An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.
Common name: isocitrate dehydrogenase (NAD+)
Reaction: isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH
For diagram click here.
Glossary: isocitrate = (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate (previously known as threo-DS-isocitrate)
Other name(s): isocitric dehydrogenase; β-ketoglutaric-isocitric carboxylase; isocitric acid dehydrogenase; NAD dependent isocitrate dehydrogenase; NAD isocitrate dehydrogenase; NAD-linked isocitrate dehydrogenase; NAD-specific isocitrate dehydrogenase; NAD isocitric dehydrogenase; isocitrate dehydrogenase (NAD); IDH (ambiguous); nicotinamide adenine dinucleotide isocitrate dehydrogenase
Systematic name: isocitrate:NAD+ oxidoreductase (decarboxylating)
Comments: Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.42, isocitrate dehydrogenase (NADP+), oxalosuccinate cannot be used as a substrate. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD+-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP+-linked enzyme that is found in both mitochondria and cytoplasm [7]. The enzyme from some species can also use NADP+ but much more slowly [9].
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 9001-58-5
References:
1. Hathaway, J.A. and Atkinson, D.E. The effect of adenylic acid on yeast nicotinamide adenine dinucleotide isocitrate dehydrogenase, a possible metabolic control mechanism. J. Biol. Chem. 238 (1963) 2875-2881. [PMID: 14063317]
2. Kornberg, A. and Pricer, W.E. Di- and triphosphopyridine nucleotide isocitric dehydrogenase in yeast. J. Biol. Chem. 189 (1951) 123-136. [PMID: 14832224]
3. Plaut, G.W.E. Isocitrate dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, pp. 105-126.
4. Plaut, G.W.E. and Sung, S.-C. Diphosphopyridine nucleotide isocitric dehydrogenase from animal tissues. J. Biol. Chem. 207 (1954) 305-314. [PMID: 13152105]
5. Ramakrishnan, C.V. and Martin, S.M. Isocitric dehydrogenase in Aspergillus niger. Arch. Biochem. Biophys. 55 (1955) 403-407.
6. Vickery, H.B. A suggested new nomenclature for the isomers of isocitric acid. J. Biol. Chem. 237 (1962) 1739-1741. [PMID: 13925783]
7. Camacho, M.L., Brown, R.A., Bonete, M.J., Danson, M.J. and Hough, D.W. Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus solfataricus: enzyme purification, characterisation and N-terminal sequence. FEMS Microbiol. Lett. 134 (1995) 85-90. [PMID: 8593959]
8. Kim, Y.O., Koh, H.J., Kim, S.H., Jo, S.H., Huh, J.W., Jeong, K.S., Lee, I.J., Song, B.J. and Huh, T.L. Identification and functional characterization of a novel, tissue-specific NAD+-dependent isocitrate dehydrogenase β subunit isoform. J. Biol. Chem. 274 (1999) 36866-36875. [PMID: 10601238]
9. Inoue, H., Tamura, T., Ehara, N., Nishito, A., Nakayama, Y., Maekawa, M., Imada, K., Tanaka, H. and Inagaki, K. Biochemical and molecular characterization of the NAD+-dependent isocitrate dehydrogenase from the chemolithotroph Acidithiobacillus thiooxidans. FEMS Microbiol. Lett. 214 (2002) 127-132. [PMID: 12204383]
Common name: isocitrate dehydrogenase (NADP+)
Reaction: (1) isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH
(2) oxalosuccinate + NADP+ = 2-oxoglutarate + CO2 + NADPH
For diagram click here.
Glossary: isocitrate = (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate (previously known as threo-DS-isocitrate)
oxalosuccinate = 1-oxopropane-1,2,3-tricarboxylate
Other name(s): oxalosuccinate decarboxylase; isocitrate dehydrogenase (NADP); oxalsuccinic decarboxylase; isocitrate (NADP) dehydrogenase; isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; NADP-specific isocitrate dehydrogenase; NADP-linked isocitrate dehydrogenase; NADP-dependent isocitrate dehydrogenase; NADP isocitric dehydrogenase; isocitrate dehydrogenase (NADP-dependent); NADP-dependent isocitric dehydrogenase; triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase; NADP+-linked isocitrate dehydrogenase; IDH (ambiguous); dual-cofactor-specific isocitrate dehydrogenase; NADP+-ICDH; NADP+-IDH; IDP; IDP1; IDP2; IDP3
Systematic name: isocitrate:NADP+ oxidoreductase (decarboxylating)
Comments: Requires Mn2+ or Mg2+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+), oxalosuccinate can be used as a substrate. In eukaryotes, isocitrate dehydrogenase exists in two forms: an NAD+-linked enzyme found only in mitochondria and displaying allosteric properties, and a non-allosteric, NADP+-linked enzyme that is found in both mitochondria and cytoplasm [6]. The enzyme from some species can also use NAD+ but much more slowly [6,7].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, ERGO, PDB, CAS registry number: 9028-48-2
References:
1. Agosin, M.U. and Weinbach, E.C. Partial purification and characterization of the isocitric dehydrogenase from Trypanosoma cruzi. Biochim. Biophys. Acta 21 (1956) 117-126. [PMID: 13363868]
2. Moyle, J. and Dixon, M. Purification of the isocitrate enzyme (triphosphopyridine nucleotide-linked isocitrate dehydrogenase-oxalosuccinate carboxylase). Biochem. J. 63 (1956) 548-552. [PMID: 13355848]
3. Plaut, G.W.E. Isocitrate dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 105-126.
4. Siebert, G., Dubuc, J., Warner, R.C. and Plaut, G.W.E. The preparation of isocitrate dehydrogenase from mammalian heart. J. Biol. Chem. 226 (1957) 965-975. [PMID: 13438885]
5. Vickery, H.B. A suggested new nomenclature for the isomers of isocitric acid. J. Biol. Chem. 237 (1962) 1739-1741. [PMID: 13925783]
6. Camacho, M.L., Brown, R.A., Bonete, M.J., Danson, M.J. and Hough, D.W. Isocitrate dehydrogenases from Haloferax volcanii and Sulfolobus solfataricus: enzyme purification, characterisation and N-terminal sequence. FEMS Microbiol. Lett. 134 (1995) 85-90. [PMID: 8593959]
7. Steen, I.H., Lien, T. and Birkeland, N.-K. Biochemical and phylogenetic characterization of isocitrate dehydrogenase from a hyperthermophilic archaeon, Archaeoglobus fulgidus. Arch. Microbiol. 168 (1997) 412-420. [PMID: 9325430]
8. Koh, H.J., Lee, S.M., Son, B.G., Lee, S.H., Ryoo, Z.Y., Chang, K.T., Park, J.W., Park, D.C., Song, B.J., Veech, R.L., Song, H. and Huh, T.L. Cytosolic NADP+-dependent isocitrate dehydrogenase plays a key role in lipid metabolism. J. Biol. Chem. 279 (2004) 39968-39974. [PMID: 15254034]
9. Ceccarelli, C., Grodsky, N.B., Ariyaratne, N., Colman, R.F. and Bahnson, B.J. Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism. J. Biol. Chem. 277 (2002) 43454-43462. [PMID: 12207025]
Common name: isocitrate—homoisocitrate dehydrogenase
Reaction: (1) isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH
(2) (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+
Other name(s): homoisocitrate—isocitrate dehydrogenase; PH1722
Systematic name: isocitrate(homoisocitrate):NAD+ oxidoreductase (decarboxylating)
Comments: Requres Mn2+ and K+ or NH4+ for activity. Unlike EC 1.1.1.41, isocitrate dehydrogenase (NAD+) and EC 1.1.1.87, homoisocitrate dehydrogenase, this enzyme, from Pyrococcus horikoshii, can use both isocitrate and homoisocitrate as substrates. The enzyme may play a role in both the lysine and glutamate biosynthesis pathways.
