The Enzyme Database

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EC 1.1.1.41     
Accepted name: isocitrate dehydrogenase (NAD+)
Reaction: isocitrate + NAD+ = 2-oxoglutarate + CO2 + NADH
For diagram of the citric-acid cycle, 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, MetaCyc, PDB, 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. (Ed.), The Enzymes, 2nd edn, 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. [DOI] [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. [DOI] [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. [DOI] [PMID: 12204383]
[EC 1.1.1.41 created 1961, modified 2005]
 
 
EC 1.1.1.42     
Accepted name: isocitrate dehydrogenase (NADP+)
Reaction: isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH + H+ (overall reaction)
(1a) isocitrate + NADP+ = oxalosuccinate + NADPH + H+
(1b) oxalosuccinate = 2-oxoglutarate + CO2
For diagram of the citric-acid cycle, 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; 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, MetaCyc, 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. [DOI] [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. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 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. [DOI] [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. [DOI] [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. [DOI] [PMID: 12207025]
[EC 1.1.1.42 created 1961, modified 2005]
 
 
EC 1.1.1.95     
Accepted name: phosphoglycerate dehydrogenase
Reaction: 3-phospho-D-glycerate + NAD+ = 3-phosphooxypyruvate + NADH + H+
For diagram of serine biosynthesis, click here
Other name(s): PHGDH (gene name); D-3-phosphoglycerate:NAD+ oxidoreductase; α-phosphoglycerate dehydrogenase; 3-phosphoglycerate dehydrogenase; 3-phosphoglyceric acid dehydrogenase; D-3-phosphoglycerate dehydrogenase; glycerate 3-phosphate dehydrogenase; glycerate-1,3-phosphate dehydrogenase; phosphoglycerate oxidoreductase; phosphoglyceric acid dehydrogenase; SerA; 3-phosphoglycerate:NAD+ 2-oxidoreductase; SerA 3PG dehydrogenase; 3PHP reductase
Systematic name: 3-phospho-D-glycerate:NAD+ 2-oxidoreductase
Comments: This enzyme catalyses the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. The reaction occurs predominantly in the direction of reduction. The enzyme from the bacterium Escherichia coli also catalyses the activity of EC 1.1.1.399, 2-oxoglutarate reductase [6].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9075-29-0
References:
1.  Pizer, L.I. The pathway and control of serine biosynthesis in Escherichia coli. J. Biol. Chem. 238 (1963) 3934–3944. [PMID: 14086727]
2.  Walsh, D.A. and Sallach, H.J. Purification and properties of chicken liver D-3-phosphoglycerate dehydrogenase. Biochemistry 4 (1965) 1076–1085. [PMID: 4378782]
3.  Slaughter, J.C. and Davies, D.D. The isolation and characterization of 3-phosphoglycerate dehydrogenase from peas. Biochem. J. 109 (1968) 743–748. [PMID: 4386930]
4.  Sugimoto, E. and Pizer, L.I. The mechanism of end product inhibition of serine biosynthesis. I. Purification and kinetics of phosphoglycerate dehydrogenase. J. Biol. Chem. 243 (1968) 2081. [PMID: 4384871]
5.  Schuller, D.J., Grant, G.A. and Banaszak, L.J. The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase. Nat. Struct. Biol. 2 (1995) 69–76. [PMID: 7719856]
6.  Zhao, G. and Winkler, M.E. A novel α-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria. J. Bacteriol. 178 (1996) 232–239. [DOI] [PMID: 8550422]
7.  Achouri, Y., Rider, M.H., Schaftingen, E.V. and Robbi, M. Cloning, sequencing and expression of rat liver 3-phosphoglycerate dehydrogenase. Biochem. J. 323 (1997) 365–370. [PMID: 9163325]
8.  Dey, S., Grant, G.A. and Sacchettini, J.C. Crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase: extreme asymmetry in a tetramer of identical subunits. J. Biol. Chem. 280 (2005) 14892–14899. [DOI] [PMID: 15668249]
[EC 1.1.1.95 created 1972, modified 2006, modified 2016]
 
 
EC 1.1.1.111     
Accepted name: 3-(imidazol-5-yl)lactate dehydrogenase
Reaction: (S)-3-(imidazol-5-yl)lactate + NAD(P)+ = 3-(imidazol-5-yl)pyruvate + NAD(P)H + H+
Other name(s): imidazol-5-yl lactate dehydrogenase
Systematic name: (S)-3-(imidazol-5-yl)lactate:NAD(P)+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37250-42-3
References:
1.  Coote, J.G. and Hassall, H. The role of imidazol-5-yl-lactate-nicotinamide-adenine dinucleotide phosphate oxidoreductase and histidine-2-oxoglutarate aminotransferase in the degradation of imidazol-5-yl-lactate by Pseudomonas acidovorans. Biochem. J. 111 (1969) 237–239. [PMID: 4303364]
2.  Cortese, R., Brevet, J., Hedegaard, J. and Roche, J. [Identification and purification of an α-ketoacid aromatic reductase of Escherichia coli B] C.R. Seances Soc. Biol. Fil. 162 (1968) 390–395. [PMID: 4237631] (in French)
[EC 1.1.1.111 created 1972]
 
 
EC 1.1.1.286     
Accepted 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+
Glossary: isocitrate = (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate (previously known as threo-Ds-isocitrate)
homoisocitrate = (-)-threo-homoisocitrate = (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
Other name(s): homoisocitrate—isocitrate dehydrogenase; PH1722
Systematic name: isocitrate(homoisocitrate):NAD+ oxidoreductase (decarboxylating)
Comments: Requires 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.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
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. [DOI] [PMID: 15845397]
[EC 1.1.1.286 created 2005]
 
 
EC 1.1.1.290     
Accepted name: 4-phosphoerythronate dehydrogenase
Reaction: 4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH + H+
For diagram of pyridoxal biosynthesis, click here
Other name(s): PdxB; PdxB 4PE dehydrogenase; 4-O-phosphoerythronate dehydrogenase; 4PE dehydrogenase; erythronate-4-phosphate dehydrogenase
Systematic name: 4-phospho-D-erythronate:NAD+ 2-oxidoreductase
Comments: This enzyme catalyses a step in a bacterial pathway for the biosynthesis of pyridoxal 5′-phosphate. The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD+. In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyses the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)-hydroxy acid [6]. cf. EC 1.1.1.399, 2-oxoglutarate reductase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 125858-75-5
References:
1.  Lam, H.M. and Winkler, M.E. Metabolic relationships between pyridoxine (vitamin B6) and serine biosynthesis in Escherichia coli K-12. J. Bacteriol. 172 (1990) 6518–6528. [DOI] [PMID: 2121717]
2.  Pease, A.J., Roa, B.R., Luo, W. and Winkler, M.E. Positive growth rate-dependent regulation of the pdxA, ksgA, and pdxB genes of Escherichia coli K-12. J. Bacteriol. 184 (2002) 1359–1369. [DOI] [PMID: 11844765]
3.  Zhao, G. and Winkler, M.E. A novel α-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria. J. Bacteriol. 178 (1996) 232–239. [DOI] [PMID: 8550422]
4.  Grant, G.A. A new family of 2-hydroxyacid dehydrogenases. Biochem. Biophys. Res. Commun. 165 (1989) 1371–1374. [DOI] [PMID: 2692566]
5.  Schoenlein, P.V., Roa, B.B. and Winkler, M.E. Divergent transcription of pdxB and homology between the pdxB and serA gene products in Escherichia coli K-12. J. Bacteriol. 171 (1989) 6084–6092. [DOI] [PMID: 2681152]
6.  Rudolph, J., Kim, J. and Copley, S.D. Multiple turnovers of the nicotino-enzyme PdxB require α-keto acids as cosubstrates. Biochemistry 49 (2010) 9249–9255. [DOI] [PMID: 20831184]
[EC 1.1.1.290 created 2006, modified 2016]
 
 
EC 1.1.1.335     
Accepted name: UDP-N-acetyl-2-amino-2-deoxyglucuronate dehydrogenase
Reaction: UDP-N-acetyl-2-amino-2-deoxy-α-D-glucuronate + NAD+ = UDP-2-acetamido-2-deoxy-α-D-ribo-hex-3-uluronate + NADH + H+
For diagram of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronate biosynthesis, click here
Other name(s): WlbA; WbpB
Systematic name: UDP-N-acetyl-2-amino-2-deoxy-α-D-glucuronate:NAD+ 3-oxidoreductase
Comments: This enzyme participates in the biosynthetic pathway for UDP-α-D-ManNAc3NAcA (UDP-2,3-diacetamido-2,3-dideoxy-α-D-mannuronic acid), an important precursor of B-band lipopolysaccharide. The enzymes from Pseudomonas aeruginosa serotype O5 and Thermus thermophilus form a complex with the the enzyme catalysing the next step the pathway (EC 2.6.1.98, UDP-2-acetamido-2-deoxy-ribo-hexuluronate aminotransferase). The enzyme also possesses an EC 1.1.99.2 (L-2-hydroxyglutarate dehydrogenase) activity, and utilizes the 2-oxoglutarate produced by EC 2.6.1.98 to regenerate the tightly bound NAD+. The enzymes from Bordetella pertussis and Chromobacterium violaceum do not bind NAD+ as tightly and do not require 2-oxoglutarate to function.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Westman, E.L., McNally, D.J., Charchoglyan, A., Brewer, D., Field, R.A. and Lam, J.S. Characterization of WbpB, WbpE, and WbpD and reconstitution of a pathway for the biosynthesis of UDP-2,3-diacetamido-2,3-dideoxy-D-mannuronic acid in Pseudomonas aeruginosa. J. Biol. Chem. 284 (2009) 11854–11862. [DOI] [PMID: 19282284]
2.  Larkin, A. and Imperiali, B. Biosynthesis of UDP-GlcNAc(3NAc)A by WbpB, WbpE, and WbpD: enzymes in the Wbp pathway responsible for O-antigen assembly in Pseudomonas aeruginosa PAO1. Biochemistry 48 (2009) 5446–5455. [DOI] [PMID: 19348502]
3.  Thoden, J.B. and Holden, H.M. Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid. Biochemistry 49 (2010) 7939–7948. [DOI] [PMID: 20690587]
4.  Thoden, J.B. and Holden, H.M. Biochemical and structural characterization of WlbA from Bordetella pertussis and Chromobacterium violaceum: enzymes required for the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid. Biochemistry 50 (2011) 1483–1491. [DOI] [PMID: 21241053]
[EC 1.1.1.335 created 2012]
 
