The Enzyme Database

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EC 1.1.1.24     
Accepted name: quinate dehydrogenase
Reaction: L-quinate + NAD+ = 3-dehydroquinate + NADH + H+
For diagram of shikimate and chorismate biosynthesis, click here
Glossary: quinate = (1R,3R,4R,5R)-1,3,4,5-tetrahydroxycyclohexanecarboxylic acid and is a cyclical carboxylate
The numbering system used for the 3-dehydroquinate is that of the recommendations on cyclitols, sections I-8 and I-9: and is shown in the reaction diagram. The use of the term ’5-dehydroquinate’ for this compound is based on an earlier system of numbering.
Other name(s): quinic dehydrogenase; quinate:NAD oxidoreductase; quinate 5-dehydrogenase; quinate:NAD+ 5-oxidoreductase
Systematic name: L-quinate:NAD+ 3-oxidoreductase
Comments: The enzyme is specific for quinate as substrate; phenylpyruvate, phenylalanine, cinnamate and shikimate will not act as substrates. NAD+ cannot be replaced by NADP+.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9028-28-8
References:
1.  Gamborg, O.L. Aromatic metabolism in plants. III. Quinate dehydrogenase from mung bean cell suspension cultures. Biochim. Biophys. Acta 128 (1966) 483–491.
2.  Mitsuhashi, S. and Davis, B.D. Aromatic biosynthesis. XIII. Conversion of quinic acid to 5-dehydroquinic acid by quinic dehydrogenase. Biochim. Biophys. Acta 15 (1954) 268–280. [DOI] [PMID: 13208693]
[EC 1.1.1.24 created 1961, modified 1976, modified 2004]
 
 
EC 1.1.1.96     
Accepted name: diiodophenylpyruvate reductase
Reaction: 3-(3,5-diiodo-4-hydroxyphenyl)lactate + NAD+ = 3-(3,5-diiodo-4-hydroxyphenyl)pyruvate + NADH + H+
Other name(s): aromatic α-keto acid; KAR; 2-oxo acid reductase
Systematic name: 3-(3,5-diiodo-4-hydroxyphenyl)lactate:NAD+ oxidoreductase
Comments: Substrates contain an aromatic ring with a pyruvate side chain. The most active substrates are halogenated derivatives. Compounds with hydroxy or amino groups in the 3 or 5 position are inactive.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 37250-31-0
References:
1.  Zannoni, V.G. and Weber, W.W. Isolation and properties of aromatic α-keto acid reductase. J. Biol. Chem. 241 (1966) 1340–1344. [PMID: 5935348]
[EC 1.1.1.96 created 1972]
 