References:
1. Miyazaki, K. Bifunctional isocitrate-homoisocitrate dehydrogenase: a missing link in the evolution of β-decarboxylating dehydrogenase. Biochem. Biophys. Res. Commun. 331 (2005) 341-346. [PMID: 15845397]
Common name: D-arabinitol dehydrogenase (NADP+)
Reaction: (1) D-arabinitol + NADP+ = D-xylulose + NADPH + H+
(2) D-arabinitol + NADP+ = D-ribulose + NADPH + H+
Other name(s): NADP+-dependent D-arabitol dehydrogenase; ARD1p; D-arabitol dehydrogenase 1
Systematic name: D-arabinitol:NADP+ oxidoreductase
Comments: The enzyme from the rust fungus Uromyces fabae can use D-arabinitol and D-mannitol as substrates in the forward direction and D-xylulose, D-ribulose and, to a lesser extent, D-fructose as substrates in the reverse direction. This enzyme carries out the reactions of both EC 1.1.1.11, D-arabinitol 4-dehydrogenase and EC 1.1.1.250, D-arabinitol 2-dehydrogenase, but unlike them, uses NADP+ rather than NAD+ as cofactor. D-Arabinitol is capable of quenching reactive oxygen species involved in defense reactions of the host plant.
References:
1. Link, T., Lohaus, G., Heiser, I., Mendgen, K., Hahn, M. and Voegele, R.T. Characterization of a novel NADP+-dependent D-arabitol dehydrogenase from the plant pathogen Uromyces fabae. Biochem. J. 389 (2005) 289-295. [PMID: 15796718]
Common name: choline oxidase
Reaction: choline + O2 = betaine aldehyde + H2O2
Systematic name: choline:oxygen 1-oxidoreductase
Comments: A flavoprotein (FAD). Also oxidizes betaine aldehyde to betaine. In many bacteria, plants and animals, betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. Different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17) [6]. The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in plants, animals and bacteria. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156, glycine/sarcosine N-methyltransferase and EC 2.1.1.157, sarcosine/dimethylglycine N-methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 9028-67-5
References:
1. Ikuta, S., Imamura, S., Misaki, H. and Horiuti, Y. Purification and characterization of choline oxidase from Arthrobacter globiformis. J. Biochem. (Tokyo) 82 (1977) 1741-1749. [PMID: 599154]
2. Rozwadowski, K.L., Khachatourians, G.G. and Selvaraj, G. Choline oxidase, a catabolic enzyme in Arthrobacter pascens, facilitates adaptation to osmotic stress in Escherichia coli. J. Bacteriol. 173 (1991) 472-478. [PMID: 1987142]
3. Rand, T., Halkier, T. and Hansen, O.C. Structural characterization and mapping of the covalently linked FAD cofactor in choline oxidase from Arthrobacter globiformis. Biochemistry 42 (2003) 7188-7194. [PMID: 12795615]
4. Gadda, G., Powell, N.L. and Menon, P. The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase. Arch. Biochem. Biophys. 430 (2004) 264-273. [PMID: 15369826]
5. Fan, F. and Gadda, G. On the catalytic mechanism of choline oxidase. J. Am. Chem. Soc. 127 (2005) 2067-2074. [PMID: 15713082]
6. Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932-4942. [PMID: 12466265]
[EC 1.1.3.25 Transferred entry: now included with EC 1.1.99.18, cellobiose dehydrogenase (acceptor) (EC 1.1.3.25 created 1986, deleted 2005)]
Common name: choline dehydrogenase
Reaction: choline + acceptor = betaine aldehyde + reduced acceptor
Glossary: betaine aldehyde = N,N,N-trimethyl-2-oxoethylammonium
choline = (2-hydroxyethyl)trimethylammonium
Other name(s): choline oxidase; choline-cytochrome c reductase; choline:(acceptor) oxidoreductase
Systematic name: choline:(acceptor) 1-oxidoreductase
Comments: A quinoprotein. In many bacteria, plants and animals, betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. Different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17) [4]. The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in plants, animals and bacteria. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156, glycine/sarcosine N-methyltransferase and EC 2.1.1.157, sarcosine/dimethylglycine N-methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 9028-67-5
References:
1. Ameyama, M., Shinagawa, E., Matsuchita, K., Takimoto, K., Nakashima, K. and Adachi, O. Mammalian choline dehydrogenase is a quinoprotein. Agric. Biol. Chem. 49 (1985) 3623-3626.
2. Ebisuzaki, K. and Williams, J.N. Preparation and partial purification of soluble choline dehydrogenase from liver mitochondria. Biochem. J. 60 (1955) 644-646. [PMID: 13249959]
3. Gadda, G. and McAllister-Wilkins, E.E. Cloning, expression, and purification of choline dehydrogenase from the moderate halophile Halomonas elongata. Appl. Environ. Microbiol. 69 (2003) 2126-2132. [PMID: 12676692]
4. Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932-4942. [PMID: 12466265]
Common name: cellobiose dehydrogenase (acceptor)
Reaction: cellobiose + acceptor = cellobiono-1,5-lactone + reduced acceptor
Other name(s): cellobiose dehydrogenase; cellobiose oxidoreductase; Phanerochaete chrysosporium cellobiose oxidoreductase; CBOR; cellobiose oxidase; cellobiose:oxygen 1-oxidoreductase; CDH
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. The enzyme from the white rot fungus Phanerochaete chrysosporium is unusual in having two redoxin domains, one containing a flavin and the other a protoheme group. It transfers reducing equivalents from cellobiose to two types of redox acceptor: two-electron oxidants, including redox dyes, benzoquinones and molecular oxygen and one-electron oxidants, including semiquinone species, iron(II) complexes and the model acceptor cytochrome c [9].
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, PDB, 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. [PMID: 8392950]
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]
7. Ayers, A.R., Ayers, S.B. and Eriksson, K.-E. Cellobiose oxidase, purification and partial characterization of a hemoprotein from Sporotrichum pulverulentum. Eur. J. Biochem. 90 (1978) 171-181. [PMID: 710416]
8. Ayers, A.R. and Eriksson, K.-E. Cellobiose oxidase from Sporotrichum pulverulentum. Methods Enzymol. 89 (1982) 129-135. [PMID: 7144569]
9. Mason, M.G., Nicholls, P., Divne, C., Hallberg, B.M., Henriksson, G. and Wilson, M.T. The heme domain of cellobiose oxidoreductase: a one-electron reducing system. Biochim. Biophys. Acta 1604 (2003) 47-54. [PMID: 12686420]
Common name: betaine-aldehyde dehydrogenase
Reaction: betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
Glossary: betaine = N,N,N-trimethylglycine
betaine aldehyde = N,N,N-trimethyl-2-oxoethylammonium
Other name(s): betaine aldehyde oxidase; BADH; betaine aldehyde dehydrogenase; BetB
Systematic name: betaine-aldehyde:NAD+ oxidoreductase
Comments: In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17) [5]. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156, glycine/sarcosine N-methyltransferase and EC 2.1.1.157, sarcosine/dimethylglycine N-methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, PDB, CAS registry number: 9028-90-4
References:
1. Rothschild, H.A. and Barron, E.S.G. The oxidation of betaine aldehyde by betaine aldehyde dehydrogenase. J. Biol. Chem. 209 (1954) 511-523. [PMID: 13192104]
2. Livingstone, J.R., Maruo, T., Yoshida, I., Tarui, Y., Hirooka, K., Yamamoto, Y., Tsutui, N. and Hirasawa, E. Purification and properties of betaine aldehyde dehydrogenase from Avena sativa. J. Plant Res. 116 (2003) 133-140. [PMID: 12736784]
3. Muñoz-Clares, R.A., González-Segura, L., Mújica-Jiménez, C. and Contreras-Diaz, L. Ligand-induced conformational changes of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa and Amaranthus hypochondriacus L. leaves affecting the reactivity of the catalytic thiol. Chem. Biol. Interact. 143-144 (2003) 129-137. [PMID: 12604197]
4. Johansson, K., El-Ahmad, M., Ramaswamy, S., Hjelmqvist, L., Jornvall, H. and Eklund, H. Structure of betaine aldehyde dehydrogenase at 2.1 Å resolution. Protein Sci. 7 (1998) 2106-2117. [PMID: 9792097]
5. Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932-4942. [PMID: 12466265]
Common name: 2-oxoglutarate synthase
Reaction: 2-oxoglutarate + CoA + 2 oxidized ferredoxin = succinyl-CoA + CO2 + 2 reduced ferredoxin
Other name(s): 2-ketoglutarate ferredoxin oxidoreductase; 2-oxoglutarate:ferredoxin oxidoreductase; KGOR; 2-oxoglutarate ferredoxin oxidoreductase; 2-oxoglutarate:ferredoxin 2-oxidoreductase (CoA-succinylating)
Systematic name: 2-oxoglutarate:ferredoxin oxidoreductase (decarboxylating)
Comments: This enzyme is one of four 2-oxoacid oxidoreductases that are differentiated by their abilities to oxidatively decarboxylate different 2-oxoacids and form their CoA derivatives (see also EC 1.2.7.1, pyruvate synthase, EC 1.2.7.7, 2-oxoisovalerate ferredoxin reductase and EC 1.2.7.8, indolepyruvate ferredoxin oxidoreductase) [3]. Contains thiamine diphosphate and 2 [4Fe-4S] clusters. Highly specific for 2-oxoglutarate.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 37251-05-1
References:
1. Buchanan, B.B. and Evans, M.C.W. The synthesis of α-ketoglutarate from succinate and carbon dioxide by a subcellular preparation of a photosynthetic bacterium. Proc. Natl Acad. Sci. USA 54 (1965) 1212-1218. [PMID: 4286833]
2. Gehring, U. and Arnon, D.I. Purification and properties of α-ketoglutarate synthase from a photosynthetic bacterium. J. Biol. Chem. 247 (1972) 6963-6969. [PMID: 4628267]
3. Dorner, E. and Boll, M. Properties of 2-oxoglutarate:ferredoxin oxidoreductase from Thauera aromatica and its role in enzymatic reduction of the aromatic ring. J. Bacteriol. 184 (2002) 3975-3983. [PMID: 12081970]
4. Mai, X. and Adams, M.W. Characterization of a fourth type of 2-keto acid-oxidizing enzyme from a hyperthermophilic archaeon: 2-ketoglutarate ferredoxin oxidoreductase from Thermococcus litoralis. J. Bacteriol. 178 (1996) 5890-5896. [PMID: 8830683]
5. Schut, G.J., Menon, A.L. and Adams, M.W.W. 2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis. Methods Enzymol. 331 (2001) 144-158. [PMID: 11265457]
[EC 1.2.7.9 Deleted entry: This enzyme is identical to EC 1.2.7.3, 2-oxoglutarate synthase (EC 1.2.7.9 created 2003, deleted 2005)]
Common name: aspartate dehydrogenase
Reaction: L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H + H+
Other name(s): NAD-dependent aspartate dehydrogenase; NADH2-dependent aspartate dehydrogenase; NADP+-dependent aspartate dehydrogenase
Systematic name: L-aspartate:NAD(P)+ oxidoreductase (deaminating)
Comments: The enzyme is strictly specific for L-aspartate as substrate. Catalyses the first step in NAD biosynthesis from aspartate. The enzyme has a higher affinity for NAD+ than NADP+ [1].