 
EC 1.1.1.399     
Accepted name: 2-oxoglutarate reductase
Reaction: (R)-2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH + H+
Other name(s): serA (gene name)
Systematic name: (R)-2-hydroxyglutarate:NAD+ 2-oxidireductase
Comments: The enzyme catalyses a reversible reaction. The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate [1,2]. The SerA enzyme from the bacterium Escherichia coli can also accept (S)-2-hydroxyglutarate with a much higher Km, and also catalyses the activity of EC 1.1.1.95, phosphoglycerate dehydrogenase [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Lerud, R.F. and Whiteley, H.R. Purification and properties of α-ketoglutarate reductase from Micrococcus aerogenes. J. Bacteriol. 106 (1971) 571–577. [PMID: 4396793]
2.  Johnson, W.M. and Westlake, D.W. Purification and characterization of glutamic acid dehydrogenase and α-ketoglutaric acid reductase from Peptococcus aerogenes. Can. J. Microbiol. 18 (1972) 881–892. [PMID: 4338318]
3.  Zhao, G. and Winkler, M.E. A novel α-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria. J. Bacteriol. 178 (1996) 232–239. [DOI] [PMID: 8550422]
[EC 1.1.1.399 created 2016]
 
 
EC 1.1.5.13     
Accepted name: (S)-2-hydroxyglutarate dehydrogenase
Reaction: (S)-2-hydroxyglutarate + a quinone = 2-oxoglutarate + a quinol
Other name(s): L-2-hydroxyglutarate dehydrogenase; lhgO (gene name); ygaF (gene name)
Systematic name: (S)-2-hydroxyglutarate:quinone oxidoreductase
Comments: The enzyme, characterized from the bacterium Escherichia coli, contains an FAD cofactor that is not covalently attached. It is bound to the cytoplasmic membrane and is coupled to the membrane quinone pool.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kalliri, E., Mulrooney, S.B. and Hausinger, R.P. Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase. J. Bacteriol. 190 (2008) 3793–3798. [PMID: 18390652]
2.  Knorr, S., Sinn, M., Galetskiy, D., Williams, R.M., Wang, C., Muller, N., Mayans, O., Schleheck, D. and Hartig, J.S. Widespread bacterial lysine degradation proceeding via glutarate and L-2-hydroxyglutarate. Nat. Commun. 9:5071 (2018). [PMID: 30498244]
[EC 1.1.5.13 created 2019]
 
 
EC 1.1.99.2     
Accepted name: L-2-hydroxyglutarate dehydrogenase
Reaction: (S)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor
Other name(s): α-ketoglutarate reductase; α-hydroxyglutarate dehydrogenase; L-α-hydroxyglutarate dehydrogenase; hydroxyglutaric dehydrogenase; α-hydroxyglutarate oxidoreductase; L-α-hydroxyglutarate:NAD+ 2-oxidoreductase; α-hydroxyglutarate dehydrogenase (NAD+ specific); (S)-2-hydroxyglutarate:(acceptor) 2-oxidoreductase
Systematic name: (S)-2-hydroxyglutarate:acceptor 2-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-80-2
References:
1.  Weil-Malherbe, H. The oxidation of l(–)α-hydroxyglutaric acid in animal tissues. Biochem. J. 31 (1937) 2080–2094. [PMID: 16746551]
[EC 1.1.99.2 created 1961, modified 2013]
 
 
EC 1.1.99.24     
Accepted name: hydroxyacid-oxoacid transhydrogenase
Reaction: (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + (R)-2-hydroxyglutarate
Other name(s): transhydrogenase, hydroxy acid-oxo acid
Systematic name: (S)-3-hydroxybutanoate:2-oxoglutarate oxidoreductase
Comments: 4-Hydroxybutanoate and (R)-2-hydroxyglutarate can also act as donors; 4-oxobutanoate can also act as acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 117698-31-4
References:
1.  Kaufman, E.E., Nelson, T., Fales, H.M. and Levin, D.M. Isolation and characterization of a hydroxyacid-oxoacid transhydrogenase from rat kidney mitochondria. J. Biol. Chem. 263 (1988) 16872–16879. [PMID: 3182820]
[EC 1.1.99.24 created 1992]
 
 
EC 1.1.99.39     
Accepted name: D-2-hydroxyglutarate dehydrogenase
Reaction: (R)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor
Other name(s): D2HGDH (gene name)
Systematic name: (R)-2-hydroxyglutarate:acceptor 2-oxidoreductase
Comments: Contains FAD. The enzyme has no activity with NAD+ or NADP+, and was assayed in vitro using artificial electron acceptors. It has lower activity with (R)-lactate, (R)-2-hydroxybutyrate and meso-tartrate, and no activity with the (S) isomers. The mammalian enzyme is stimulated by Zn2+, Co2+ and Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Engqvist, M., Drincovich, M.F., Flugge, U.I. and Maurino, V.G. Two D-2-hydroxy-acid dehydrogenases in Arabidopsis thaliana with catalytic capacities to participate in the last reactions of the methylglyoxal and β-oxidation pathways. J. Biol. Chem. 284 (2009) 25026–25037. [DOI] [PMID: 19586914]
2.  Achouri, Y., Noel, G., Vertommen, D., Rider, M.H., Veiga-Da-Cunha, M. and Van Schaftingen, E. Identification of a dehydrogenase acting on D-2-hydroxyglutarate. Biochem. J. 381 (2004) 35–42. [DOI] [PMID: 15070399]
[EC 1.1.99.39 created 2013]
 
 
EC 1.1.99.40     
Accepted name: (R)-2-hydroxyglutarate—pyruvate transhydrogenase
Reaction: (R)-2-hydroxyglutarate + pyruvate = 2-oxoglutarate + (R)-lactate
Other name(s): DLD3 (gene name)
Systematic name: (R)-2-hydroxyglutarate:pyruvate oxidoreductase [(R)-lactate-forming]
Comments: The enzyme, characterized in the yeast Saccharomyces cerevisiae, also functions as EC 1.1.2.4, D-lactate dehydrogenase (cytochrome), and is active with oxaloacetate as electron acceptor forming (R)-malate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Becker-Kettern, J., Paczia, N., Conrotte, J.F., Kay, D.P., Guignard, C., Jung, P.P. and Linster, C.L. Saccharomyces cerevisiae forms D-2-hydroxyglutarate and couples its degradation to D-lactate formation via a cytosolic transhydrogenase. J. Biol. Chem. 291 (2016) 6036–6058. [DOI] [PMID: 26774271]
[EC 1.1.99.40 created 2017]
 
 
EC 1.2.1.25     
Accepted name: branched-chain α-keto acid dehydrogenase system
Reaction: 3-methyl-2-oxobutanoate + CoA + NAD+ = 2-methylpropanoyl-CoA + CO2 + NADH
Other name(s): branched-chain α-keto acid dehydrogenase complex; 2-oxoisovalerate dehydrogenase; α-ketoisovalerate dehydrogenase; 2-oxoisovalerate dehydrogenase (acylating)
Systematic name: 3-methyl-2-oxobutanoate:NAD+ 2-oxidoreductase (CoA-methylpropanoylating)
Comments: This enzyme system catalyses the oxidative decarboxylation of branched-chain α-keto acids derived from L-leucine, L-isoleucine, and L-valine to branched-chain acyl-CoAs. It belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.104, pyruvate dehydrogenase system, EC 1.2.1.105, 2-oxoglutarate dehydrogenase system, EC 1.4.1.27, glycine cleavage system, and EC 2.3.1.190, acetoin dehydrogenase system. With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). The reaction catalysed by this system is the sum of three activities: EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring), EC 2.3.1.168, dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The system also acts on (S)-3-methyl-2-oxopentanoate and 4-methyl-2-oxopentanoate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37211-61-3
References:
1.  Namba, Y., Yoshizawa, K., Ejima, A., Hayashi, T. and Kaneda, T. Coenzyme A- and nicotinamide adenine dinucleotide-dependent branched chain α-keto acid dehydrogenase. I. Purification and properties of the enzyme from Bacillus subtilis. J. Biol. Chem. 244 (1969) 4437–4447. [PMID: 4308861]
2.  Pettit, F.H., Yeaman, S.J. and Reed, L.J. Purification and characterization of branched chain α-keto acid dehydrogenase complex of bovine kidney. Proc. Natl. Acad. Sci. USA 75 (1978) 4881–4885. [DOI] [PMID: 283398]
3.  Harris, R.A., Hawes, J.W., Popov, K.M., Zhao, Y., Shimomura, Y., Sato, J., Jaskiewicz, J. and Hurley, T.D. Studies on the regulation of the mitochondrial α-ketoacid dehydrogenase complexes and their kinases. Adv. Enzyme Regul. 37 (1997) 271–293. [DOI] [PMID: 9381974]
4.  Evarsson, A., Chuang, J.L., Wynn, R.M., Turley, S., Chuang, D.T. and Hol, W.G. Crystal structure of human branched-chain α-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease. Structure 8 (2000) 277–291. [PMID: 10745006]
5.  Reed, L.J. A trail of research from lipoic acid to α-keto acid dehydrogenase complexes. J. Biol. Chem. 276 (2001) 38329–38336. [DOI] [PMID: 11477096]
[EC 1.2.1.25 created 1972, modified 2019, modified 2020]
 
