca, V. Developmental and light regulation of desacetoxyvindoline 4-hydroxylase in Catharanthus roseus (L.) G. Don. Evidence of a multilevel regulatory mechanism. Plant Physiol. 117 (1998) 1351-1361. [PMID: 9701591]
Common name: tabersonine 16-hydroxylase
Reaction: tabersonine + NADPH + H+ + O2 = 16-hydroxytabersonine + NADP+ + H2O
For diagram click here.
Systematic name: tabersonine,NADPH:oxygen oxidoreductase (16-hydroxylating)
Comments: A heme-thiolate protein (P-450).
References:
1. St-Pierre, B. and De Luca, V. A cytochrome-P-450 monooxygenase catalyzes the first step in the conversion of tabersonine to vindoline in Catharanthus-roseus. Plant Physiol. 109 (1995) 131-139.
Common name: 7-deoxyloganin 7-hydroxylase
Reaction: 7-deoxyloganin + NADPH + H+ + O2 = loganin + NADP+ + H2O
For diagram click here.
Systematic name: 7-deoxyloganin,NADPH:oxygen oxidoreductase (7α-hydroxylating)
Comments: A heme-thiolate protein (P-450).
References:
1. Katano, N., Yamamoto, H., Iio, R. and Inoue, K. 7-Deoxyloganin 7-hydroxylase in Lonicera japonica cell cultures Phytochemistry 58 (2001) 53-58. [PMID: 11524113]
Common name: vinorine hydroxylase
Reaction: vinorine + NADPH + H+ + O2 = vomilenine + NADP+ + H2O
For diagram click here.
Systematic name: vinorine ,NADPH:oxygen oxidoreductase (21α-hydroxylating)
Comments: A heme-thiolate protein (P-450). Forms a stage in the biosynthesis of the indole alkaloid ajmaline.
References:
1. Falkenhagen, H. and Stöckligt, J. Enzymatic biosynthesis of vomilenine, a key intermediate of the ajmaline pathway, catalysed by a novel cytochrome P-450-dependent enzyme from plant cell cultures of Rauwolfia serpentina. Z. Naturforsch. C: Biosci. 50 (1995) 45-53.
Common name: taxane 10β-hydroxylase
Reaction: taxa-4(20),11-dien-5α-yl acetate+ NADPH + H+ + O2 = 10β-hydroxytaxa-4(20),11-dien-5α-yl acetate+ NADP + H2O
For diagram click here.
Systematic name: taxa-4(20),11-dien-5α-yl acetate,NADPH:oxygen oxidoreductase (10β-hydroxylating)
References:
1. Wheeler, A.L., Long, R.M., Ketchum, R.E., Rithner, C.D., Williams, R.M. and Croteau, R. Taxol biosynthesis: differential transformations of taxadien-5α-ol and its acetate ester by cytochrome P450 hydroxylases from Taxus suspension cells. Arch. Biochem. Biophys. 390 (2001) 265-78. [PMID: 11396929]
2. Jennewein, S., Rithner, C.D., Williams, R.M. and Croteau, R.B. Taxol biosynthesis: taxane 13 α-hydroxylase is a cytochrome P450-dependent monooxygenase. Proc. Natl. Acad. Sci. U S A 98 (2001) 13595-135600. [PMID: 11707604]
Common name: taxane 13α-hydroxylase
Reaction: taxa-4(20),11-dien-5α-ol+ NADPH + H+ + O2 = taxa-4(20),11-dien-5α,13α-diol+ NADP+ + H2O
For diagram click here.