Links to other databases: CAS registry number: 37278-97-0
References:
1. Yang, Z., Savchenko, A., Yakunin, A., Zhang, R., Edwards, A., Arrowsmith, C. and Tong, L. Aspartate dehydrogenase, a novel enzyme identified from structural and functional studies of TM1643. J. Biol. Chem. 278 (2003) 8804-8808. [PMID: 12496312]
2. Okamura, T., Noda, H., Fukuda, S. and Ohsugi, M. Aspartate dehydrogenase in vitamin B12-producing Klebsiella pneumoniae IFO 13541. J. Nutr. Sci. Vitaminol. (Tokyo) 44 (1998) 483-490. [PMID: 9819709]
3. Kretovich, W.L., Kariakina, T.I., Weinova, M.K., Sidelnikova, L.I. and Kazakova, O.W. The synthesis of aspartic acid in Rhizobium lupini bacteroids. Plant Soil 61 (1981) 145-156.
Common name: sulfiredoxin
Reaction: peroxiredoxin-(S-hydroxy-S-oxocysteine) + ATP + 2 R-SH = peroxiredoxin-(S-hydroxycysteine) + ADP + phosphate + R-S-S-R
Other name(s): Srx1; sulphiredoxin; peroxiredoxin-(S-hydroxy-S-oxocysteine) reductase
Systematic name: peroxiredoxin-(S-hydroxy-S-oxocysteine):thiol oxidoreductase [ATP-hydrolysing; peroxiredoxin-(S-hydroxycysteine)-forming]
Comments: In the course of the reaction of EC 1.11.1.15, peroxiredoxin, its cysteine residue is alternately oxidized to the sulfenic acid, S-hydroxycysteine, and reduced back to cysteine. Occasionally the S-hydroxycysteine residue is further oxidized to the sulfinic acid S-hydroxy-S-oxocysteine, thereby inactivating the enzyme. The reductase provides a mechanism for regenerating the active form of peroxiredoxin, i.e. the peroxiredoxin-(S-hydroxycysteine) form. Apparently the reductase first catalyses the phosphorylation of the -S(O)-OH group by ATP to give -S(O)-O-P, which is attached to the peroxiredoxin by a cysteine residue, forming an -S(O)-S- link between the two enzymes. Attack by a thiol splits this bond, leaving the peroxiredoxin as the sulfenic acid and the reductase as the thiol.
References:
1. Biteau, B., Labarre, J. and Toledano, M.B. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 425 (2003) 980-984. [PMID: 14586471]
2. Chang, T.S., Jeong, W., Woo, H.A., Lee, S.M., Park, S. and Rhee, S.G. Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine. J. Biol. Chem. 279 (2004) 50994-51001. [PMID: 15448164]
3. Woo, H.A., Jeong, W., Chang, T.S., Park, K.J., Park, S.J., Yang, J.S. and Rhee, S.G. Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-Cys peroxiredoxins. J. Biol. Chem. 280 (2005) 3125-3128. [PMID: 15590625]
Common name: tyrosine N-monooxygenase
Reaction: (1) L-tyrosine + O2 + NADPH + H+ = N-hydroxy-L-tyrosine + NADP+ + H2O
(2) N-hydroxy-L-tyrosine + O2 + NADPH + H+ = N,N-dihydroxy-L-tyrosine + NADP+ + H2O
(3) N,N-dihydroxy-L-tyrosine = (Z)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O
For diagram click here.
Other name(s): tyrosine N-hydroxylase; CYP79A1
Systematic name: L-tyrosine,NADPH:oxygen oxidoreductase (N-hydroxylating)
Comments: A heme-thiolate protein (P-450). This enzyme is involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum, along with EC 1.14.13.68, 4-hydroxyphenylacetaldehyde oxime monooxygenase and EC 2.4.1.85, cyanohydrin β-glucosyltransferase. Some 2-(4-hydroxyphenyl)-1-nitroethane is formed as a side product.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 112692-57-6
References:
1. Halkier, B.A. and Møller, B.L. The biosynthesis of cyanogenic glucosides in higher plants. Identification of three hydroxylation steps in the biosynthesis of dhurrin in Sorghum bicolor (L.) Moench and the involvement of 1-ACI-nitro-2-(p-hydroxyphenyl)ethane as an intermediate. J. Biol. Chem. 265 (1990) 21114-21121. [PMID: 2250015]
2. Sibbesen, O., Koch, B., Halkier, B.A. and Møller, B.L. Cytochrome P-450TYR is a multifunctional heme-thiolate enzyme catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench. J. Biol. Chem. 270 (1995) 3506-3511. [PMID: 7876084]
3. Bak, S., Olsen, C.E., Halkier, B.A. and Møller, B.L. Transgenic tobacco and Arabidopsis plants expressing the two multifunctional sorghum cytochrome P450 enzymes, CYP79A1 and CYP71E1, are cyanogenic and accumulate metabolites derived from intermediates in dhurrin biosynthesis. Plant Physiol. 123 (2000) 1437-1448. [PMID: 10938360]
4. Nielsen, J.S. and Møller, B.L. Cloning and expression of cytochrome P450 enzymes catalyzing the conversion of tyrosine to p-hydroxyphenylacetaldoxime in the biosynthesis of cyanogenic glucosides in Triglochin maritima. Plant Physiol. 122 (2000) 1311-1321. [PMID: 10759528]
5. Busk, P.K. and Møller, B.L. Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants. Plant Physiol. 129 (2002) 1222-1231. [PMID: 12114576]
6. Kristensen, C., Morant, M., Olsen, C.E., Ekstrøm, C.T., Galbraith, D.W., Møller, B.L. and Bak, S. Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome. Proc. Natl. Acad. Sci. USA 102 (2005) 1779-1784. [PMID: 15665094]
Common name: pentachlorophenol monooxygenase
Reaction: (1) pentachlorophenol + 2 NADPH + H+ + O2 = 2,3,5,6-tetrachlorohydroquinone + 2 NADP+ + chloride + H2O
(2) 2,3,5,6-tetrachlorophenol + NADPH + H+ + O2 = 2,3,5,6-tetrachlorohydroquinone + NADP+ + H2O
Other name(s): pentachlorophenol dechlorinase; pentachlorophenol dehalogenase; pentachlorophenol 4-monooxygenase; PCP hydroxylase; pentachlorophenol hydroxylase; PcpB; PCB 4-monooxygenase; PCB4MO
Systematic name: pentachlorophenol,NADPH:oxygen oxidoreductase (hydroxylating, dechlorinating)
Comments: A flavoprotein (FAD). The enzyme displaces a diverse range of substituents from the 4-position of polyhalogenated phenols but requires that a halogen substituent be present at the 2-position [2]. The enzyme converts many polyhalogenated phenols into hydroquinones, and requires that a halogen substituent be present at C-2 [2]. If C-4 carries a halogen substituent, reaction 1 is catalysed, e.g. 2,4,6-triiodophenol is oxidized to 2,6-diiodohydroquinone; if C-4 is unsubstituted, reaction 2 is catalysed.