 
EC 1.2.1.26     
Accepted name: 2,5-dioxovalerate dehydrogenase
Reaction: 2,5-dioxopentanoate + NADP+ + H2O = 2-oxoglutarate + NADPH + 2 H+
Other name(s): 2-oxoglutarate semialdehyde dehydrogenase; α-ketoglutaric semialdehyde dehydrogenase
Systematic name: 2,5-dioxopentanoate:NADP+ 5-oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-92-3
References:
1.  Adams, E. and Rosso, G. α-Ketoglutaric semialdehyde dehydrogenase of Pseudomonas. Properties of the purified enzyme induced by hydroxyproline and of the glucarate-induced and constitutive enzymes. J. Biol. Chem. 242 (1967) 1803–1814. [PMID: 6024771]
[EC 1.2.1.26 created 1972]
 
 
EC 1.2.1.52     
Accepted name: oxoglutarate dehydrogenase (NADP+)
Reaction: 2-oxoglutarate + CoA + NADP+ = succinyl-CoA + CO2 + NADPH
Other name(s): oxoglutarate dehydrogenase (NADP)
Systematic name: 2-oxoglutarate:NADP+ 2-oxidoreductase (CoA-succinylating)
Comments: The Euglena enzyme can also use NAD+ as acceptor, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 126469-85-0
References:
1.  Inui, H., Miyatake, K., Nakano, Y. and Kitaoka, S. Occurrence of oxygen-sensitive, NADP +-dependent pyruvate dehydrogenase in mitochondria of Euglena gracilis. J. Biochem. (Tokyo) 96 (1984) 931–934. [PMID: 6438078]
[EC 1.2.1.52 created 1989]
 
 
EC 1.2.1.104     
Accepted name: pyruvate dehydrogenase system
Reaction: pyruvate + CoA + NAD+ = acetyl-CoA + CO2 + NADH
Other name(s): pyruvate dehydrogenase complex; PDH
Systematic name: pyruvate:NAD+ 2-oxidoreductase (CoA-acetylating)
Comments: The pyruvate dehydrogenase system (PDH) is a large enzyme complex that belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.25, branched-chain α-keto acid dehydrogenase system, EC 1.2.1.105, 2-oxoglutarate dehydrogenase system, EC 1.4.1.27, glycine cleavage system, and EC 2.3.1.190, acetoin dehydrogenase system. With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and a dihydrolipoamide dehydrogenase (E3). The reaction catalysed by this system is the sum of three activities: EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring) (E1), EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase (E2), and EC 1.8.1.4, dihydrolipoyl dehydrogenase (E3). The mammalian system also includes E3 binding protein, which is involved in the interaction between the E2 and E3 subunits.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Reed, L.J., Pettit, F.H., Eley, M.H., Hamilton, L., Collins, J.H. and Oliver, R.M. Reconstitution of the Escherichia coli pyruvate dehydrogenase complex. Proc. Natl. Acad. Sci. USA 72 (1975) 3068–3072. [DOI] [PMID: 1103138]
2.  Bates, D.L., Danson, M.J., Hale, G., Hooper, E.A. and Perham, R.N. Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Nature 268 (1977) 313–316. [DOI] [PMID: 329143]
3.  Stanley, C.J., Packman, L.C., Danson, M.J., Henderson, C.E. and Perham, R.N. Intramolecular coupling of active sites in the pyruvate dehydrogenase multienzyme complexes from bacterial and mammalian sources. Biochem. J. 195 (1981) 715–721. [DOI] [PMID: 7032507]
4.  Yang, H.C., Hainfeld, J.F., Wall, J.S. and Frey, P.A. Quaternary structure of pyruvate dehydrogenase complex from Escherichia coli. J. Biol. Chem. 260 (1985) 16049–16051. [PMID: 3905803]
5.  Patel, M.S. and Roche, T.E. Molecular biology and biochemistry of pyruvate dehydrogenase complexes. FASEB J. 4 (1990) 3224–3233. [DOI] [PMID: 2227213]
[EC 1.2.1.104 created 2020]
 
 
EC 1.2.1.105     
Accepted name: 2-oxoglutarate dehydrogenase system
Reaction: 2-oxoglutarate + CoA + NAD+ = succinyl-CoA + CO2 + NADH
Other name(s): 2-oxoglutarate dehydrogenase complex
Systematic name: 2-oxoglutarate:NAD+ 2-oxidoreductase (CoA-succinylating)
Comments: The 2-oxoglutarate dehydrogenase system is a large enzyme complex that belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.25, branched-chain α-keto acid dehydrogenase system, EC 1.2.1.104, pyruvate dehydrogenase system, EC 1.4.1.27, glycine cleavage system, and EC 2.3.1.190, acetoin dehydrogenase system. With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and a dihydrolipoamide dehydrogenase (E3). This enzyme system converts 2-oxoglutarate to succinyl-CoA and produces NADH and CO2 in a complicated series of irreversible reactions. The reaction catalysed by this system is the sum of three activities: EC 1.2.4.2, oxoglutarate dehydrogenase (succinyl-transferring) (E1), EC 2.3.1.61, dihydrolipoyllysine-residue succinyltransferase (E2) and EC 1.8.1.4, dihydrolipoyl dehydrogenase (E3).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Robien, M.A., Clore, G.M., Omichinski, J.G., Perham, R.N., Appella, E., Sakaguchi, K. and Gronenborn, A.M. Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli. Biochemistry 31 (1992) 3463–3471. [DOI] [PMID: 1554728]
2.  Knapp, J.E., Mitchell, D.T., Yazdi, M.A., Ernst, S.R., Reed, L.J. and Hackert, M.L. Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. J. Mol. Biol. 280 (1998) 655–668. [DOI] [PMID: 9677295]
3.  Reed, L.J. A trail of research from lipoic acid to α-keto acid dehydrogenase complexes. J. Biol. Chem. 276 (2001) 38329–38336. [DOI] [PMID: 11477096]
4.  Murphy, G.E. and Jensen, G.J. Electron cryotomography of the E. coli pyruvate and 2-oxoglutarate dehydrogenase complexes. Structure 13 (2005) 1765–1773. [DOI] [PMID: 16338405]
5.  Frank, R.A., Price, A.J., Northrop, F.D., Perham, R.N. and Luisi, B.F. Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. J. Mol. Biol. 368 (2007) 639–651. [DOI] [PMID: 17367808]
6.  Bunik, V.I. and Degtyarev, D. Structure-function relationships in the 2-oxo acid dehydrogenase family: substrate-specific signatures and functional predictions for the 2-oxoglutarate dehydrogenase-like proteins. Proteins 71 (2008) 874–890. [DOI] [PMID: 18004749]
7.  Shim da, J., Nemeria, N.S., Balakrishnan, A., Patel, H., Song, J., Wang, J., Jordan, F. and Farinas, E.T. Assignment of function to histidines 260 and 298 by engineering the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase complex; substitutions that lead to acceptance of substrates lacking the 5-carboxyl group. Biochemistry 50 (2011) 7705–7709. [DOI] [PMID: 21809826]
[EC 1.2.1.105 created 2020]
 
 
EC 1.2.4.2     
Accepted name: oxoglutarate dehydrogenase (succinyl-transferring)
Reaction: 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2
For diagram of the citric acid cycle, click here and for diagram of oxo-acid dehydrogenase complexes, click here
Glossary: dihydrolipoyl group
thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium
Other name(s): 2-ketoglutarate dehydrogenase; 2-oxoglutarate dehydrogenase; 2-oxoglutarate: lipoate oxidoreductase; 2-oxoglutarate:lipoamide 2-oxidoreductase (decarboxylating and acceptor-succinylating); α-ketoglutarate dehydrogenase; alphaketoglutaric acid dehydrogenase; α-ketoglutaric dehydrogenase; α-oxoglutarate dehydrogenase; AKGDH; OGDC; ketoglutaric dehydrogenase; oxoglutarate decarboxylase (misleading); oxoglutarate dehydrogenase; oxoglutarate dehydrogenase (lipoamide)
Systematic name: 2-oxoglutarate:[dihydrolipoyllysine-residue succinyltransferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-succinylating)
Comments: Contains thiamine diphosphate. It is a component of the multienzyme 2-oxoglutarate dehydrogenase complex, EC 1.2.1.105, in which multiple copies of it are bound to a core of molecules of EC 2.3.1.61, dihydrolipoyllysine-residue succinyltransferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.61.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-02-1
References:
1.  Massey, V. The composition of the ketoglutarate dehydrogenase complex. Biochim. Biophys. Acta 38 (1960) 447–460. [DOI] [PMID: 14422131]
2.  Ochoa, S. Enzymic mechanisms in the citric acid cycle. Adv. Enzymol. Relat. Subj. Biochem. 15 (1954) 183–270. [PMID: 13158180]
3.  Sanadi, D.R., Littlefield, J.W. and Bock, R.M. Studies on α-ketoglutaric oxidase. II. Purification and properties. J. Biol. Chem. 197 (1952) 851–862. [PMID: 12981117]
4.  Perham, R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961–1004. [DOI] [PMID: 10966480]
[EC 1.2.4.2 created 1961, modified 1980, modified 1986, modified 2003]
 