Systematic name: taxa-4(20),11-dien-5α-ol,NADPH:oxygen oxidoreductase (13α-hydroxylating)
References:
1. Wheeler, A.L., Long, R.M., Ketchum, R.E., Rithner, C.D., Williams, R.M. and Croteau, R. Taxol biosynthesis: differential transformations of taxadien-5α-ol and its acetate ester by cytochrome P450 hydroxylases from Taxus suspension cells. Arch. Biochem. Biophys. 390 (2001) 265-78. [PMID: 11396929]
2. Jennewein, S., Rithner, C.D., Williams, R.M. and Croteau, R.B. Taxol biosynthesis: taxane 13 α-hydroxylase is a cytochrome P450-dependent monooxygenase. Proc. Natl. Acad. Sci. U S A 98 (2001) 13595-135600. [PMID: 11707604]
Common name: ent-kaurene oxidase
Reaction: (1) ent-kaur-16-ene + NADPH + H+ + O2 = ent-kaur-16-en-19-ol + NADP+ + H2O
(2) ent-kaur-16-en-19-ol + NADPH + H+ + O2 = ent-kaur-16-en-19-al + NADP+ + 2 H2O
(3) ent-kaur-16-en-19-al + NADPH + O2 = ent-kaur-16-en-19-oate + NADP+ + H2O
For diagram click here.
Systematic name: ent-kaur-16-ene,NADPH:oxygen oxidoreductase (hydroxylating)
Comments: Requires cytochrome P450. Catalyses three sucessive oxidations of the 4-methyl group of ent-kaurene giving kaurenoic acid.
References:
1. Ashman, P.J., Mackenzie, A. and Bramley, P.M. Characterization of ent-kaurene oxidase activity from Gibberella fujikuroi. Biochim. Biophys. Acta 1036 (1990) 151-157. [PMID: 2223832]
2. Archer, C., Ashman, P.J., Hedden, P., Bowyer, J.R. and Bramley, P.M. Purification of ent-kaurene oxidase from Gibberella fujikuroi and Cucurbita maxima. Biochem. Soc. Trans. 20 (1992) 218S only. [PMID: 1397591]
3. Helliwell, C.A., Poole, A., Peacock, W.J. and Dennis, E.S. Arabidopsis ent-kaurene oxidase catalyzes three steps of gibberellin biosynthesis. Plant Physiol. 119 (1999) 507-510. [PMID: 9952446]
Common name: ent-kaurenoic acid oxidase
Reaction: (1) ent-kaur-16-en-19-oate + NADPH + H+ + O2 = ent-7α-hydroxykaur-16-en-19-oate + NADP+ + H2O
(2) ent-7α-hydroxykaur-16-en-19-oate + NADPH + H+ + O2 = gibberellin A12 aldehyde + NADP+ + 2 H2O
(3) gibberellin A12 aldehyde + NADPH + O2 = gibberellin A12 + NADP+ + H2O
For diagram click here.
Systematic name: ent-kaur-16-en-19-oate,NADPH:oxygen oxidoreductase (hydroxylating)
Comments: Requires cytochrome P450. Catalyses three sucessive oxidations of ent-kaurenoic acid. The second step includes a ring-B contraction giving the gibbane skeleton. In pumpkin (Cucurbita maxima) ent-6α,7α-dihydroxykaur-16-en-19-oate is also formed.
References:
1. Helliwell, C.A., Chandler, P.M., Poole, A., Dennis, E.S. and Peacock, W.J. The CYP88A cytochrome P450, ent-kaurenoic acid oxidase, catalyzes three steps of the gibberellin biosynthesis pathway. Proc. Natl. Acad. Sci. USA 98 (2001) 2065-2070. [PMID: 11172076]
Common name: alkanesulfonate monooxygenase
Reaction: an alkanesufonate (R-CH2-SO3H) + FMNH2 + O2 = an aldehyde (R-CHO) + FMN + sulfite + H2O
Other name(s): SsuD; sulfate starvation-induced protein 6
Systematic name: alkanesulfonate, reduced-FMN:oxygen oxidoreductase
Comments: The enzyme from Escherichia coli catalyses the desulfonation of a wide range of aliphatic sulfonates (unsubstituted C1- to C14-sulfonates as well as substituted C2-sulfonates). Does not desulfonate taurine (2-aminoethanesulfonate) or aromatic sulfonates. Does not use FMN as a bound cofactor. Instead, it uses reduced FMN (i.e., FMNH2) as a substrate. FMNH2 is provided by SsuE, the associated FMN reductase (EC 1.5.1.29).