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, ERGO, CAS registry number: 124148-88-5 and 136111-57-4
References:
1. Schenk, T., Müller, R., Mörsberger, F., Otto, M.K. and Lingens, F. Enzymatic dehalogenation of pentachlorophenol by extracts from Arthrobacter sp. strain ATCC 33790. J. Bacteriol. 171 (1989) 5487-5491. [PMID: 2793827]
2. Xun, L., Topp, E. and Orser, C.S. Diverse substrate range of a Flavobacterium pentachlorophenol hydroxylase and reaction stoichiometries. J. Bacteriol. 174 (1992) 2898-2902. [PMID: 1569020]
3. Xun, L., Topp, E. and Orser, C.S. Confirmation of oxidative dehalogenation of pentachlorophenol by a Flavobacterium pentachlorophenol hydroxylase. J. Bacteriol 174 (1992) 5745-5747. [PMID: 1512208]
4. Lange, C.C., Schneider, B.J. and Orser, C.S. Verification of the role of PCP 4-monooxygenase in chlorine elimination from pentachlorophenol by Flavobacterium sp. strain ATCC 39723. Biochem. Biophys. Res. Commun. 219 (1996) 146-149. [PMID: 8619798]
5. Nakamura, T., Motoyama, T., Hirono, S. and Yamaguchi, I. Identification, characterization, and site-directed mutagenesis of recombinant pentachlorophenol 4-monooxygenase. Biochim. Biophys. Acta 1700 (2004) 151-159. [PMID: 15262224]
Common name: 4-hydroxyphenylacetaldehyde oxime monooxygenase
Reaction: (Z)-4-hydroxyphenylacetaldehyde oxime + NADPH + H+ + O2 = (S)-4-hydroxymandelonitrile + NADP+ + 2 H2O
For diagram click here.
Other name(s): 4-hydroxybenzeneacetaldehyde oxime monooxygenase; cytochrome P450II-dependent monooxygenase; NADPH-cytochrome P450 reductase (CYP71E1); CYP71E1; 4-hydroxyphenylacetaldehyde oxime,NADPH:oxygen oxidoreductase
Systematic name: (Z)-4-hydroxyphenylacetaldehyde oxime,NADPH:oxygen oxidoreductase
Comments: This enzyme is involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum, along with EC 1.14.13.41, tyrosine N-monooxygenase and EC 2.4.1.85, cyanohydrin β-glucosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number:
References:
1. MacFarlane, I.J., Lees, E.M. and Conn, E.E. The in vitro biosynthesis of dhurrin, the cyanogenic glycoside of Sorghum bicolor. J. Biol. Chem. 250 (1975) 4708-4713. [PMID: 237909]
2. Shimada, M. and Conn, E.E. The enzymatic conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile Arch. Biochem. Biophys. 180 (1977) 199-207. [PMID: 193443]
3. Busk, P.K. and Møller, B.L. Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants. Plant Physiol. 129 (2002) 1222-1231. [PMID: 12114576]
4. Kristensen, C., Morant, M., Olsen, C.E., Ekstrøm, C.T., Galbraith, D.W., Møller, B.L. and Bak, S. Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome. Proc. Natl. Acad. Sci. USA 102 (2005) 1779-1784. [PMID: 15665094]
Common name: choline monooxygenase
Reaction: choline + O2 + 2 reduced ferredoxin + 2 H+ = betaine aldehyde hydrate + H2O + 2 oxidized ferredoxin
Glossary: betaine = N,N,N-trimethylammonioacetate
betaine aldehyde = N,N,N-trimethyl-2-oxoethylammonium
choline = (2-hydroxyethyl)trimethylammonium
Systematic name: choline,reduced-ferredoxin:oxygen oxidoreductase
Comments: The spinach enzyme, which is located in the chloroplast, contains a Rieske-type [2Fe-2S] cluster, and probably also a mononuclear Fe centre. Requires Mg2+. Catalyses the first step of glycine betaine synthesis. In many bacteria, plants and animals, betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. Different enzymes are involved in the first reaction. In plants, the reaction is catalysed by this enzyme whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17) [7]. The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in plants, animals and bacteria. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156, glycine/sarcosine N-methyltransferase and EC 2.1.1.157, sarcosine/dimethylglycine N-methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number:
References:
1. Brouquisse, R., Weigel, P., Rhodes, D., Yocum, C.F. and Hanson, A.D. Evidence for a ferredoxin-dependent choline monooxygenase from spinach chloroplast stroma. Plant Physiol. 90 (1989) 322-329.
2. Burnet, M., Lafontaine, P.J. and Hanson, A.D. Assay, purification, and partial characterization of choline monooxygenase from spinach. Plant Physiol. 108 (1995) 581-588. [PMID: 12228495]
3. Rathinasabapathi, B., Burnet, M., Russell, B.L., Gage, D.A., Liao, P., Nye, G.J., Scott, P., Golbeck, J.H. and Hanson, A.D. Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: Prosthetic group characterization and cDNA cloning. Proc. Natl. Acad. Sci. USA 94 (1997) 3454-3458. [PMID: 9096415]
4. Russell, B.L., Rathinasabapathi, B. and Hanson, A.D. Osmotic stress induces expression of choline monooxygenase in sugar beet and amaranth. Plant Physiol. 116 (1998) 859-865. [PMID: 9489025]
5. Nuccio, M.L., Russell, B.L., Nolte, K.D., Rathinasabapathi, B., Gage, D.A. and Hanson, A.D. Glycine betaine synthesis in transgenic tobacco expressing choline monooxygenase is limited by the endogenous choline supply. Plant J. 16 (1998) 101-110.