 
EC 1.2.7.1     
Accepted name: pyruvate synthase
Reaction: pyruvate + CoA + 2 oxidized ferredoxin = acetyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): pyruvate oxidoreductase; pyruvate synthetase; pyruvate:ferredoxin oxidoreductase; pyruvic-ferredoxin oxidoreductase; 2-oxobutyrate synthase; α-ketobutyrate-ferredoxin oxidoreductase; 2-ketobutyrate synthase; α-ketobutyrate synthase; 2-oxobutyrate-ferredoxin oxidoreductase; 2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propionylating); 2-oxobutanoate:ferredoxin 2-oxidoreductase (CoA-propanoylating)
Systematic name: pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating)
Comments: Contains thiamine diphosphate and [4Fe-4S] clusters. The enzyme also decarboxylates 2-oxobutyrate with lower efficiency, but shows no activity with 2-oxoglutarate. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9082-51-3
References:
1.  Evans, M.C.W. and Buchanan, B.B. Photoreduction of ferredoxin and its use in carbon dioxide fixation by a subcellular system from a photosynthetic bacterium. Proc. Natl. Acad. Sci. USA 53 (1965) 1420–1425. [DOI] [PMID: 5217644]
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.  Uyeda, K. and Rabinowitz, J.C. Pyruvate-ferredoxin oxidoreductase. 3. Purification and properties of the enzyme. J. Biol. Chem. 246 (1971) 3111–3119. [PMID: 5574389]
4.  Uyeda, K. and Rabinowitz, J.C. Pyruvate-ferredoxin oxidoreductase. IV. Studies on the reaction mechanism. J. Biol. Chem. 246 (1971) 3120–3125. [PMID: 4324891]
5.  Charon, M.-H., Volbeda, A., Chabriere, E., Pieulle, L. and Fontecilla-Camps, J.C. Structure and electron transfer mechanism of pyruvate:ferredoxin oxidoreductase. Curr. Opin. Struct. Biol. 9 (1999) 663–669. [DOI] [PMID: 10607667]
[EC 1.2.7.1 created 1972, modified 2003, modified 2013]
 
 
EC 1.2.7.3     
Accepted name: 2-oxoglutarate synthase
Reaction: 2-oxoglutarate + CoA + 2 oxidized ferredoxin = succinyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
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: The enzyme contains thiamine diphosphate and two [4Fe-4S] clusters. Highly specific for 2-oxoglutarate. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.1, pyruvate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, 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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [PMID: 11265457]
[EC 1.2.7.3 created 1972, modified 2005]
 
 
EC 1.2.7.7     
Accepted name: 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin)
Reaction: 3-methyl-2-oxobutanoate + CoA + 2 oxidized ferredoxin = S-(2-methylpropanoyl)-CoA + CO2 + 2 reduced ferredoxin + H+
Other name(s): 2-ketoisovalerate ferredoxin reductase; 3-methyl-2-oxobutanoate synthase (ferredoxin); VOR; branched-chain ketoacid ferredoxin reductase; branched-chain oxo acid ferredoxin reductase; keto-valine-ferredoxin oxidoreductase; ketoisovalerate ferredoxin reductase; 2-oxoisovalerate ferredoxin reductase
Systematic name: 3-methyl-2-oxobutanoate:ferredoxin oxidoreductase (decarboxylating; CoA-2-methylpropanoylating)
Comments: The enzyme is CoA-dependent and contains thiamine diphosphate and iron-sulfur clusters. Preferentially utilizes 2-oxo-acid derivatives of branched chain amino acids, e.g. 3-methyl-2-oxopentanoate, 4-methyl-2-oxo-pentanoate, and 2-oxobutanoate. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that reversibly catalyse the oxidative decarboxylation of different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.1, pyruvate synthase, and EC 1.2.7.3, 2-oxoglutarate synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Buchanan, B.B. Role of ferredoxin in the synthesis of α-ketobutyrate from propionyl coenzyme A and carbon dioxide by enzymes from photosynthetic and nonphotosynthetic bacteria. J. Biol. Chem. 244 (1969) 4218–4223. [PMID: 5800441]
2.  Heider, J., Mai, X.H. and Adams, M.W.W. Characterization of 2-ketoisovalerate ferredoxin oxidoreductase, a new and reversible coenzyme A-dependent enzyme involved in peptide fermentation by hyperthermophilic archaea. J. Bacteriol. 178 (1996) 780–787. [DOI] [PMID: 8550513]
3.  Tersteegen, A., Linder, D., Thauer, R.K. and Hedderich, R. Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum. Eur. J. Biochem. 244 (1997) 862–868. [DOI] [PMID: 9108258]
4.  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. [DOI] [PMID: 11265457]
[EC 1.2.7.7 created 2003]
 
 
EC 1.2.7.8     
Accepted name: indolepyruvate ferredoxin oxidoreductase
Reaction: (indol-3-yl)pyruvate + CoA + 2 oxidized ferredoxin = S-2-(indol-3-yl)acetyl-CoA + CO2 + 2 reduced ferredoxin + H+
Other name(s): 3-(indol-3-yl)pyruvate synthase (ferredoxin); IOR
Systematic name: 3-(indol-3-yl)pyruvate:ferredoxin oxidoreductase (decarboxylating, CoA-indole-acetylating)
Comments: Contains thiamine diphosphate and [4Fe-4S] clusters. Preferentially utilizes the transaminated forms of aromatic amino acids and can use phenylpyruvate and p-hydroxyphenylpyruvate as substrates. This enzyme, which is found in archaea, is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For examples of other members of this family, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 158886-06-7
References:
1.  Mai, X.H. and Adams, M.W.W. Indolepyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus - a new enzyme involved in peptide fermentation. J. Biol. Chem. 269 (1994) 16726–16732. [PMID: 8206994]
2.  Siddiqui, M.A., Fujiwara, S. and Imanaka, T. Indolepyruvate ferredoxin oxidoreductase from Pyrococcus sp. K0d1 possesses a mosaic: Structure showing features of various oxidoreductases. Mol. Gen. Genet. 254 (1997) 433–439. [PMID: 9180697]
3.  Tersteegen, A., Linder, D., Thauer, R.K. and Hedderich, R. Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum. Eur. J. Biochem. 244 (1997) 862–868. [DOI] [PMID: 9108258]
4.  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. [DOI] [PMID: 11265457]
[EC 1.2.7.8 created 2003]
 
 
EC 1.2.7.9      
Deleted entry: 2-oxoglutarate ferredoxin oxidoreductase. This enzyme is identical to EC 1.2.7.3, 2-oxoglutarate synthase
[EC 1.2.7.9 created 2003, deleted 2005]
 
 
EC 1.2.7.11     
Accepted name: 2-oxoacid oxidoreductase (ferredoxin)
Reaction: a 2-oxocarboxylate + CoA + 2 oxidized ferredoxin = an acyl-CoA + CO2 + 2 reduced ferredoxin + 2 H+
Other name(s): OFOR
Systematic name: 2-oxocarboxylate:ferredoxin 2-oxidoreductase (decarboxylating, CoA-acylating)
Comments: Contains thiamine diphosphate and [4Fe-4S] clusters [2]. This enzyme is a member of the 2-oxoacid oxidoreductases, a family of enzymes that oxidatively decarboxylate different 2-oxoacids to form their CoA derivatives, and are differentiated based on their substrate specificity. For example, see EC 1.2.7.3, 2-oxoglutarate synthase and EC 1.2.7.7, 3-methyl-2-oxobutanoate dehydrogenase (ferredoxin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kerscher, L. and Oesterhelt, D. Purification and properties of two 2-oxoacid:ferredoxin oxidoreductases from Halobacterium halobium. Eur. J. Biochem. 116 (1981) 587–594. [DOI] [PMID: 6266826]
2.  Zhang, Q., Iwasaki, T., Wakagi, T. and Oshima, T. 2-oxoacid:ferredoxin oxidoreductase from the thermoacidophilic archaeon, Sulfolobus sp. strain 7. J. Biochem. 120 (1996) 587–599. [PMID: 8902625]
3.  Fukuda, E., Kino, H., Matsuzawa, H. and Wakagi, T. Role of a highly conserved YPITP motif in 2-oxoacid:ferredoxin oxidoreductase: heterologous expression of the gene from Sulfolobus sp.strain 7, and characterization of the recombinant and variant enzymes. Eur. J. Biochem. 268 (2001) 5639–5646. [DOI] [PMID: 11683888]
4.  Fukuda, E. and Wakagi, T. Substrate recognition by 2-oxoacid:ferredoxin oxidoreductase from Sulfolobus sp. strain 7. Biochim. Biophys. Acta 1597 (2002) 74–80. [DOI] [PMID: 12009405]
5.  Nishizawa, Y., Yabuki, T., Fukuda, E. and Wakagi, T. Gene expression and characterization of two 2-oxoacid:ferredoxin oxidoreductases from Aeropyrum pernix K1. FEBS Lett. 579 (2005) 2319–2322. [DOI] [PMID: 15848165]
6.  Park, Y.J., Yoo, C.B., Choi, S.Y. and Lee, H.B. Purifications and characterizations of a ferredoxin and its related 2-oxoacid:ferredoxin oxidoreductase from the hyperthermophilic archaeon, Sulfolobus solfataricus P1. J. Biochem. Mol. Biol. 39 (2006) 46–54. [PMID: 16466637]
[EC 1.2.7.11 created 2013]
 
 
EC 1.4.1.2     
Accepted name: glutamate dehydrogenase
Reaction: L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+
Other name(s): glutamic dehydrogenase; glutamate dehydrogenase (NAD); glutamate oxidoreductase; glutamic acid dehydrogenase; L-glutamate dehydrogenase; NAD-dependent glutamate dehydrogenase; NAD-dependent glutamic dehydrogenase; NAD-glutamate dehydrogenase; NAD-linked glutamate dehydrogenase; NAD-linked glutamic dehydrogenase; NAD-specific glutamic dehydrogenase; NAD-specific glutamate dehydrogenase; NAD:glutamate oxidoreductase; NADH-linked glutamate dehydrogenase
Systematic name: L-glutamate:NAD+ oxidoreductase (deaminating)
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-46-1
References:
1.  Frieden, C. L-Glutamate dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 3–24.
2.  Nisman, B. The Stickland reaction. Bacteriol. Rev. 18 (1954) 16–42. [PMID: 13140081]
3.  Pahlich, E. and Joy, K.W. Glutamate dehydrogenase from pea roots: purification and properties of the enzyme. Can. J. Biochem. 49 (1971) 127–138. [PMID: 4324282]
4.  Smith, E.L., Austen, B.M., Blumenthal, K.M. and Nyc, J.F. Glutamate dehydrogenases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 11, Academic Press, New York, 1975, pp. 293–367.
[EC 1.4.1.2 created 1961]
 