 
EC 1.1.1.110     
Accepted name: aromatic 2-oxoacid reductase
Reaction: (1) (R)-3-(phenyl)lactate + NAD+ = 3-phenylpyruvate + NADH + H+
(2) (R)-3-(4-hydroxyphenyl)lactate + NAD+ = 3-(4-hydroxyphenyl)pyruvate + NADH + H+
(3) (R)-(indol-3-yl)lactate + NAD+ = (indol-3-yl)pyruvate + NADH + H+
Glossary: 3-phenylpyruvate = 2-oxo-3-phenylpropanoate
Other name(s): (R)-aromatic lactate dehydrogenase; (R)-4-hydroxyphenyllactate dehydrogenase; indolelactate:NAD+ oxidoreductase; indolelactate dehydrogenase; fldH (gene name); (indol-3-yl)lactate:NAD+ oxidoreductase
Systematic name: aromatic 2-oxoacid:NAD+ oxidoreductase
Comments: The enzymes from anaerobic bacteria such as Clostridium sporogenes participate in the fermentation pathways of L-phenylalanine, L-tyrosine and L-tryptophan. The enzyme from the yeast Candida maltosa has similar activity, but, unlike the bacterial enzyme, requires Mn2+ and can also use NADPH with lower activity.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 37250-41-2
References:
1.  Jean, M. and DeMoss, R.D. Indolelactate dehydrogenase from Clostridium sporogenes. Can. J. Microbiol. 14 (1968) 429–435. [PMID: 4384683]
2.  Giesel, H. and Simon, H. On the occurrence of enoate reductase and 2-oxo-carboxylate reductase in clostridia and some observations on the amino acid fermentation by Peptostreptococcus anaerobius. Arch. Microbiol. 135 (1983) 51–57. [PMID: 6354130]
3.  Bode, R., Lippoldt, A. and Birnbaum, D. Purification and properties of D-aromatic lactate dehydrogenase an enzyme involved in the catabolism of the aromatic amino acids of Candida maltosa. Biochem. Physiol. Pflanzen 181 (1986) 189–198.
4.  Dickert, S., Pierik, A.J., Linder, D. and Buckel, W. The involvement of coenzyme A esters in the dehydration of (R)-phenyllactate to (E)-cinnamate by Clostridium sporogenes. Eur. J. Biochem. 267 (2000) 3874–3884. [DOI] [PMID: 10849007]
5.  Dodd, D., Spitzer, M.H., Van Treuren, W., Merrill, B.D., Hryckowian, A.J., Higginbottom, S.K., Le, A., Cowan, T.M., Nolan, G.P., Fischbach, M.A. and Sonnenburg, J.L. A gut bacterial pathway metabolizes aromatic amino acids into nine circulating metabolites. Nature 551 (2017) 648–652. [PMID: 29168502]
[EC 1.1.1.110 created 1972 (EC 1.1.1.222 created 2000, incorporated 2018), modified 2018]
 
 
EC 1.1.1.237     
Accepted name: hydroxyphenylpyruvate reductase
Reaction: (1) (R)-3-(4-hydroxyphenyl)lactate + NAD(P)+ = 3-(4-hydroxyphenyl)pyruvate + NAD(P)H + H+
(2) (R)-3-(3,4-dihydroxyphenyl)lactate + NAD(P)+ = 3-(3,4-dihydroxyphenyl)pyruvate + NAD(P)H + H+
For diagram of 4-hydroxyphenylpyruvate metabolites, click here and for diagram of rosmarinate biosynthesis, click here
Other name(s): HPPR
Systematic name: (R)-3-(4-hydroxyphenyl)lactate:NAD(P)+ oxidoreductase
Comments: The enzyme participates in the biosynthesis of rosmarinic acid. It belongs to the family of D-isomer-specific 2-hydroxyacid dehydrogenases, and prefers NADPH to NADH.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 117590-77-9
References:
1.  Petersen, M. and Alfermann, A.W. Two new enzymes of rosmarinic acid biosynthesis from cell cultures of Coleus blumei: hydroxyphenylpyruvate reductase and rosmarinic acid synthase. Z. Naturforsch. C: Biosci. 43 (1988) 501–504.
2.  Kim, K.H., Janiak, V. and Petersen, M. Purification, cloning and functional expression of hydroxyphenylpyruvate reductase involved in rosmarinic acid biosynthesis in cell cultures of Coleus blumei. Plant Mol. Biol. 54 (2004) 311–323. [PMID: 15284489]
3.  Kim, Y.B., Uddina, M.R., Kim, Y., Park, C.G. and Park, S.U. Molecular cloning and characterization of tyrosine aminotransferase and hydroxyphenylpyruvate reductase, and rosmarinic acid accumulation in Scutellaria baicalensis. Nat. Prod. Commun. 9 (2014) 1311–1314. [PMID: 25918800]
4.  Wang, G.Q., Chen, J.F., Yi, B., Tan, H.X., Zhang, L. and Chen, W.S. HPPR encodes the hydroxyphenylpyruvate reductase required for the biosynthesis of hydrophilic phenolic acids in Salvia miltiorrhiza. Chin J Nat Med 15 (2017) 917–927. [PMID: 29329649]
[EC 1.1.1.237 created 1992, modified 2018]
 