6. Nuccio, M.L., Russell, B.L., Nolte, K.D., Rathinasabapathi, B., Gage, D.A. and Hanson, A.D. The endogenous choline supply limits glycine betaine synthesis in transgenic tobacco expressing choline. Plant J. 16 (1998) 487-496. [PMID: 9881168]
7. Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932-4942. [PMID: 12466265]
Common name: glycine N-methyltransferase
Reaction: S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine
Glossary: sarcosine = N-methylglycine
Other name(s): glycine methyltransferase; S-adenosyl-L-methionine:glycine methyltransferase; GNMT
Systematic name: S-adenosyl-L-methionine:glycine N-methyltransferase
Comments: This enzyme is thought to play an important role in the regulation of methyl group metabolism in the liver and pancreas by regulating the ratio between S-adenosyl-L-methionine and S-adenosyl-L-homocysteine. It is inhibited by 5-methyltetrahydrofolate pentaglutamate [4]. Sarcosine, which has no physiological role, is converted back into glycine by the action of EC 1.5.99.1, sarcosine dehydrogenase.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, PDB, CAS registry number: 37228-72-1
References:
1. Blumenstein, J. and Williams, G.R. Glycine methyltransferase. Can. J. Biochem. Physiol. 41 (1963) 201-210. [PMID: 13971907]
2. Ogawa, H., Gomi, T., Takusagawa, F. and Fujioka, M. Structure, function and physiological role of glycine N-methyltransferase. Int. J. Biochem. Cell Biol. 30 (1998) 13-26. [PMID: 9597750]
3. Yeo, E.J., Briggs, W.T. and Wagner, C. Inhibition of glycine N-methyltransferase by 5-methyltetrahydrofolate pentaglutamate. J. Biol. Chem. 274 (1999) 37559-37564. [PMID: 10608809]
4. Martinov, M.V., Vitvitsky, V.M., Mosharov, E.V., Banerjee, R. and Ataullakhanov, F.I. A substrate switch: a new mode of regulation in the methionine metabolic pathway. J. Theor. Biol. 204 (2000) 521-532. [PMID: 10833353]
5. Takata, Y., Huang, Y., Komoto, J., Yamada, T., Konishi, K., Ogawa, H., Gomi, T., Fujioka, M. and Takusagawa, F. Catalytic mechanism of glycine N-methyltransferase. Biochemistry 42 (2003) 8394-8402. [PMID: 12859184]
6. Pakhomova, S., Luka, Z., Grohmann, S., Wagner, C. and Newcomer, M.E. Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes. Proteins 57 (2004) 331-337. [PMID: 15340920]
Common name: glycine/sarcosine N-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine
(2) S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine + N,N-dimethylglycine
Glossary: sarcosine = N-methylglycine
Other name(s): ApGSMT; glycine-sarcosine methyltransferase; GSMT; GMT; glycine sarcosine N-methyltransferase
Systematic name: S-adenosyl-L-methionine:sarcosine N-methyltransferase
Comments: Cells of the oxygen-evolving halotolerant cyanobacterium Aphanocthece halophytica synthesize betaine from glycine by a three-step methylation process. This is the first enzyme and it leads to the formation of either sarcosine or N,N-dimethylglycine, which is further methylated to yield betaine (N,N,N-trimethylglycine) by the action of EC 2.1.1.157, sarcosine/dimethylglycine N-methyltransferase. Differs from EC 2.1.1.20, glycine N-methyltransferase, as it can further methylate the product of the first reaction. Acetate, dimethylglycine and S-adenosyl-L-homocysteine can inhibit the reaction [3].
References:
1. Nyyssölä, A., Kerovuo, J., Kaukinen, P., von Weymarn, N. and Reinikainen, T. Extreme halophiles synthesize betaine from glycine by methylation. J. Biol. Chem. 275 (2000) 22196-22201. [PMID: 10896953]
2. Nyyssölä, A., Reinikainen, T. and Leisola, M. Characterization of glycine sarcosine N-methyltransferase and sarcosine dimethylglycine N-methyltransferase. Appl. Environ. Microbiol. 67 (2001) 2044-2050. [PMID: 11319079]
3. Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932-4942. [PMID: 12466265]
Common name: sarcosine/dimethylglycine N-methyltransferase
Reaction: (1) S-adenosyl-L-methionine + sarcosine = S-adenosyl-L-homocysteine + N,N-dimethylglycine
(2) S-adenosyl-L-methionine + N,N-dimethylglycine = S-adenosyl-L-homocysteine + betaine
Glossary: sarcosine = N-methylglycine
betaine = N,N,N-trimethylglycine
Other name(s): ApDMT; sarcosine-dimethylglycine methyltransferase; SDMT; sarcosine dimethylglycine N-methyltransferase
Systematic name: S-adenosyl-L-methionine:N,N-dimethylglycine N-methyltransferase
Comments: Cells of the oxygen-evolving halotolerant cyanobacterium Aphanocthece halophytica synthesize betaine from glycine by a three-step methylation process. The first enzyme, EC 2.1.1.156, glycine/sarcosine N-methyltransferase, leads to the formation of either sarcosine or N,N-dimethylglycine, which is further methylated to yield betaine (N,N,N-trimethylglycine) by the action of this enzyme. Both of these enzymes can catalyse the formation of N,N-dimethylglycine from sarcosine [3]. The reactions are strongly inhibited by S-adenosyl-L-homocysteine.
References:
1. Nyyssölä, A., Kerovuo, J., Kaukinen, P., von Weymarn, N. and Reinikainen, T. Extreme halophiles synthesize betaine from glycine by methylation. J. Biol. Chem. 275 (2000) 22196-22201. [PMID: 10896953]
2. Nyyssölä, A., Reinikainen, T. and Leisola, M. Characterization of glycine sarcosine N-methyltransferase and sarcosine dimethylglycine N-methyltransferase. Appl. Environ. Microbiol. 67 (2001) 2044-2050. [PMID: 11319079]
3. Waditee, R., Tanaka, Y., Aoki, K., Hibino, T., Jikuya, H., Takano, J., Takabe, T. and Takabe, T. Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica. J. Biol. Chem. 278 (2003) 4932-4942. [PMID: 12466265]
Common name: N-acetylornithine carbamoyltransferase
Reaction: carbamoyl phosphate + N2-acetyl-L-ornithine = phosphate + N-acetyl-L-citrulline
Glossary: N-acetyl-L-citrulline = N5-acetylcarbamoyl-L-ornithine
Other name(s): acetylornithine transcarbamylase; N-acetylornithine transcarbamylase; AOTC
Systematic name: carbamoyl-phosphate:N2-acetyl-L-ornithine carbamoyltransferase
Comments: Differs from EC 2.1.3.3, ornithine carbamoyltransferase. This enzyme replaces EC 2.1.3.3 in the canonic arginine biosynthetic pathway of several Eubacteria and has no catalytic activity with L-ornithine as substrate.
References:
1. Shi, D., Morizono, H., Yu, X., Roth, L., Caldovic, L., Allewell, N.M., Malamy, M.H. and Tuchman, M. Crystal structure of N-acetylornithine transcarbamylase from Xanthomonas campestris: a novel enzyme in a new arginine biosynthetic pathway found in several Eubacteria. J. Biol. Chem. 280 (2005) 14366-14369. [PMID: 15731101]
Common name: cyanohydrin β-glucosyltransferase
Reaction: UDP-D-glucose + (S)-4-hydroxymandelonitrile = UDP + (S)-4-hydroxymandelonitrile β-D-glucoside
For diagram click here.
Glossary: (S)-4-hydroxymandelonitrile β-D-glucoside = dhurrin
Other name(s): uridine diphosphoglucose-p-hydroxymandelonitrile glucosyltransferase; UDP-glucose-p-hydroxymandelonitrile glucosyltransferase; uridine diphosphoglucose-cyanohydrin glucosyltransferase; uridine diphosphoglucose:aldehyde cyanohydrin β-glucosyltransferase; UDP-glucose:(S)-4-hydroxymandelonitrile β-D-glucosyltransferase; UGT85B1; UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase
Systematic name: UDP-D-glucose:(S)-4-hydroxymandelonitrile β-D-glucosyltransferase
Comments: Acts on a wide range of substrates in vitro, including cyanohydrins, terpenoids, phenolics, hexanol derivatives and plant hormones, in a regiospecific manner [3]. This enzyme is involved in the biosynthesis of the cyanogenic glucoside dhurrin in sorghum, along with EC 1.14.13.41, tyrosine N-monooxygenase and EC 1.14.13.68, 4-hydroxyphenylacetaldehyde oxime monooxygenase. This reaction prevents the disocciation and release of toxic hydrogen cyanide [3].
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 55354-52-4
References:
1. Reay, P.F. and Conn, E.E. The purification and properties of a uridine diphosphate glucose: aldehyde cyanohydrin β-glucosyltransferase from sorghum seedlings. J. Biol. Chem. 249 (1974) 5826-5830. [PMID: 4416442]
2. Jones, P.R., Møller, B.L. and Hoj, P.B. The UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase that catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor. Isolation, cloning, heterologous expression, and substrate specificity. J. Biol. Chem. 274 (1999) 35483-35491. [PMID: 10585420]
3. Hansen, K.S., Kristensen, C., Tattersall, D.B., Jones, P.R., Olsen, C.E., Bak, S. and Møller, B.L. The in vitro substrate regiospecificity of recombinant UGT85B1, the cyanohydrin glucosyltransferase from Sorghum bicolor. Phytochemistry 64 (2003) 143-151. [PMID: 12946413]
4. Busk, P.K. and Møller, B.L. Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants. Plant Physiol. 129 (2002) 1222-1231. [PMID: 12114576]
5. Kristensen, C., Morant, M., Olsen, C.E., Ekstrøm, C.T., Galbraith, D.W., Møller, B.L. and Bak, S. Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome. Proc. Natl. Acad. Sci. USA 102 (2005) 1779-1784. [PMID: 15665094]
Common name: anthocyanidin 3-O-glucosyltransferase
Reaction: UDP-D-glucose + an anthocyanidin = UDP + an anthocyanidin-3-O-β-D-glucoside
For diagram click here.