 
EC 1.4.1.3     
Accepted name: glutamate dehydrogenase [NAD(P)+]
Reaction: L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H + H+
Other name(s): glutamic dehydrogenase; glutamate dehydrogenase [NAD(P)]
Systematic name: L-glutamate:NAD(P)+ oxidoreductase (deaminating)
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9029-12-3
References:
1.  Olson, J.A. and Anfinsen, C.B. The crystallization and characterization of L-glutamic acid dehydrogenase. J. Biol. Chem. 197 (1952) 67–79. [PMID: 12981035]
2.  Smith, E.L., Austen, B.M., Blumenthal, K.M. and Nyc, J.F. Glutamate dehydrogenases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 11, Academic Press, New York, 1975, pp. 293–367.
3.  Strecker, H.J. Glutamic dehydrogenase. Arch. Biochem. Biophys. 46 (1953) 128–140. [DOI] [PMID: 13092953]
[EC 1.4.1.3 created 1961]
 
 
EC 1.4.1.4     
Accepted name: glutamate dehydrogenase (NADP+)
Reaction: L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH + H+
Other name(s): glutamic dehydrogenase; dehydrogenase, glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP)
Systematic name: L-glutamate:NADP+ oxidoreductase (deaminating)
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9029-11-2
References:
1.  Coulton, J.W. and Kapoor, M. Purification and some properties of the glutamate dehydrogenase of Salmonella typhimurium. Can. J. Microbiol. 19 (1973) 427–438. [PMID: 4144743]
2.  Grisolia, S., Quijada, C.L. and Fernandez, M. Glutamate dehydrogenase from yeast and from animal tissues. Biochim. Biophys. Acta 81 (1964) 61–70.
3.  Shiio, I. and Ozaki, H. Regulation of nicotinamide adenine dinucleotide phosphate-specific glutamate dehydrogenase from Brevibacterium flavum, a glutamate-producing bacterium. J. Biochem. (Tokyo) 68 (1970) 633–647. [PMID: 4394939]
4.  Smith, E.L., Austen, B.M., Blumenthal, K.M. and Nyc, J.F. Glutamate dehydrogenases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 11, Academic Press, New York, 1975, pp. 293–367.
[EC 1.4.1.4 created 1961]
 
 
EC 1.4.1.13     
Accepted name: glutamate synthase (NADPH)
Reaction: 2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH + H+ (overall reaction)
(1a) L-glutamate + NH3 = L-glutamine + H2O
(1b) L-glutamate + NADP+ + H2O = NH3 + 2-oxoglutarate + NADPH + H+
Other name(s): glutamate (reduced nicotinamide adenine dinucleotide phosphate) synthase; L-glutamate synthase; L-glutamate synthetase; glutamate synthetase (NADP); NADPH-dependent glutamate synthase; glutamine-ketoglutaric aminotransferase; NADPH-glutamate synthase; NADPH-linked glutamate synthase; glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP); L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing; GOGAT
Systematic name: L-glutamate:NADP+ oxidoreductase (transaminating)
Comments: Binds FMN, FAD, 2 [4Fe-4S] clusters and 1 [3Fe-4S] cluster. The reaction takes place in the direction of L-glutamate production. The protein is composed of two subunits, α and β. The α subunit is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.4, glutamate dehydrogenase [NADP+]). The β subunit transfers electrons from the cosubstrate. The NH3 is channeled within the α subunit through a 31 Å channel. The chanelling is very efficient and in the intact α-β complex ammonia is produced only within the complex. In the absence of the β subunit, coupling between the two domains of the α subunit is compromised and some ammonium can leak.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37213-53-9
References:
1.  Miller, R.E. and Stadtman, E.R. Glutamate synthase from Escherichia coli. An iron-sulfide flavoprotein. J. Biol. Chem. 247 (1972) 7407–7419. [PMID: 4565085]
2.  Tempest, D.W., Meers, J.L. and Brown, C.M. Synthesis of glutamate in Aerobacter aerogenes by a hitherto unknown route. Biochem. J. 117 (1970) 405–407. [PMID: 5420057]
3.  Vanoni, M.A. and Curti, B. Glutamate synthase: a complex iron-sulfur flavoprotein. Cell. Mol. Life Sci. 55 (1999) 617–638. [DOI] [PMID: 10357231]
4.  Ravasio, S., Curti, B. and Vanoni, M.A. Determination of the midpoint potential of the FAD and FMN flavin cofactors and of the 3Fe-4S cluster of glutamate synthase. Biochemistry 40 (2001) 5533–5541. [DOI] [PMID: 11331018]
[EC 1.4.1.13 created 1972 as EC 2.6.1.53, transferred 1976 to EC 1.4.1.13, modified 2001, modified 2012]
 
 
EC 1.4.1.14     
Accepted name: glutamate synthase (NADH)
Reaction: 2 L-glutamate + NAD+ = L-glutamine + 2-oxoglutarate + NADH + H+
(1a) L-glutamate + NH3 = L-glutamine + H2O
(1b) L-glutamate + NAD+ + H2O = NH3 + 2-oxoglutarate + NADH + H+
Other name(s): glutamate (reduced nicotinamide adenine dinucleotide) synthase; NADH: GOGAT; L-glutamate synthase (NADH); L-glutamate synthetase; NADH-glutamate synthase; NADH-dependent glutamate synthase
Systematic name: L-glutamate:NAD+ oxidoreductase (transaminating)
Comments: A flavoprotein (FMN). The reaction takes place in the direction of L-glutamate production. The protein is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.2, glutamate dehydrogenase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 65589-88-0
References:
1.  Roon, R.J., Even, H.L. and Larimore, F. Glutamate synthase: properties of the reduced nicotinamide adenine dinucleotide-dependent enzyme from Saccharomyces cerevisiae. J. Bacteriol. 118 (1974) 89–95. [PMID: 4362465]
2.  Boland, M.J. and Benny, A.G. Enzymes of nitrogen metabolism in legume nodules. Purification and properties of NADH-dependent glutamate synthase from lupin nodules. Eur. J. Biochem. 79 (1977) 355–362. [DOI] [PMID: 21790]
3.  Masters, D.S., Jr. and Meister, A. Inhibition of homocysteine sulfonamide of glutamate synthase purified from Saccharomyces cerevisiae. J. Biol. Chem. 257 (1982) 8711–8715. [PMID: 7047525]
4.  Anderson, M.P., Vance, C.P., Heichel, G.H. and Miller, S.S. Purification and characterization of NADH-glutamate synthase from alfalfa root nodules. Plant Physiol. 90 (1989) 351–358. [PMID: 16666762]
5.  Blanco, L., Reddy, P.M., Silvente, S., Bucciarelli, B., Khandual, S., Alvarado-Affantranger, X., Sanchez, F., Miller, S., Vance, C. and Lara-Flores, M. Molecular cloning, characterization and regulation of two different NADH-glutamate synthase cDNAs in bean nodules. Plant Cell Environ. 31 (2008) 454–472. [PMID: 18182018]
[EC 1.4.1.14 created 1978, modified 2019]
 
 
EC 1.4.1.27     
Accepted name: glycine cleavage system
Reaction: glycine + tetrahydrofolate + NAD+ = 5,10-methylenetetrahydrofolate + NH3 + CO2 + NADH
Other name(s): GCV
Systematic name: glycine:NAD+ 2-oxidoreductase (tetrahydrofolate-methylene-adding)
Comments: The glycine cleavage (GCV) system is a large multienzyme complex that belongs to the 2-oxoacid dehydrogenase complex family, which also includes EC 1.2.1.25, branched-chain α-keto acid dehydrogenase system, EC 1.2.1.105, 2-oxoglutarate dehydrogenase system, EC 1.2.1.104, pyruvate dehydrogenase system, and EC 2.3.1.190, acetoin dehydrogenase system. The GCV system catalyses the reversible oxidation of glycine, yielding carbon dioxide, ammonia, 5,10-methylenetetrahydrofolate and a reduced pyridine nucleotide. Tetrahydrofolate serves as a recipient for one-carbon units generated during glycine cleavage to form the methylene group. The GCV system consists of four protein components, the P protein (EC 1.4.4.2, glycine dehydrogenase (aminomethyl-transferring)), T protein (EC 2.1.2.10, aminomethyltransferase), L protein (EC 1.8.1.4, dihydrolipoyl dehydrogenase), and the non-enzyme H protein (lipoyl-carrier protein). The P protein catalyses the pyridoxal phosphate-dependent liberation of CO2 from glycine, leaving a methylamine moiety. The methylamine moiety is transferred to the lipoic acid group of the H protein, which is bound to the P protein prior to decarboxylation of glycine. The T protein catalyses the release of ammonia from the methylamine group and transfers the remaining C1 unit to tetrahydrofolate, forming 5,10-methylenetetrahydrofolate. The L protein then oxidizes the lipoic acid component of the H protein and transfers the electrons to NAD+, forming NADH.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Motokawa, Y. and Kikuchi, G. Glycine metabolism by rat liver mitochondria. Reconstruction of the reversible glycine cleavage system with partially purified protein components. Arch. Biochem. Biophys. 164 (1974) 624–633. [DOI] [PMID: 4460882]
2.  Hiraga, K. and Kikuchi, G. The mitochondrial glycine cleavage system. Functional association of glycine decarboxylase and aminomethyl carrier protein. J. Biol. Chem. 255 (1980) 11671–11676. [PMID: 7440563]
3.  Okamura-Ikeda, K., Fujiwara, K. and Motokawa, Y. Purification and characterization of chicken liver T-protein, a component of the glycine cleavage system. J. Biol. Chem. 257 (1982) 135–139. [PMID: 7053363]
4.  Fujiwara, K., Okamura-Ikeda, K. and Motokawa, Y. Mechanism of the glycine cleavage reaction. Further characterization of the intermediate attached to H-protein and of the reaction catalyzed by T-protein. J. Biol. Chem. 259 (1984) 10664–10668. [PMID: 6469978]
5.  Okamura-Ikeda, K., Ohmura, Y., Fujiwara, K. and Motokawa, Y. Cloning and nucleotide sequence of the gcv operon encoding the Escherichia coli glycine-cleavage system. Eur. J. Biochem. 216 (1993) 539–548. [DOI] [PMID: 8375392]
[EC 1.4.1.27 created 2020]
 