References:
1. Eichhorn, E., van der Ploeg, J.R. and Leisinger, T. Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli. J. Biol. Chem. 274 (1999) 26639-26646. [PMID: 10480865]
Common name: phenylalanine 4-monooxygenase
Reaction: L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + dihydrobiopterin + H2O
For diagram click here and mechanism here.
Other name(s): phenylalaninase; phenylalanine 4-hydroxylase; phenylalanine hydroxylase
Systematic name: L-phenylalanine,tetrahydrobiopterin:oxygen oxidoreductase (4-hydroxylating)
Comments: The mammalian enzyme is an iron protein. The reaction involves an arene oxide which rearranges to give the phenolic hydroxy group. This results in the hydrogen at C-4 migrating to C-3 and in part being retained. A process known as the NIH-shift. Formerly EC 1.14.3.1 and EC 1.99.1.2.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9029-73-6
References:
1. Guroff, G. and Rhoads, C.A. Phenylalanine hydroxylation by Pseudomonas species (ATCC 11299a). Nature of the cofactor. J. Biol. Chem. 244 (1969) 142-146. [PMID: 5773277]
2. Kaufman, S. Studies on the mechanism of the enzymic conversion of phenylalanine to tyrosine. J. Biol. Chem. 234 (1959) 2677-2682.
3. Mitoma, C. Studies on partially purified phenylalanine hydroxylase. Arch. Biochem. Biophys. 60 (1956) 476-484.
4. Udenfriend, S. and Cooper, J.R. The enzymic conversion of phenylalanine to tyrosine. J. Biol. Chem. 194 (1952) 503-511.
5. Carr, R.T., Balasubramanian, S., Hawkins, P.C. and Benkovic, S.J. Mechanism of metal-independent hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase. Biochemistry 34 (1995) 7525-7532. [PMID: 7779797]
.
EC 1.14.20 With 2-oxoglutarate as one donor, and the other dehydrogenated
Common name: deacetoxycephalosporin-C synthase
Reaction: penicillin N + 2-oxoglutarate + O2 = deacetoxycephalosporin C + succinate + CO2 + H2O
For diagram click here.
Other names: DAOCS; penicillin N expandase
Systematic name: penicillin-N,2-oxoglutarate:oxygen oxidoreductase (ring-expanding)
Comments: Forms part of the penicillin biosynthesis pathway (for pathway, click here).
References:
1. Cantwell, C., Beckmann, R., Whiteman, P., Queener, S.W. and Abraham, E.P. Isolation of deacetoxycephalosporin-c from fermentation broths of Penicillium chrysogenum transformants - construction of a new fungal biosynthetic-pathway. Proc. R. Soc. Lond. B Biol. Sci. 248 (1992) 283-289. [PMID: 1354366]
2. Lee, H.J., Lloyd, M.D., Harlos, K., Clifton, I.J., Baldwin, J.E. and Schofield, C.J. Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS). J. Mol. Biol. 308 (2001) 937-948. [PMID: 11352583]
3. Yeh, W.K., Ghag, S.K. and Queener, S.W. Enzymes for epimerization of isopenicillin N, ring expansion of penicillin N, and 3'-hydroxylation of deacetoxycephalosporin C. Function, evolution, refolding, and enzyme engineering. Ann. N.Y. Acad. Sci. 672 (1992) 396-408.
4. Valegård, K., van Scheltinga, A.C.T., Lloyd, M.D., Hara, T., Ramaswamy, S., Perrakis, A., Thompson, A., Lee, H.-J., Baldwin, J.E., Schofield, C.J., Hajdu, J. and Andersson, I. Structure of a cephalosporin synthase. Nature 394 (1998) 805-809. [PMID: 9723623]
EC 1.14.21 With NADH or NADPH as one donor, and the other dehydrogenated
Common name: (S)-stylopine synthase
Reaction: (S)-cheilanthifoline + NADPH + H+ + O2 = (S)-stylopine + NADP+ + 2 H2O
For diagram click here.