Other name(s): uridine diphosphoglucose-anthocyanidin 3-O-glucosyltransferase; UDP-glucose:anthocyanidin/flavonol 3-O-glucosyltransferase; UDP-glucose:cyanidin-3-O-glucosyltransferase; UDP-glucose:anthocyanidin 3-O-D-glucosyltransferase; 3-GT
Systematic name: UDP-D-glucose:anthocyanidin 3-O-β-D-glucosyltransferase
Comments: The anthocyanidin compounds cyanidin, delphinidin, peonidin and to a lesser extent pelargonidin can act as substrates. The enzyme does not catalyse glucosylation of the 5-position of cyanidin and does not act on flavanols such as quercetin and kaempferol (cf. EC 2.4.1.91 flavonol 3-O-glucosyltransferase). In conjunction with EC 1.14.11.19, leucocyanidin oxygenase, it is involved in the conversion of leucoanthocyanidin into anthocyanidin 3-glucoside. It may act on the pseudobase precursor of the anthocyanidin rather than on the anthocyanidin itself [3].
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 65607-32-1
References:
1. Kamsteeg, J., van Brederode, J. and van Nigtevecht, G. Identification and properties of UDP-glucose: cyanidin-3-O-glucosyltransferase isolated from petals of the red campion (Silene dioica). Biochem. Genet. 16 (1978) 1045-1058. [PMID: 751640]
2. Ford, C.M., Boss, P.K. and Høj, P.B. Cloning and characterization of Vitis vinifera UDP-glucose:flavonoid 3-O-glucosyltransferase, a homologue of the enzyme encoded by the maize Bronze-1 locus that may primarily serve to glucosylate anthocyanidins in vivo. J. Biol. Chem. 273 (1998) 9224-9233. [PMID: 9535914]
3. Nakajima, J., Tanaka, Y., Yamazaki, M. and Saito, K. Reaction mechanism from leucoanthocyanidin to anthocyanidin 3-glucoside, a key reaction for coloring in anthocyanin biosynthesis. J. Biol. Chem. 276 (2001) 25797-25803. [PMID: 11316805]
[EC 2.4.1.233 Deleted entry: anthocyanidin 3-O-glucosyltransferase. The enzyme is identical to EC 2.4.1.115, anthocyanidin 3-O-glucosyltransferase (EC 2.4.1.233 created 2004, deleted 2005)]
Common name: cephalosporin-C transaminase
Reaction: (7R)-7-(5-carboxy-5-oxopentanoyl)aminocephalosporinate + D-glutamate = cephalosporin C + 2-oxoglutarate
For diagram click here.
Glossary: cephalosporin C = (7R)-7-(5-carboxy-5-oxopentanamido)cephalosporanate
Other name(s): cephalosporin C aminotransferase; L-alanine:cephalosporin-C aminotransferase
Systematic name: cephalosporin-C:2-oxoglutarate aminotransferase
Comments: A number of D-amino acids, including D-alanine, D-aspartate and D-methionine can also act as amino-group donors. Although this enzyme acts on several free D-amino acids, it differs from EC 2.6.1.21, D-amino acid transaminase, in that it can use cephalosporin C as an amino donor.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 122096-91-7
References:
1. Aretz, W. and Sauber, K. Novel D-amino acid transaminase. Ann. N.Y. Acad. Sci. 542 (1988) 366-370. [PMID: 3228235]
Common name: N-acetylgalactosamine kinase
Reaction: ATP + N-acetyl-D-galactosamine = ADP + N-acetyl-α-D-galactosamine 1-phosphate
Other name(s): GALK2; GK2; GalNAc kinase; N-acetylgalactosamine (GalNAc)-1-phosphate kinase
Systematic name: ATP:N-acetyl-D-galactosamine 1-phosphotransferase
Comments: The enzyme is highly specific for GalNAc as substrate, but has slight activity with D-galactose [2]. Requires Mg2+, Mn2+ or Co2+ for activity, with Mg2+ resulting in by far the greatest stimulation of enzyme activity.
References:
1. Pastuszak, I., Drake, R. and Elbein, A.D. Kidney N-acetylgalactosamine (GalNAc)-1-phosphate kinase, a new pathway of GalNAc activation. J. Biol. Chem. 271 (1999) 20776-20782. [PMID: 8702831]
2. Pastuszak, I., O'Donnell, J. and Elbein, A.D. Identification of the GalNAc kinase amino acid sequence. J. Biol. Chem. 271 (1996) 23653-23656. [PMID: 8798585]
3. Thoden, J.B. and Holden, H.M. The molecular architecture of human N-acetylgalactosamine kinase. J. Biol. Chem. (2005) in press [PMID: 16006554]
Common name: acetate kinase
Reaction: (1) ATP + acetate = ADP + acetyl phosphate
(2) ATP + propanoate = ADP + propanoyl phosphate
Other name(s): acetokinase; AckA; AK; acetic kinase; acetate kinase (phosphorylating)
Systematic name: ATP:acetate phosphotransferase
Comments: Requires Mg2+ for activity. While purified enzyme from Escherichia coli is specific for acetate [4], others have found that the enzyme can also use propanoate as a substrate, but more slowly [7]. Acetate can be converted into the key metabolic intermediate acetyl-CoA by coupling acetate kinase with EC 2.3.1.8, phosphate acetyltransferase. Both this enzyme and EC 2.7.2.15, propionate kinase, play important roles in the production of propanoate [9].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, UM-BBD, ERGO, PDB, CAS registry number: 9027-42-3
References:
1. Romain, Y., Demassieux, S. and Carriere, S. Partial purification and characterization of two isoenzymes involved in the sulfurylation of catecholamines. Biochem. Biophys. Res. Commun. 106 (1982) 999-1005. [PMID: 6956338]
2. Romano, A.H. and Nickerson, W.J. Cystine reductase of pea seeds and yeasts. J. Biol. Chem. 208 (1954) 409-416. [PMID: 13174550]
3. Stern, J.R. and Ochoa, S. Enzymatic synthesis of citric acid. I. Synthesis with soluble enzymes. J. Biol. Chem. 191 (1951) 161-172. [PMID: 14850456]
4. Fox, D.K. and Roseman, S. Isolation and characterization of homogeneous acetate kinase from Salmonella typhimurium and Escherichia coli. J. Biol. Chem. 261 (1986) 13487-13497. [PMID: 3020034]
5. Knorr, R., Ehrmann, M.A. and Vogel, R.F. Cloning, expression, and characterization of acetate kinase from Lactobacillus sanfranciscensis. Microbiol. Res. 156 (2001) 267-277. [PMID: 11716215]
6. Buss, K.A., Cooper, D.R., Ingram-Smith, C., Ferry, J.G., Sanders, D.A. and Hasson, M.S. Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases. J. Bacteriol. 183 (2001) 680-686. [PMID: 11133963]
7. Ingram-Smith, C., Gorrell, A., Lawrence, S.H., Iyer, P., Smith, K. and Ferry, J.G. Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase. J. Bacteriol. 187 (2005) 2386-2394. [PMID: 15774882]
8. Gorrell, A., Lawrence, S.H. and Ferry, J.G. Structural and kinetic analyses of arginine residues in the active site of the acetate kinase from Methanosarcina thermophila. J. Biol. Chem. 280 (2005) 10731-10742. [PMID: 15647264]
9. Heßlinger, C., Fairhurst, S.A. and Sawers, G. Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate. Mol. Microbiol. 27 (1998) 477-492. [PMID: 9484901]
Common name: propionate kinase
Reaction: (1) ATP + propanoate = ADP + propanoyl phosphate
(2) ATP + acetate = ADP + acetyl phosphate
Other name(s): PduW; TdcD; propionate/acetate kinase
Systematic name: ATP:propanoate phosphotransferase
Comments: Requires Mg2+. Both propanoate and acetate can act as a substrate. Involved in the anaerobic degradation of L-threonine in bacteria [1]. Both this enzyme and EC 2.7.2.1, acetate kinase, play important roles in the production of propanoate [1].