 
EC 1.4.3.7     
Accepted name: D-glutamate oxidase
Reaction: D-glutamate + H2O + O2 = 2-oxoglutarate + NH3 + H2O2
Other name(s): D-glutamic oxidase; D-glutamic acid oxidase
Systematic name: D-glutamate:oxygen oxidoreductase (deaminating)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37255-41-7
References:
1.  Rocca, E. and Ghiretti, F. Purification and properties of D-glutamic acid oxidase from Octopus vulgaris Lam. Arch. Biochem. Biophys. 77 (1958) 336–349. [DOI] [PMID: 13583997]
2.  Urich, K. [D-Glutamate oxidase from the antennal gland of the crayfish Oronectes limosus: purification and characterization] Z. Naturforsch. B 23 (1968) 1508–1511. [PMID: 4387700]
[EC 1.4.3.7 created 1972]
 
 
EC 1.4.3.11     
Accepted name: L-glutamate oxidase
Reaction: L-glutamate + O2 + H2O = 2-oxoglutarate + NH3 + H2O2
Other name(s): glutamate (acceptor) dehydrogenase; glutamate oxidase; glutamic acid oxidase; glutamic dehydrogenase (acceptor); L-glutamic acid oxidase
Systematic name: L-glutamate:oxygen oxidoreductase (deaminating)
Comments: A flavoprotein (FAD).The enzyme from Azotobacter previously listed under this number, which did not produce H2O2, was a crude cell-free extract that probably contained catalase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39346-34-4
References:
1.  Kusakabe, H., Midorikawa, Y., Fujishima, T., Kuninaka, A. and Yoshino, H. Purification and properties of a new enzyme, L-glutamate oxidase, from Streptomyces sp X-119-6 grown on wheat bran. Agric. Biol. Chem. 47 (1983) 1323–1328.
[EC 1.4.3.11 created 1976, modified 1989]
 
 
EC 1.4.3.15     
Accepted name: D-glutamate(D-aspartate) oxidase
Reaction: (1) D-glutamate + H2O + O2 = 2-oxoglutarate + NH3 + H2O2
(2) D-aspartate + H2O + O2 = oxaloacetate + NH3 + H2O2
Other name(s): D-glutamic-aspartic oxidase; D-monoaminodicarboxylic acid oxidase
Systematic name: D-glutamate(D-aspartate):oxygen oxidoreductase (deaminating)
Comments: A flavoprotein (FAD). D-Glutamate and D-aspartate are oxidized at the same rate. Other D-monoaminodicarboxylates, and other D- and L-amino acids, are not oxidized. cf. EC 1.4.3.7, D-glutamate oxidase and EC 1.4.3.1, D-aspartate oxidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9029-20-3
References:
1.  Mizushima, S. Purified D-glutamic-aspartic oxidase of Aspergillus ustus. J. Gen. Appl. Microbiol. 3 (1957) 233–239.
[EC 1.4.3.15 created 1983, modified 2012]
 
 
EC 1.4.7.1     
Accepted name: glutamate synthase (ferredoxin)
Reaction: 2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+ (overall reaction)
(1a) L-glutamate + NH3 = L-glutamine + H2O
(1b) L-glutamate + 2 oxidized ferredoxin + H2O = NH3 + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
Other name(s): ferredoxin-dependent glutamate synthase; ferredoxin-glutamate synthase; glutamate synthase (ferredoxin-dependent)
Systematic name: L-glutamate:ferredoxin oxidoreductase (transaminating)
Comments: Binds a [3Fe-4S] cluster as well as FAD and FMN. The protein is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate. The NH3 is channeled through a 24 Å channel in the active protein. No hydrolysis of glutamine takes place without ferredoxin and 2-oxoglutarate being bound to the protein [5,6].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-56-3
References:
1.  Galván, F., Márquez, A.J. and Vega, J.M. Purification and molecular properties of ferredoxin-glutamate synthase from Chlamydomonas reinhardii. Planta 162 (1984) 180–187. [PMID: 24254054]
2.  Lea, P.J. and Miflin, B.J. Alternative route for nitrogen assimilation in higher plants. Nature (Lond.) 251 (1974) 614–616. [PMID: 4423889]
3.  Ravasio, S., Dossena, L., Martin-Figueroa, E., Florencio, F.J., Mattevi, A., Morandi, P., Curti, B. and Vanoni, M.A. Properties of the recombinant ferredoxin-dependent glutamate synthase of Synechocystis PCC6803. Comparison with the Azospirillum brasilense NADPH-dependent enzyme and its isolated α subunit. Biochemistry 41 (2002) 8120–8133. [DOI] [PMID: 12069605]
4.  Navarro, F., Martin-Figueroa, E., Candau, P. and Florencio, F.J. Ferredoxin-dependent iron-sulfur flavoprotein glutamate synthase (GlsF) from the cyanobacterium Synechocystis sp. PCC 6803: expression and assembly in Escherichia coli. Arch. Biochem. Biophys. 379 (2000) 267–276. [DOI] [PMID: 10898944]
5.  van den Heuvel, R.H., Ferrari, D., Bossi, R.T., Ravasio, S., Curti, B., Vanoni, M.A., Florencio, F.J. and Mattevi, A. Structural studies on the synchronization of catalytic centers in glutamate synthase. J. Biol. Chem. 277 (2002) 24579–24583. [DOI] [PMID: 11967268]
6.  van den Heuvel, R.H., Svergun, D.I., Petoukhov, M.V., Coda, A., Curti, B., Ravasio, S., Vanoni, M.A. and Mattevi, A. The active conformation of glutamate synthase and its binding to ferredoxin. J. Mol. Biol. 330 (2003) 113–128. [DOI] [PMID: 12818206]
[EC 1.4.7.1 created 1976, modified 2012]
 
 
EC 1.5.1.7     
Accepted name: saccharopine dehydrogenase (NAD+, L-lysine-forming)
Reaction: N6-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-lysine + 2-oxoglutarate + NADH + H+
For diagram of lysine catabolism, click here and for diagram of L-lysine synthesis, click here
Glossary: L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine
Other name(s): lysine-2-oxoglutarate reductase; dehydrogenase, saccharopine (nicotinamide adenine dinucleotide, lysine forming); ε-N-(L-glutaryl-2)-L-lysine:NAD oxidoreductase (L-lysine forming); N6-(glutar-2-yl)-L-lysine:NAD oxidoreductase (L-lysine-forming); 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-lysine-forming)
Systematic name: N6-(L-1,3-dicarboxypropyl)-L-lysine:NAD+ oxidoreductase (L-lysine-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9073-96-5
References:
1.  Fujioka, M. and Nakatani, Y. Saccharopine dehydrogenase. Interaction with substrate analogues. Eur. J. Biochem. 25 (1972) 301–307. [DOI] [PMID: 4339117]
2.  Saunders, P.P. and Broquist, H.P. Saccharopine, an intermediate of the aminoadipic acid pathway of lysine biosynthesis. IV. Saccharopine dehydrogenase. J. Biol. Chem. 241 (1966) 3435–3440. [PMID: 4287986]
[EC 1.5.1.7 created 1972]
 
 
EC 1.5.1.8     
Accepted name: saccharopine dehydrogenase (NADP+, L-lysine-forming)
Reaction: N6-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-lysine + 2-oxoglutarate + NADPH + H+
Glossary: L-saccharopine = N6-(L-1,3-dicarboxypropyl)-L-lysine
Other name(s): lysine-2-oxoglutarate reductase; lysine-ketoglutarate reductase; L-lysine-α-ketoglutarate reductase; lysine:α-ketoglutarate:TPNH oxidoreductase (ε-N-[gultaryl-2]-L-lysine forming); saccharopine (nicotinamide adenine dinucleotide phosphate, lysine-forming) dehydrogenase; 6-N-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-lysine-forming)
Systematic name: N6-(L-1,3-dicarboxypropyl)-L-lysine:NADP+ oxidoreductase (L-lysine-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-19-0
References:
1.  Hutzler, J. and Dancis, J. Conversion of lysine to saccharopine by human tissues. Biochim. Biophys. Acta 158 (1968) 62–69. [DOI] [PMID: 4385118]
2.  Markovitz, P.J., Chuang, D.T. and Cox, R.P. Familial hyperlysinemias. Purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities. J. Biol. Chem. 259 (1984) 11643–11646. [PMID: 6434529]
[EC 1.5.1.8 created 1972]
 
 
EC 1.5.1.19     
Accepted name: D-nopaline dehydrogenase
Reaction: N2-(D-1,3-dicarboxypropyl)-L-arginine + NADP+ + H2O = L-arginine + 2-oxoglutarate + NADPH + H+
Other name(s): D-nopaline synthase; nopaline dehydrogenase; nopaline synthase; NOS; 2-N-(D-1,3-dicarboxypropyl)-L-arginine:NADP+ oxidoreductase (L-arginine-forming)
Systematic name: N2-(D-1,3-dicarboxypropyl)-L-arginine:NADP+ oxidoreductase (L-arginine-forming)
Comments: In the reverse direction, forms D-nopaline from L-arginine and D-ornaline from L-ornithine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 64763-57-1
References:
1.  Kemp, J.D., Sutton, D.W. and Hack, E. Purification and characterization of the crown gall specific enzyme nopaline synthase. Biochemistry 18 (1979) 3755–3760. [PMID: 476084]
[EC 1.5.1.19 created 1984]
 