 
EC 1.1.1.345     
Accepted name: D-2-hydroxyacid dehydrogenase (NAD+)
Reaction: an (R)-2-hydroxycarboxylate + NAD+ = a 2-oxocarboxylate + NADH + H+
Other name(s): LdhA; HdhD; D-2-hydroxyisocaproate dehydrogenase; R-HicDH; D-HicDH; (R)-2-hydroxy-4-methylpentanoate:NAD+ oxidoreductase; (R)-2-hydroxyisocaproate dehydrogenase; D-mandelate dehydrogenase (ambiguous)
Systematic name: (R)-2-hydroxycarboxylate:NAD+ oxidoreductase
Comments: The enzymes, characterized from bacteria (Peptoclostridium difficile, Enterococcus faecalis and from lactic acid bacteria) prefer substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain. It also utilizes phenylpyruvate. The enzyme from the halophilic archaeon Haloferax mediterranei prefers substrates with a main chain of 3-4 carbons (pyruvate and 2-oxobutanoate). cf. EC 1.1.1.272, (D)-2-hydroxyacid dehydrogenase (NADP+).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Dengler, U., Niefind, K., Kiess, M. and Schomburg, D. Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 Å resolution. J. Mol. Biol. 267 (1997) 640–660. [DOI] [PMID: 9126843]
2.  Bonete, M.J., Ferrer, J., Pire, C., Penades, M. and Ruiz, J.L. 2-Hydroxyacid dehydrogenase from Haloferax mediterranei, a D-isomer-specific member of the 2-hydroxyacid dehydrogenase family. Biochimie 82 (2000) 1143–1150. [DOI] [PMID: 11120357]
3.  Kim, J., Darley, D., Selmer, T. and Buckel, W. Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme A transferase involved in reduction of L-leucine to isocaproate by Clostridium difficile. Appl. Environ. Microbiol. 72 (2006) 6062–6069. [DOI] [PMID: 16957230]
4.  Wada, Y., Iwai, S., Tamura, Y., Ando, T., Shinoda, T., Arai, K. and Taguchi, H. A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases. Biosci. Biotechnol. Biochem. 72 (2008) 1087–1094. [DOI] [PMID: 18391442]
5.  Chambellon, E., Rijnen, L., Lorquet, F., Gitton, C., van Hylckama Vlieg, J.E., Wouters, J.A. and Yvon, M. The D-2-hydroxyacid dehydrogenase incorrectly annotated PanE is the sole reduction system for branched-chain 2-keto acids in Lactococcus lactis. J. Bacteriol. 191 (2009) 873–881. [DOI] [PMID: 19047348]
6.  Miyanaga, A., Fujisawa, S., Furukawa, N., Arai, K., Nakajima, M. and Taguchi, H. The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase. Biochem. Biophys. Res. Commun. 439 (2013) 109–114. [DOI] [PMID: 23954635]
[EC 1.1.1.345 created 2013]
 
 
EC 1.2.3.13     
Accepted name: 4-hydroxyphenylpyruvate oxidase
Reaction: 2 4-hydroxyphenylpyruvate + O2 = 2 4-hydroxyphenylacetate + 2 CO2
For diagram of 4-hydroxyphenylpyruvate metabolites, click here
Systematic name: 4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating)
Comments: Involved in tyrosine degradation pathway in Arthrobacter sp.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 78213-74-8
References:
1.  Blakley, E.R. The catabolism of L-tyrosine by an Arthrobacter sp. Can. J. Microbiol. 23 (1977) 1128–1139. [PMID: 20216]
[EC 1.2.3.13 created 2000]
 
 
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 1.3.1.12     
Accepted name: prephenate dehydrogenase
Reaction: prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH
For diagram of phenylalanine and tyrosine biosynthesis, click here
Other name(s): hydroxyphenylpyruvate synthase; chorismate mutase—prephenate dehydrogenase
Systematic name: prephenate:NAD+ oxidoreductase (decarboxylating)
Comments: This enzyme in the enteric bacteria also possesses chorismate mutase activity (EC 5.4.99.5 chorismate mutase) and converts chorismate into prephenate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9044-92-2
References:
1.  Koch, G.L.E., Shaw, D.C. and Gibson, F. Tyrosine biosynthesis in Aerobacter aerogenes. Purification and properties of chorismate mutase-prephenate dehydrogenase. Biochim. Biophys. Acta 212 (1970) 375–386. [DOI] [PMID: 5456988]
[EC 1.3.1.12 created 1972]
 