References:
1. Heßlinger, C., Fairhurst, S.A. and Sawers, G. Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate. Mol. Microbiol. 27 (1998) 477-492. [PMID: 9484901]
2. Palacios, S., Starai, V.J. and Escalante-Semerena, J.C. Propionyl coenzyme A is a common intermediate in the 1,2-propanediol and propionate catabolic pathways needed for expression of the prpBCDE operon during growth of Salmonella enterica on 1,2-propanediol. J. Bacteriol. 185 (2003) 2802-2810. [PMID: 12700259]
3. Wei, Y. and Miller, C.G. Characterization of a group of anaerobically induced, fnr-dependent genes of Salmonella typhimurium. J. Bacteriol. 181 (1999) 6092-6097. [PMID: 10498722]
4. Ingram-Smith, C., Gorrell, A., Lawrence, S.H., Iyer, P., Smith, K. and Ferry, J.G. Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase. J. Bacteriol. 187 (2005) 2386-2394. [PMID: 15774882]
5. Simanshu, D.K. and Murthy M.R.N. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of propionate kinase (TdcD) from Salmonella typhimurium. Acta Crystallogr. F Struct. Biol. Cryst. Commun. 61 (2005) 52-55.
6. Simanshu, D.K., Savithri, H.S. and Murthy M.R.N. Crystal structures of ADP and AMPPNP-bound propionate kinase (TdcD) from Salmonella typhimurium: Comparison with members of acetate and sugar kinase/heat shock cognate 70/actin superfamily. J. Mol. Biol. 2005, in press.
Common name: N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase
Reaction: (1) 3'-phosphoadenylyl sulfate + dermatan = adenosine 3',5'-bisphosphate + dermatan 6'-sulfate
(2) 3'-phosphoadenylyl sulfate + chondroitin = adenosine 3',5'-bisphosphate + chondroitin 6'-sulfate
Other name(s): GalNAc4S-6ST
Systematic name: 3'-phosphoadenylyl-sulfate:dermatan 6'-sulfotransferase
Comments: The enzyme is activated by divalent cations and reduced glutathione. The enzyme from human transfers sulfate to position 6 of both internal residues and nonreducing terminal GalNAc 4-sulfate residues of chondroitin sulfate. Oligosaccharides derived from chondroitin sulfate also serve as acceptors but chondroitin sulfate E, keratan sulfate and heparan sulfate do not. Differs from EC 2.8.2.17, chondroitin 6-sulfotransferase, in being able to use both condoitin and dermatan as effective substrates
References:
1. Ito, Y. and Habuchi, O. Purification and characterization of N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase from the squid cartilage. J. Biol. Chem. 275 (2000) 34728-34736. [PMID: 10871629]
2. Ohtake, S., Ito, Y., Fukuta, M. and Habuchi, O. Human N-acetylgalactosamine 4-sulfate 6-O-sulfotransferase cDNA is related to human B cell recombination activating gene-associated gene. J. Biol. Chem. 276 (2001) 43894-43900. [PMID: 11572857]
Recommended name: rhomboid protease
Reaction: Cleaves type-1 transmembrane domains using a catalytic triad composed of serine, histidine and asparagine contributed by different transmembrane domains
Comments: These endopeptidases are multi-spanning membrane proteins. Their catalytic site is embedded within the membrane and they cleave type-1 transmembrane domains. Important for embryo development in Drosophila melanogaster. Rhomboid is a key regulator of EGF receptor signalling and is responsible for cleaving Spitz, the main ligand of the Drosophila EGF receptor pathway. Belongs in peptidase family S54. Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.
References:
1. Urban, S. and Wolfe, M.S. Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificity. Proc. Natl. Acad. Sci. USA 102 (2005) 1883-1888. [PMID: 15684070]
2. Brossier F., Jewett T., Sibley D.L. and Urban, S. A spatially-localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma. Proc. Natl. Acad. Sci. USA 102 (2005) 4146-4151. [PMID: 15753289]
3. Herlan, M., Bornhovd, C., Hell, K., Neupert, W. and Reichert, A.S. Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor. J. Cell Biol. 165 (2004) 167-173. [PMID: 15096522]
4. Pascall, J.C. and Brown, K.D. Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDL2. Biochem. Biophys. Res. Commun. 317 (2004) 244-252. [PMID: 15047175]
5. Sik, A., Passer, B.J., Koonin, E.V. and Pellegrini, L. Self-regulated cleavage of the mitochondrial intramembrane-cleaving protease PARL yields Pβ, a nuclear-targeted peptide. J. Biol. Chem. 279 (2004) 15323-15329. [PMID: 14732705]
6. Urban, S. and Freeman, M. Substrate specificity of Rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain. Mol. Cell 11 (2003) 1425-1434. [PMID: 12820957]
7. Herlan, M., Vogel, F., Bornhovd, C., Neupert, W. and Reichert, A.S. Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA. J. Biol. Chem. 278 (2003) 27781-27788. [PMID: 12707284]
8. McQuibban, G.A., Saurya, S. and Freeman, M. Mitochondrial membrane remodelling regulated by a conserved rhomboid protease. Nature 423 (2003) 537-541. [PMID: 12774122]
9. Koonin, E.V., Makarova, K.S., Rogozin, I.B., Davidovic, L., Letellier, M.C. and Pellegrini, L. The rhomboids: a nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfers. Genome Biol. 4 (2003) R19. [PMID: 12620104]
10. Urban, S. and Freeman, M. Intramembrane proteolysis controls diverse signalling pathways throughout evolution. Curr. Opin. Genet. Dev. 12 (2002) 512-518. [PMID: 12200155]
11. Urban, S., Schlieper, D. and Freeman, M. Conservation of intramembrane proteolytic activity and substrate specificity in prokaryotic and eukaryotic Rhomboids. Curr. Biol. 12 (2002) 1507-1512. [PMID: 12225666]
12. Urban, S., Lee, J.R. and Freeman, M. A family of Rhomboid intramembrane proteases activates all Drosophila membrane-tethered EGF-like ligands. EMBO J. 21 (2002) 4277-4286. [PMID: 12169630]
13. Urban, S., Lee, J.R. and Freeman, M. Drosophila Rhomboid-1 defines a family of putative intramembrane serine proteases. Cell 107 (2001) 173-182. [PMID: 11672525]
Common name: pantetheine hydrolase
Reaction: (R)-pantetheine + H2O = (R)-pantothenate + cysteamine
Other name(s): pantetheinase; vanin; vanin-1
Systematic name: (R)-pantetheine amidohydrolase
Comments: The enzyme hydrolyses only one of the amide bonds of pantetheine. The substrate analogues phosphopantetheine and CoA are not substrates. The enzyme recycles pantothenate (vitamin B5) and produces cysteamine, a potent anti-oxidant [5].