 
EC 1.5.1.51     
Accepted name: N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate dehydrogenase
Reaction: N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate + NAD+ + H2O = 2-oxoglutarate + L-2,3-diaminopropanoate + NADH + H+
Other name(s): SbnB
Systematic name: N-[(2S)-2-amino-2-carboxyethyl]-L-glutamate:NAD+ dehydrogenase (L-2,3-diaminopropanoate-forming)
Comments: The enzyme, characterized from the bacterium Staphylococcus aureus, is involved in the biosynthesis of the siderophore staphyloferrin B.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Beasley, F.C., Cheung, J. and Heinrichs, D.E. Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in Staphylococcus aureus. BMC Microbiol. 11:199 (2011). [DOI] [PMID: 21906287]
2.  Kobylarz, M.J., Grigg, J.C., Takayama, S.J., Rai, D.K., Heinrichs, D.E. and Murphy, M.E. Synthesis of L-2,3-diaminopropionic acid, a siderophore and antibiotic precursor. Chem. Biol. 21 (2014) 379–388. [DOI] [PMID: 24485762]
[EC 1.5.1.51 created 2017]
 
 
EC 1.13.12.15     
Accepted name: 3,4-dihydroxyphenylalanine oxidative deaminase
Reaction: 2 L-dopa + O2 = 2 3,4-dihydroxyphenylpyruvate + 2 NH3
Glossary: L-dopa = 3,4-dihydroxy-L-phenylalanine
Other name(s): 3,4-dihydroxy-L-phenylalanine: oxidative deaminase; oxidative deaminase; DOPA oxidative deaminase; DOPAODA
Systematic name: 3,4-dihydroxy-L-phenylalanine:oxygen oxidoreductase (deaminating)
Comments: This enzyme is one of the three enzymes involved in L-dopa (3,4-dihydroxy-L-phenylalanine) catabolism in the non-oxygenic phototrophic bacterium Rubrivivax benzoatilyticus OU5 (and not Rhodobacter sphaeroides OU5 as had been thought [1]), the other two being EC 4.3.1.22 (dihydroxyphenylalanine reductive deaminase) and EC 2.6.1.49 (3,4-dihydroxyphenylalanine transaminase). In addition to L-dopa, the enzyme can also use L-tyrosine, L-phenylalanine, L-tryptophan and glutamate as substrate, but more slowly. The enzyme is inhibited by NADH and 2-oxoglutarate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Ranjith, N.K., Ramana, Ch.V. and Sasikala, Ch. Purification and characterization of 3,4-dihydroxyphenylalanine oxidative deaminase from Rhodobacter sphaeroides OU5. Can. J. Microbiol. 54 (2008) 829–834. [DOI] [PMID: 18923551]
[EC 1.13.12.15 created 2008]
 
 
EC 1.13.12.19     
Accepted name: 2-oxoglutarate dioxygenase (ethene-forming)
Reaction: 2-oxoglutarate + O2 = ethene + 3 CO2 + H2O
Glossary: ethene = ethylene
Other name(s): ethylene-forming enzyme; EFE; 2-oxoglutarate dioxygenase (ethylene-forming); 2-oxoglutarate:oxygen oxidoreductase (decarboxylating, ethylene-forming)
Systematic name: 2-oxoglutarate:oxygen oxidoreductase (decarboxylating, ethene-forming)
Comments: This is one of two simultaneous reactions catalysed by the enzyme, which is responsible for ethene production in bacteria of the Pseudomonas syringae group. In the other reaction [EC 1.14.20.7, 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)] the enzyme catalyses the mono-oxygenation of both 2-oxoglutarate and L-arginine, forming succinate, carbon dioxide and 5-hydroxy-L-arginine, which is subsequently cleaved into guanidine and (S)-1-pyrroline-5-carboxylate.The enzymes catalyse two cycles of the ethene-forming reaction for each cycle of the succinate-forming reaction, so that the stoichiometry of the products ethene and succinate is 2:1.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Nagahama, K., Ogawa, T., Fujii, T., Tazaki, M., Tanase, S., Morino, Y. and Fukuda, H. Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2. J. Gen. Microbiol. 137 (1991) 2281–2286. [DOI] [PMID: 1770346]
2.  Fukuda, H., Ogawa, T., Tazaki, M., Nagahama, K., Fujii, T., Tanase, S. and Morino, Y. Two reactions are simultaneously catalyzed by a single enzyme: the arginine-dependent simultaneous formation of two products, ethylene and succinate, from 2-oxoglutarate by an enzyme from Pseudomonas syringae. Biochem. Biophys. Res. Commun. 188 (1992) 483–489. [DOI] [PMID: 1445291]
3.  Fukuda, H., Ogawa, T., Ishihara, K., Fujii, T., Nagahama, K., Omata, T., Inoue, Y., Tanase, S. and Morino, Y. Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of Pseudomonas syringae pv. phaseolicola PK2. Biochem. Biophys. Res. Commun. 188 (1992) 826–832. [DOI] [PMID: 1445325]
[EC 1.13.12.19 created 2011]
 
 
EC 1.14.11.1     
Accepted name: γ-butyrobetaine dioxygenase
Reaction: 4-trimethylammoniobutanoate + 2-oxoglutarate + O2 = 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO2
Other name(s): α-butyrobetaine hydroxylase; γ-butyrobetaine hydroxylase; butyrobetaine hydroxylase
Systematic name: 4-trimethylammoniobutanoate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9045-31-2
References:
1.  Lindstedt, G. and Lindstedt, S. Cofactor requirements of γ-butyrobetaine hydroxylase from rat liver. J. Biol. Chem. 245 (1970) 4178–4186. [PMID: 4396068]
[EC 1.14.11.1 created 1972]
 
 
EC 1.14.11.2     
Accepted name: procollagen-proline 4-dioxygenase
Reaction: procollagen L-proline + 2-oxoglutarate + O2 = procollagen trans-4-hydroxy-L-proline + succinate + CO2
For diagram of reaction, click here
Other name(s): P4HA (gene name); P4HB (gene name); protocollagen hydroxylase; proline hydroxylase; proline,2-oxoglutarate 4-dioxygenase; collagen proline hydroxylase; hydroxylase, collagen proline; peptidyl proline hydroxylase; proline protocollagen hydroxylase; proline, 2-oxoglutarate dioxygenase; prolyl hydroxylase; prolylprotocollagen dioxygenase; prolylprotocollagen hydroxylase; protocollagen proline 4-hydroxylase; protocollagen proline dioxygenase; protocollagen proline hydroxylase; protocollagen prolyl hydroxylase; prolyl 4-hydroxylase; prolyl-glycyl-peptide, 2-oxoglutarate:oxygen oxidoreductase, 4-hydroxylating; procollagen-proline 4-dioxygenase (ambiguous)
Systematic name: procollagen-L-proline,2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating)
Comments: Requires Fe2+ and ascorbate.The enzyme, which is located within the lumen of the endoplasmic reticulum, catalyses the 4-hydroxylation of prolines in -X-Pro-Gly- sequences. The 4-hydroxyproline residues are essential for the formation of the collagen triple helix. The enzyme forms a complex with protein disulfide isomerase and acts not only on procollagen but also on more than 15 other proteins that have collagen-like domains.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9028-06-2
References:
1.  Hutton, J.J., Jr., Tappel, A.L. and Udenfriend, S. Cofactor and substrate requirements of collagen proline hydroxylase. Arch. Biochem. Biophys. 118 (1967) 231–240.
2.  Kivirikko, K.I. and Prockop, D.J. Purification and partial characterization of the enzyme for the hydroxylation of proline in protocollogen. Arch. Biochem. Biophys. 118 (1967) 611–618.
3.  Kivirikko, K.I., Kishida, Y., Sakakibara, S. and Prockop, J. Hydroxylation of (X-Pro-Gly)n by protocollagen proline hydroxylase. Effect of chain length, helical conformation and amino acid sequence in the substrate. Biochim. Biophys. Acta 271 (1972) 347–356. [DOI] [PMID: 5046811]
4.  Berg, R.A. and Prockop, D.J. Affinity column purification of protocollagen proline hydroxylase from chick embryos and further characterization of the enzyme. J. Biol. Chem. 248 (1973) 1175–1182. [PMID: 4346946]
5.  John, D.C. and Bulleid, N.J. Prolyl 4-hydroxylase: defective assembly of α-subunit mutants indicates that assembled α-subunits are intramolecularly disulfide bonded. Biochemistry 33 (1994) 14018–14025. [PMID: 7947811]
6.  Lamberg, A., Pihlajaniemi, T. and Kivirikko, K.I. Site-directed mutagenesis of the α subunit of human prolyl 4-hydroxylase. Identification of three histidine residues critical for catalytic activity. J. Biol. Chem. 270 (1995) 9926–9931. [DOI] [PMID: 7730375]
7.  Myllyharju, J. and Kivirikko, K.I. Characterization of the iron- and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase. EMBO J. 16 (1997) 1173–1180. [DOI] [PMID: 9135134]
8.  Kivirikko, K.I. and Myllyharju, J. Prolyl 4-hydroxylases and their protein disulfide isomerase subunit. Matrix Biol 16 (1998) 357–368. [DOI] [PMID: 9524356]
[EC 1.14.11.2 created 1972, modified 1981, modified 1983, modified 2017]
 
 
EC 1.14.11.3     
Accepted 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 iron(II) and ascorbate. Also acts on thymidine. cf. EC 1.14.11.10, pyrimidine-deoxynucleoside 1′-dioxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, 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]
[EC 1.14.11.3 created 1972, modified 1976, modified 1989, modified 2002]
 