 
EC 1.3.1.13     
Accepted name: prephenate dehydrogenase (NADP+)
Reaction: prephenate + NADP+ = 4-hydroxyphenylpyruvate + CO2 + NADPH
For diagram of phenylalanine and tyrosine biosynthesis, click here
Other name(s): prephenate dehydrogenase (ambiguous); prephenate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; prephenate dehydrogenase (NADP)
Systematic name: prephenate:NADP+ oxidoreductase (decarboxylating)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37251-11-9
References:
1.  Gamborg, O.L. and Keeley, F.W. Aromatic metabolism in plants. I. A study of the prephenate dehydrogenase from bean plants. Biochim. Biophys. Acta 115 (1966) 65–72. [DOI] [PMID: 4379953]
[EC 1.3.1.13 created 1972]
 
 
EC 1.4.1.20     
Accepted name: phenylalanine dehydrogenase
Reaction: L-phenylalanine + H2O + NAD+ = phenylpyruvate + NH3 + NADH + H+
Other name(s): L-phenylalanine dehydrogenase; PHD
Systematic name: L-phenylalanine:NAD+ oxidoreductase (deaminating)
Comments: The enzymes from Bacillus badius and Sporosarcina ureae are highly specific for L-phenylalanine; that from Bacillus sphaericus also acts on L-tyrosine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 69403-12-9
References:
1.  Asano, Y., Nakazawa, A. and Endo, K. Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization. J. Biol. Chem. 262 (1987) 10346–10354. [PMID: 3112142]
2.  Asano, Y., Nakazawa, A., Endo, K., Hibino, Y., Ohmori, M., Numao, N. and Kondo, K. Phenylalanine dehydrogenase of Bacillus badius. Purification, characterization and gene cloning. Eur. J. Biochem. 168 (1987) 153–159. [DOI] [PMID: 3311741]
[EC 1.4.1.20 created 1989]
 
 
EC 1.13.11.27     
Accepted name: 4-hydroxyphenylpyruvate dioxygenase
Reaction: 4-hydroxyphenylpyruvate + O2 = homogentisate + CO2
For diagram of 4-hydroxyphenylpyruvate metabolites, click here
Other name(s): p-hydroxyphenylpyruvic hydroxylase; p-hydroxyphenylpyruvate hydroxylase; p-hydroxyphenylpyruvate oxidase; p-hydroxyphenylpyruvic oxidase; p-hydroxyphenylpyruvate dioxygenase; p-hydroxyphenylpyruvic acid hydroxylase; 4-hydroxyphenylpyruvic acid dioxygenase
Systematic name: 4-hydroxyphenylpyruvate:oxygen oxidoreductase (hydroxylating, decarboxylating)
Comments: The Pseudomonas enzyme contains one Fe3+ per mole of enzyme; the enzymes from other sources may contain essential iron or copper.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9029-72-5
References:
1.  Lindstedt, S. and Rundgren, M. Blue color, metal content, and substrate binding in 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874. J. Biol. Chem. 257 (1982) 11922–11931. [PMID: 7118918]
2.  Roche, P.A., Moorehead, T.J. and Hamilton, G.A. Purification and properties of hog liver 4-hydroxyphenylpyruvate dioxygenase. Arch. Biochem. Biophys. 216 (1982) 62–73. [DOI] [PMID: 7103516]
[EC 1.13.11.27 created 1961 as EC 1.99.1.14, transferred 1965 to EC 1.14.2.2, transferred 1972 to EC 1.13.11.27]
 