References:
1. Duprè, S. and Cavallini, D. Purification and properties of pantetheinase from horse kidney. Methods Enzymol. 62 (1979) 262-267. [PMID: 440106]
2. Duprè, S., Chiaraluce, R., Nardini, M., Cannella, C., Ricci, G. and Cavallini, D. Continuous spectrophotometric assay of pantetheinase activity. Anal. Biochem. 142 (1984) 175-181. [PMID: 6549111]
3. Maras, B., Barra, D., Duprè, S. and Pitari, G. Is pantetheinase the actual identity of mouse and human vanin-1 proteins? FEBS Lett. 461 (1999) 149-152. [PMID: 10567687]
4. Aurrand-Lions, M., Galland, F., Bazin, H., Zakharyev, V.M., Imhof, B.A. and Naquet, P. Vanin-1, a novel GPI-linked perivascular molecule involved in thymus homing. Immunity 5 (1996) 391-405. [PMID: 8934567]
5. Pitari, G., Malergue, F., Martin, F., Philippe, J.M., Massucci, M.T., Chabret, C., Maras, B., Dupre, S., Naquet, P. and Galland, F. Pantetheinase activity of membrane-bound vanin-1: lack of free cysteamine in tissues of Vanin-1 deficient mice. FEBS Lett. 483 (2000) 149-154. [PMID: 11042271]
6. Martin, F., Malergue, F., Pitari, G., Philippe, J.M., Philips, S., Chabret, C., Granjeaud, S., Mattei, M.G., Mungall, A.J., Naquet, P. and Galland, F. Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode isoforms of pantetheinase ectoenzymes. Immunogenetics 53 (2001) 296-306. [PMID: 11491533]
7. Pace, H.C. and Brenner, C. The nitrilase superfamily: classification, structure and function. Genome Biol. 2 (2001) 0001.1-001.9. [PMID: 11380987]
Common name: D-dopachrome decarboxylase
Reaction: D-dopachrome = 5,6-dihydroxyindole + CO2
Glossary: D-dopachrome = (2R)-5,6-dioxo-2,3,5,6-tetrahydro-1H-indole-2-carboxylate
Other name(s): phenylpyruvate tautomerase II; D-tautomerase; D-dopachrome tautomerase
Systematic name: D-dopachrome carboxy-lyase
Comments: This enzyme is specific for D-dopachrome as substrate and belongs to the MIF (macrophage migration inhibitory factor) family of proteins. L-Dopachrome, L- or D-α-methyldopachrome and dopaminochrome do not act as substrates (see also EC 5.3.3.12, L-dopachrome isomerase)
Links to other databases: PDB, CAS number: 184111-06-6
References:
1. Odh, G., Hindemith, A., Rosengren, A.M., Rosengren, E. and Rorsman, H. Isolation of a new tautomerase monitored by the conversion of D-dopachrome to 5,6-dihydroxyindole. Biochem. Biophys. Res. Commun. 197 (1993) 619-624. [PMID: 8267597]
2. Yoshida, H., Nishihira, J., Suzuki, M. and Hikichi, K. NMR characterization of physicochemical properties of rat D-dopachrome tautomerase. Biochem. Mol. Biol. Int. 42 (1997) 891-899. [PMID: 9285056]
3. Sugimoto, H., Taniguchi, M., Nakagawa, A., Tanaka, I., Suzuki, M. and Nishihira, J. Crystal structure of human D-dopachrome tautomerase, a homologue of macrophage migration inhibitory factor, at 1.54 Å resolution. Biochemistry 38 (1999) 3268-3279. [PMID: 10079069]
4. Nishihira, J., Fujinaga, M., Kuriyama, T., Suzuki, M., Sugimoto, H., Nakagawa, A., Tanaka, I. and Sakai, M. Molecular cloning of human D-dopachrome tautomerase cDNA: N-terminal proline is essential for enzyme activation. Biochem. Biophys. Res. Commun. 243 (1998) 538-544. [PMID: 9480844]
Common name: chondroitin B lyase
Reaction: Eliminative cleavage of dermatan sulfate containing 1,4-β-D-hexosaminyl and 1,3-β-D-glucurosonyl or 1,3-α-L-iduronosyl linkages to disaccharides containing 4-deoxy-β-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (δUA-GalNAC-4S).
Glossary: dermatan sulfate = chondroitin sulfate B
Other name(s): chondroitinase B; ChonB; ChnB
Systematic name: chondroitin B lyase
Comments: This is the only lyase that is known to be specific for dermatan sulfate as substrate. The minimum substrate length required for catalysis is a tetrasaccharide [2].
Links to other databases: CAS registry number: 52227-83-5
References:
1. Gu, K., Linhardt, R.J., Laliberte, M., Gu, K. and Zimmermann, J. Purification, characterization and specificity of chondroitin lyases and glycuronidase from Flavobacterium heparinum. Biochem. J. 312 (1995) 569-577. [PMID: 8526872]
2. Pojasek, K., Raman, R., Kiley, P., Venkataraman, G. and Sasisekharan, R. Biochemical characterization of the chondroitinase B active site. J. Biol. Chem. 277 (2000) 31179-31186. [PMID: 12063249]
3. Pojasek, K., Shriver, Z., Kiley, P., Venkataraman, G. and Sasisekharan, R. Recombinant expression, purification, and kinetic characterization of chondroitinase AC and chondroitinase B from Flavobacterium heparinum. Biochem. Biophys. Res. Commun. 286 (2001) 343-351. [PMID: 11500043]
4. Suzuki, K., Terasaki, Y. and Uyeda, M. Inhibition of hyaluronidases and chondroitinases by fatty acids. J. Enzyme Inhib. Med. Chem. 17 (2002) 183-186. [PMID: 12443044]
5. Ototani, N. and Yosizawa, Z. Purification of chondroitinase B and chondroitinase C using glycosaminoglycan-bound AH-Sepharose 4B. Carbohydr. Res. 70 (1979) 295-306. [PMID: 427837]
6. Tkalec, A.L., Fink, D., Blain, F., Zhang-Sun, G., Laliberte, M., Bennett, D.C., Gu, K., Zimmermann, J.J. and Su, H. Isolation and expression in Escherichia coli of cslA and cslB, genes coding for the chondroitin sulfate-degrading enzymes chondroitinase AC and chondroitinase B, respectively, from Flavobacterium heparinum. Appl. Environ. Microbiol. 66 (2000) 29-35. [PMID: 10618199]
7. Michel, G., Pojasek, K., Li, Y., Sulea, T., Linhardt, R.J., Raman, R., Prabhakar, V., Sasisekharan, R. and Cygler, M. The structure of chondroitin B lyase complexed with glycosaminoglycan oligosaccharides unravels a calcium-dependent catalytic machinery. J. Biol. Chem. 279 (2004) 32882-32896. [PMID: 15155751]
8. Li, Y., Matte, A., Su, H. and Cygler, M. Crystallization and preliminary X-ray analysis of chondroitinase B from Flavobacterium heparinum. Acta Crystallogr. D Biol. Crystallogr. 55 (1999) 1055-1057. [PMID: 10216304]
9. Huang, W., Matte, A., Li, Y., Kim, Y.S., Linhardt, R.J., Su, H. and Cygler, M. Crystal structure of chondroitinase B from Flavobacterium heparinum and its complex with a disaccharide product at 1.7 Å resolution. J. Mol. Biol. 294 (1999) 1257-1269. [PMID: 10600383]
[EC 5.2.1.11 Deleted entry: 4-hydroxyphenylacetaldehyde-oxime isomerase. The existence of this enzyme has been called into question by one of the authors of the reference cited (EC 5.2.1.11 created 1992, deleted 2005)]
Common name: L-dopachrome isomerase
Reaction: L-dopachrome = 5,6-dihydroxyindole-2-carboxylate
For diagram click here.
Glossary: L-dopachrome = (2S)-5,6-dioxo-2,3,5,6-tetrahydro-1H-indole-2-carboxylate
Other name(s): dopachrome tautomerase; tyrosinase-related protein 2; TRP-1; TRP2; TRP-2; tyrosinase-related protein-2; dopachrome δ7,δ2-isomerase; dopachrome δ-isomerase; dopachrome conversion factor; dopachrome isomerase; dopachrome oxidoreductase; dopachrome-rearranging enzyme; DCF; DCT; dopachrome keto-enol isomerase; L-dopachrome-methyl ester tautomerase
Systematic name: L-dopachrome keto-enol isomerase
Comments: A zinc enzyme. Stereospecific for L-dopachrome. Dopachrome methyl ester is a substrate, but dopaminochrome (2,3-dihydroindole-5,6-quinone) is not (see also EC 4.1.1.84, D-dopachrome decarboxylase).
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 130122-81-5
References:
1. Solano, F., Jiménez-Cervantes, C., Martinez-Liarte, J.H., Garcia-Borrón and J.C., Lozano, J.A. Molecular mechanism for catalysis by a new zinc enzyme, dopachrome tautomerase. Biochem. J. 313 (1996) 447-453. [PMID: 8573077]
2. Pawelek, J.M. Dopachrome conversion factor functions as an isomerase. Biochem. Biophys. Res. Commun. 166 (1990) 1328-1333. [PMID: 2106316]
3. Pennock, J.L., Behnke, J.M., Bickle, Q.D., Devaney, E., Grencis, R.K., Isaac, R.E., Joshua. G.W., Selkirk. M.E., Zhang. Y. and Meyer, D.J. Rapid purification and characterization of L-dopachrome-methyl ester tautomerase (macrophage-migration-inhibitory factor) from Trichinella spiralis, Trichuris muris and Brugia pahangi. Biochem. J. 335 (1998) 495-498. [PMID: 9794786]
Common name: glutamate—putrescine ligase
Reaction: ATP + L-glutamate + putrescine = ADP + phosphate + γ-L-glutamylputrescine
Other name(s): γ-glutamylputrescine synthetase; YcjK
Systematic name: L-glutamate:putrescine ligase (ADP-forming)
Comments: Forms part of a novel bacterial putrescine utilization pathway in Escherichia coli.
References:
1. Kurihara, S., Oda, S., Kato, K., Kim, H.G., Koyanagi, T., Kumagai, H. and Suzuki, H. A novel putrescine utilization pathway involves γ-glutamylated intermediates of Escherichia coli K-12. J. Biol. Chem. 280 (2005) 4602-4608. [PMID: 15590624]