 
EC 1.14.11.4     
Accepted name: procollagen-lysine 5-dioxygenase
Reaction: [procollagen]-L-lysine + 2-oxoglutarate + O2 = [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
Other name(s): lysine hydroxylase; lysine,2-oxoglutarate 5-dioxygenase; protocollagen lysine dioxygenase; collagen lysine hydroxylase; lysine-2-oxoglutarate dioxygenase; lysyl hydroxylase; lysylprotocollagen dioxygenase; protocollagen lysyl hydroxylase; peptidyl-lysine, 2-oxoglutarate: oxygen oxidoreductase; peptidyllysine, 2-oxoglutarate:oxygen 5-oxidoreductase; protocollagen lysine hydroxylase; procollagen-L-lysine,2-oxoglutarate:oxygen oxidoreductase (5-hydroxylating); L-lysine-[procollagen],2-oxoglutarate:oxygen oxidoreductase (5-hydroxylating)
Systematic name: [procollagen]-L-lysine,2-oxoglutarate:oxygen oxidoreductase (5-hydroxylating)
Comments: Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9059-25-0
References:
1.  Hausmann, E. Cofactor requirements for the enzymatic hydroxylation of lysine in a polypeptide precursor of collagen. Biochim. Biophys. Acta 133 (1967) 591–598. [DOI] [PMID: 6033801]
2.  Rhoads, R.E. and Udenfriend, S. Decarboxylation of α-ketoglutarate coupled to collagen proline hydroxylase. Proc. Natl. Acad. Sci. USA 60 (1968) 1473–1478. [DOI] [PMID: 5244754]
3.  Puistola, U., Turpeenniemi-Hujanen, T.M., Myllyla, R. and Kivirikko, K.I. Studies on the lysyl hydroxylase reaction. I. Initial velocity kinetics and related aspects. Biochim. Biophys. Acta 611 (1980) 40–50. [DOI] [PMID: 6766066]
4.  Puistola, U., Turpeenniemi-Hujanen, T.M., Myllyla, R. and Kivirikko, K.I. Studies on the lysyl hydroxylase reaction. II. Inhibition kinetics and the reaction mechanism. Biochim. Biophys. Acta 611 (1980) 51–60. [DOI] [PMID: 6766067]
[EC 1.14.11.4 created 1972, modified 1983]
 
 
EC 1.14.11.5      
Deleted entry:  5-hydroxymethyluracil,2-oxoglutarate dioxygenase. Now included with EC 1.14.11.6 thymine dioxygenase
[EC 1.14.11.5 created 1972, deleted 1976]
 
 
EC 1.14.11.6     
Accepted name: thymine dioxygenase
Reaction: thymine + 2-oxoglutarate + O2 = 5-hydroxymethyluracil + succinate + CO2
Other name(s): thymine 7-hydroxylase; 5-hydroxy-methyluracil dioxygenase; 5-hydroxymethyluracil oxygenase
Systematic name: thymine,2-oxoglutarate:oxygen oxidoreductase (7-hydroxylating)
Comments: Requires Fe2+ and ascorbate. Also acts on 5-hydroxymethyluracil to oxidize its -CH2OH group first to -CHO and then to -COOH.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37256-67-0
References:
1.  Bankel, L., Holme, E., Lindstedt, G. and Lindstedt, S. Oxygenases involved in thymine and thymidine metabolism in Neurospora crassa. FEBS Lett. 21 (1972) 135–138. [DOI] [PMID: 11946494]
2.  Liu, C.-K., Hsu, C.-A. and Abbott, M.T. Catalysis of three sequential dioxygenase reactions by thymine 7-hydroxylase. Arch. Biochem. Biophys. 159 (1973) 180–187. [DOI] [PMID: 4274083]
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]
[EC 1.14.11.6 created 1972, modified 1976 (EC 1.14.11.5 created 1972, incorporated 1976)]
 
 
EC 1.14.11.7     
Accepted name: procollagen-proline 3-dioxygenase
Reaction: [procollagen]-L-proline + 2-oxoglutarate + O2 = [procollagen]-trans-3-hydroxy-L-proline + succinate + CO2
For diagram of reaction, click here
Other name(s): proline,2-oxoglutarate 3-dioxygenase; prolyl 3-hydroxylase; protocollagen proline 3-hydroxylase; prolyl-4-hydroxyprolyl-glycyl-peptide,2-oxoglutarate:oxygen oxidoreductase, 3-hydroxylating
Systematic name: [procollagen]-L-proline,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires Fe2+ and ascorbate. The enzyme forms a complex with protein disulfide isomerase, and is located in the endoplasmic reticulum. It modifies proline residues within the procollagen peptide of certain collagen types. The modification is essential for proper collagen triple helix formation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 63551-75-7
References:
1.  Risteli, J., Tryggvason, K. and Kivirikko, K.I. Prolyl 3-hydroxylase: partial characterization of the enzyme from rat kidney cortex. Eur. J. Biochem. 73 (1977) 485–492. [DOI] [PMID: 191255]
2.  Risteli, J., Tryggvason, K. and Kivirikko, K.I. A rapid assay for prolyl 3-hydroxylase activity. Anal. Biochem. 84 (1978) 423–431. [DOI] [PMID: 204218]
3.  Vranka, J.A., Sakai, L.Y. and Bachinger, H.P. Prolyl 3-hydroxylase 1, enzyme characterization and identification of a novel family of enzymes. J. Biol. Chem. 279 (2004) 23615–23621. [DOI] [PMID: 15044469]
4.  Tiainen, P., Pasanen, A., Sormunen, R. and Myllyharju, J. Characterization of recombinant human prolyl 3-hydroxylase isoenzyme 2, an enzyme modifying the basement membrane collagen IV. J. Biol. Chem. 283 (2008) 19432–19439. [DOI] [PMID: 18487197]
[EC 1.14.11.7 created 1981, modified 1983, modified 2017]
 
 
EC 1.14.11.8     
Accepted name: trimethyllysine dioxygenase
Reaction: N6,N6,N6-trimethyl-L-lysine + 2-oxoglutarate + O2 = (3S)-3-hydroxy-N6,N6,N6-trimethyl-L-lysine + succinate + CO2
Other name(s): trimethyllysine α-ketoglutarate dioxygenase; TML-α-ketoglutarate dioxygenase; TML hydroxylase; 6-N,6-N,6-N-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Systematic name: N6,N6,N6-trimethyl-L-lysine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires Fe2+ and ascorbate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 74622-49-4
References:
1.  Hulse, J.D., Ellis, S.R. and Henderson, L.M. Carnitine biosynthesis. β-Hydroxylation of trimethyllysine by an α-ketoglutarate-dependent mitochondrial dioxygenase. J. Biol. Chem. 253 (1978) 1654–1659. [PMID: 627563]
2.  Al Temimi, A.H., Pieters, B.J., Reddy, Y.V., White, P.B. and Mecinovic, J. Substrate scope for trimethyllysine hydroxylase catalysis. Chem. Commun. (Camb.) 52 (2016) 12849–12852. [PMID: 27730239]
3.  Lesniak, R.K., Markolovic, S., Tars, K. and Schofield, C.J. Human carnitine biosynthesis proceeds via (2S,3S)-3-hydroxy-Nε-trimethyllysine. Chem. Commun. (Camb.) 53 (2016) 440–442. [PMID: 27965989]
4.  Reddy, Y.V., Al Temimi, A.H., White, P.B. and Mecinovic, J. Evidence that trimethyllysine hydroxylase catalyzes the formation of (2S,3S)-3-hydroxy-Nε-trimethyllysine. Org. Lett. 19 (2017) 400–403. [PMID: 28045275]
[EC 1.14.11.8 created 1983]
 
 
EC 1.14.11.9     
Accepted name: flavanone 3-dioxygenase
Reaction: a (2S)-flavan-4-one + 2-oxoglutarate + O2 = a (2R,3R)-dihydroflavonol + succinate + CO2
For diagram of flavonoid biosynthesis, click here and for diagram of naringenin derivatives biosynthesis, click here
Other name(s): naringenin 3-hydroxylase; flavanone 3-hydroxylase; flavanone 3β-hydroxylase; flavanone synthase I; (2S)-flavanone 3-hydroxylase; naringenin,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating); F3H; flavanone,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Systematic name: (2S)-flavan-4-one,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Comments: Requires Fe2+ and ascorbate. This plant enzyme catalyses an early step in the flavonoid biosynthesis pathway, leading to the production of flavanols and anthocyanins. Substrates include (2S)-naringenin, (2S)-eriodictyol, (2S)-dihydrotricetin and (2S)-pinocembrin. Some enzymes are bifuctional and also catalyse EC 1.14.20.6, flavonol synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 75991-43-4
References:
1.  Forkmann, G., Heller, W. and Grisebach, H. Anthocyanin biosynthesis in flowers of Matthiola incana flavanone 3- and flavonoid 3′-hydroxylases. Z. Naturforsch. C: Biosci. 35 (1980) 691–695.
2.  Charrier, B., Coronado, C., Kondorosi, A. and Ratet, P. Molecular characterization and expression of alfalfa (Medicago sativa L.) flavanone-3-hydroxylase and dihydroflavonol-4-reductase encoding genes. Plant Mol. Biol. 29 (1995) 773–786. [PMID: 8541503]
3.  Pelletier, M.K. and Shirley, B.W. Analysis of flavanone 3-hydroxylase in Arabidopsis seedlings. Coordinate regulation with chalcone synthase and chalcone isomerase. Plant Physiol. 111 (1996) 339–345. [PMID: 8685272]
4.  Wellmann, F., Matern, U. and Lukačin, R. Significance of C-terminal sequence elements for Petunia flavanone 3β-hydroxylase activity. FEBS Lett. 561 (2004) 149–154. [DOI] [PMID: 15013767]
5.  Jin, Z., Grotewold, E., Qu, W., Fu, G. and Zhao, D. Cloning and characterization of a flavanone 3-hydroxylase gene from Saussurea medusa. DNA Seq 16 (2005) 121–129. [DOI] [PMID: 16147863]
6.  Shen, G., Pang, Y., Wu, W., Deng, Z., Zhao, L., Cao, Y., Sun, X. and Tang, K. Cloning and characterization of a flavanone 3-hydroxylase gene from Ginkgo biloba. Biosci Rep 26 (2006) 19–29. [DOI] [PMID: 16779664]
[EC 1.14.11.9 created 1983, modified 1989, modified 2004, modified 2016]
 
 


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