Other name(s): (S)-cheilanthifoline oxidase (methylenedioxy-bridge-forming)
Systematic name: (S)-cheilanthifoline,NADPH:oxygen oxidoreductase (methylenedioxy-bridge-forming)
Comments: A heme-thiolate enzyme (P-450) catalysing an oxidative reaction that does not incorporate oxygen into the product. Forms the second methylenedioxy bridge of the protoberberine alkaloid stylopine from oxidative ring closure of adjacent phenolic and methoxy groups of cheilanthifoline.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 138791-29-4
References:
1. Bauer, W. and Zenk, M.H. Two methylenedioxy bridge-forming cytochrome P-450 dependent enzymes are involved in (S)-stylopine biosynthesis. Phytochemistry 30 (1991) 2953-2961.
Common name: (S)-cheilanthifoline synthase
Reaction: (S)-scoulerine + NADPH + H+ + O2 = (S)-cheilanthifoline + NADP+ + 2 H2O
For diagram click here.
Other name(s): (S)-scoulerine oxidase (methylenedioxy-bridge-forming)
Systematic name: (S)-scoulerine,NADPH:oxygen oxidoreductase (methylenedioxy-bridge-forming)
Comments: A heme-thiolate enzyme (P-450) catalysing an oxidative reaction that does not incorporate oxygen into the product. Forms the methylenedioxy bridge of the protoberberine alkaloid cheilanthifoline from oxidative ring closure of adjacent phenolic and methoxy groups of scoulerine.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 138791-27-2
References:
1. Bauer, W. and Zenk, M.H. Two methylenedioxy bridge-forming cytochrome P-450 dependent enzymes are involved in (S)-stylopine biosynthesis. Phytochemistry 30 (1991) 2953-2961.
Common name: berbamunine synthase
Reaction: (S)-N-methylcoclaurine + (R)-N-methylcoclaurine + NADPH + H+ + O2 = berbamunine + NADP+ + 2 H2O
For diagram click here.
Other name(s): (S)-N-methylcoclaurine oxidase (C-O phenol-coupling)
Systematic name: (S)-N-methylcoclaurine,NADPH:oxygen oxidoreductase (C-O phenol-coupling)
Comments: A heme-thiolate enzyme (P-450). Forms the bisbenzylisoquinoline alkaloid berbamunine by phenol oxidation of N-methylcoclaurine without the incorporation of oxygen into the product. Reaction of two molecules of (R)-N-methylcoclaurine gives the dimer guattagaumerine.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 144941-42-4
References:
1. Stadler, R. and Zenk, M.H. The purification and characterization of a unique cytochrome P-450 enzyme from Berberis stolifera plant cell cultures. J. Biol. Chem. 268 (1993) 823-831. [PMID: 8380416]
Common name: salutaridine synthase
Reaction: (R)-reticuline + NADPH + H+ + O2 = salutaridine + NADP+ + 2 H2O
For diagram click here.
Other name(s): (R)-reticuline oxidase (C-C phenol-coupling)
Systematic name: (R)-reticuline,NADPH:oxygen oxidoreductase (C-C phenol-coupling)
Comments: A heme-thiolate enzyme (P-450). Forms the morphinan alkaloid salutaridine by intramolecular phenol oxidation of reticuline without the incorporation of oxygen into the product.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 149433-84-1
References:
1. Gerady, R. and Zenk, M.H. Formation of salutaridine from (R)-reticuline by a membrane-bound cytochrome P-450 enzyme from Papaver somniferum. Phytochemistry 32 (1993) 79-86.
Common name: (S)-canadine synthase
Reaction: (S)-tetrahydrocolumbamine + NADPH + H+ + O2 = (S)-canadine + NADP+ + 2 H2O
For diagram click here.
Other name(s): (S)-tetrahydroberberine synthase; (S)-tetrahydrocolumbamine oxidase (methylenedioxy-bridge-forming)
Systematic name: (S)-tetrahydrocolumbamine,NADPH:oxygen oxidoreductase (methylenedioxy-bridge-forming)
Comments: A heme-thiolate enzyme (P-450) catalysing an oxidative reaction that does not incorporate oxygen into the product. Oxidation of the methoxyphenol group of the alkaloid tetrahydrocolumbamine results in the formation of the methylenedioxy bridge of canadine.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 114308-22-4
References:
1. Rueffer, M. and Zenk, M.H. Canadine synthase from Thalictrum tuberosum cell cultures catalyses the formation of the methylenedioxy bridge in berberine synthesis. Phytochemistry 36 (1994) 1219-1223.
Common name: taxadiene 5α-hydroxylase
Reaction: taxa-4,11-diene + AH2 + O2 = taxa-4(20),11-dien-5α-ol + A + H2O
For diagram click here.
Systematic name: taxa-4,11-diene,hydrogen-donor:oxygen oxidoreductase (5α-hydroxylating)
Comments: Requires P-450. The reaction includes rearrangement of the 4(5)-double bond to a 4(20)-double bond, possibly through allylic oxidation.
References:
1. Hefner, J., Rubenstein, S.M., Ketchum, R.E., Gibson, D.M., Williams, R.M. and Croteau, R. Cytochrome P450-catalyzed hydroxylation of taxa-4(5),11(12)-diene to taxa-4(20),11(12)-dien-5alpha-ol: the first oxygenation step in taxol biosynthesis. Chem. Biol. 3 (1996) 479-489. [PMID: 8807878]
[EC 1.18.99.1 Transferred entry: now EC 1.12.7.2, ferredoxin hydrogenase (EC 1.18.99.1 created 1961 as EC 1.98.1.1, transferred 1965 to EC 1.12.1.1, transferred 1972 to EC 1.12.7.1, transferred 1978 to EC 1.18.3.1, transferred 1984 to EC 1.18.99.1, deleted 2002)]
EC 1.21 ACTING ON X-H AND Y-H TO FORM AN X-Y BOND
EC 1.21.3 With oxygen as acceptor
Common name: isopenicillin-N synthase
Reaction: N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O
For diagram click here and possible mechanism click here.
Systematic name: N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine:oxygen oxidoreductase (cyclizing)
Comments: Forms part of the penicillin biosynthesis pathway (for pathway, click here).
References:
1. Huffman, G.W., Gesellchen, P.D., Turner, J.R., Rothenberger, R.B., Osborne, H.E., Miller, F.D., Chapman, J.L. and Queener, S.W. Substrate specificity of isopenicillin N synthase. J. Med. Chem. 35 (1992) 1897-1914. [PMID: 1588566]
2. Roach, P.L., Clifton, I.J., Fulop, V., Harlos, K., Barton, G.J., Hajdu, J., Andersson, I., Schofield, C.J. and Baldwin, J.E. Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes. Nature 375 (1995) 700-704. [PMID: 7791906]
Common name: columbamine oxidase
Reaction: 2 columbamine + O2 = 2 berberine + 2 H2O
For diagram click here.
Other name(s): berberine synthase
Systematic name: columbamine:oxygen oxidoreductase (cyclizing)
Comments: An iron protein. Oxidation of the O-methoxyphenol structure forms the methylenedioxy group of berberine.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 95329-18-3
References:
1. Rueffer, M. and Zenk, M.H. Berberine synthesis, the methylenedioxy group forming enzyme in berberine synthesis. Tetrahedron Lett. 26 (1985) 201-202.
Common name: reticuline oxidase
Reaction: (S)-reticuline + O2 = (S)-scoulerine + H2O2
For diagram click here.
Other name(s): BBE; berberine bridge enzyme; berberine-bridge-forming enzyme; tetrahydroprotoberberine synthase
Systematic name: (S)-reticuline:oxygen oxidoreductase (methylene-bridge-forming)
Comments: The product of the reaction, (S)-scoulerine, is a precursor of protopine, protoberberine and benzophenanthridine alkaloid biosynthesis in plants. Acts on (S)-reticuline and related compounds, converting the N-methyl group into the methylene bridge ('berberine bridge') of (S)-tetrahydroprotoberberines.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 152232-28-5
References:
1. Steffens, P., Nagakura, N. and Zenk, M.H. The berberine bridge forming enzyme in tetrahydroprotoberberine biosynthesis. Tetrahedron Lett. 25 (1984) 951-952.
2. Dittrich, H. and Kutchan, T.M. Molecular cloning, expression and induction of the berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Proc. Natl. Acad. Sci. USA 88 (1991) 9969-9973. [PMID: 1946465]
3. Kutchan, T.M. and Dittrich, H. Characterization and mechanism of the berberine bridge enzyme, a covalently flavinylated oxidase of benzophenanthridine alkaloid biosynthesis in higher plants. J. Biol. Chem. 270 (1995) 24475-24481. [PMID: 7592663]
Common name: sulochrin oxidase [(+)-bisdechlorogeodin-forming]
Reaction: 2 sulochrin + O2 = 2 (+)-bisdechlorogeodin + 2 H2O
For diagram click here.
Other name(s): sulochrin oxidase
Systematic name: sulochrin:oxygen oxidoreductase (cyclizing, (+)-specific)
Comments: Also acts on several diphenols and phenylenediamines, but has low affinity for these substrates. Involved in the biosynthesis of mould metabolites related to the antibiotic griseofulvin.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 82469-87-2
References:
1. Nordlöv, H. and Gatenbeck, S. Enzymatic synthesis of (+)- and (-)-bisdechlorogeodin with sulochrin oxidase from Penicillium frequentans and Oospora sulphurea ochracea. Arch. Microbiol. 131 (1982) 208-211. [PMID: 7049104]
Common name: sulochrin oxidase [(-)-bisdechlorogeodin-forming]
Reaction: 2 sulochrin + O2 = 2 (-)-bisdechlorogeodin + 2 H2O
For diagram click here.
Other name(s): sulochrin oxidase
Systematic name: sulochrin:oxygen oxidoreductase (cyclizing, (-)-specific)
Comments: Also acts on several diphenols and phenylenediamines, but has low affinity for these substrates. Involved in the biosynthesis of mould metabolites related to the antibiotic griseofulvin.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 82469-87-2
References:
1. Nordlöv, H. and Gatenbeck, S. Enzymatic synthesis of (+)- and (-)-bisdechlorogeodin with sulochrin oxidase from Penicillium frequentans and Oospora sulphurea ochracea. Arch. Microbiol. 131 (1982) 208-211. [PMID: 7049104]
EC 1.21.99 With other acceptors
Common name: β-cyclopiazonate dehydrogenase
Reaction: β-cyclopiazonate + acceptor = α-cyclopiazonate + reduced acceptor
For diagram click here.
Other name(s): β-cyclopiazonate oxidocyclase; β-cyclopiazonic oxidocyclase
Systematic name: β-cyclopiazonate:(acceptor) oxidoreductase (cyclizing)
Comments: A flavoprotein (FAD). Cytochrome c and various dyes can act as acceptor. Cyclopiazonate is a microbial toxin.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9059-00-1
References:
1. Edmondson, D.E., Kenney, W.C. and Singer, T.P. Structural elucidation and properties of 8α-(N1-histidyl)riboflavin: the flavin component of thiamine dehydrogenase and β-cyclopiazonate oxidocyclase. Biochemistry 15 (1976) 2937-2945. [PMID: 8076]
2. Schabort, J.C. and Potgieter, D.J.J. β-Cyclopiazonate oxidocyclase from Penicillium cyclopium. II. Studies on electron acceptors, inhibitors, enzyme kinetics, amino acid composition, flavin prosthetic group and other properties. Biochim. Biophys. Acta 250 (1971) 329-345. [PMID: 5143340]