 
EC 1.13.11.46     
Accepted name: 4-hydroxymandelate synthase
Reaction: 4-hydroxyphenylpyruvate + O2 = (S)-4-hydroxymandelate + CO2
For diagram of 4-hydroxyphenylpyruvate metabolites, click here
Glossary: (S)-4-hydroxymandelate = (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate
Other name(s): 4-hydroxyphenylpyruvate dioxygenase II
Systematic name: (S)-4-hydroxyphenylpyruvate:oxygen oxidoreductase (decarboxylating)
Comments: Requires Fe2+. Involved in the biosynthesis of the vancomycin group of glycopeptide antibiotics.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 280566-04-3
References:
1.  Hubbard, B.K., Thomas, M.G. and Walsh, C.T. Biosynthesis of L-p-hydroxyphenylglycine, a non-proteinogenic amino acid constituent of peptide antibiotics. Chem. Biol. 7 (2000) 931–942. [DOI] [PMID: 11137816]
2.  Choroba, O.W., Williams, D.H. and Spencer, J.B. Biosynthesis of the vancomycin group of antibiotics: involvement of an unusual dioxygenase in the pathway to (S)-4-hydroxyphenylglycine. J. Am. Chem. Soc. 122 (2000) 5389–5390.
[EC 1.13.11.46 created 2001]
 
 
EC 1.13.11.83     
Accepted name: 4-hydroxy-3-prenylphenylpyruvate oxygenase
Reaction: 3-dimethylallyl-4-hydroxyphenylpyruvate + O2 = 3-dimethylallyl-4-hydroxymandelate + CO2
For diagram of 3-dimethylallyl-4-hydroxybenzoate biosynthesis, click here
Other name(s): CloR
Systematic name: 3-dimethylallyl-4-hydroxyphenylpyruvate:oxygen 1,2-oxidoreductase (3-dimethylallyl-4-hydroxymandelate forming)
Comments: Requires non-heme-Fe(II). Isolated from the bacterium Streptomyces roseochromogenes DS 12976. A bifunctional enzyme involved in clorobiocin biosynthesis that also catalyses the activity of EC 1.13.12.23, 3-dimethylallyl-4-hydroxybenzoate synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Pojer, F., Kahlich, R., Kammerer, B., Li, S.M. and Heide, L. CloR, a bifunctional non-heme iron oxygenase involved in clorobiocin biosynthesis. J. Biol. Chem. 278 (2003) 30661–30668. [DOI] [PMID: 12777382]
[EC 1.13.11.83 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
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 1.13.12.23     
Accepted name: 4-hydroxy-3-prenylbenzoate synthase
Reaction: 3-dimethylallyl-4-hydroxymandelate + O2 = 3-dimethylallyl-4-hydroxybenzoate + CO2 + H2O
For diagram of 3-dimethylallyl-4-hydroxybenzoate biosynthesis, click here
Other name(s): CloR; novR (gene name)
Systematic name: 3-dimethylallyl-4-hydroxymandelate:oxygen oxidoreductase (3-dimethylallyl-4-hydroxybenzoate forming)
Comments: Isolated from the bacterium Streptomyces roseochromogenes DS 12976. A bifunctional enzyme involved in clorobiocin biosynthesis that also catalyses the activity of EC 1.13.11.83, 3-dimethylallyl-4-hydroxyphenylpyruvate oxygenase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Pojer, F., Kahlich, R., Kammerer, B., Li, S.M. and Heide, L. CloR, a bifunctional non-heme iron oxygenase involved in clorobiocin biosynthesis. J. Biol. Chem. 278 (2003) 30661–30668. [DOI] [PMID: 12777382]
[EC 1.13.12.23 created 2017]
 
 
EC 1.14.2.2      
Transferred entry: now EC 1.13.11.27, 4-hydroxyphenylpyruvate dioxygenase
[EC 1.14.2.2 created 1961 as EC 1.99.1.14, transferred 1965 to EC 1.14.2.2, deleted 1972]
 
 
EC 1.99.1.14      
Transferred entry: Now EC 1.13.11.27, 4-hydroxyphenylpyruvate dioxygenase
[EC 1.99.1.14 created 1961, deleted 1965]
 
 
EC 2.1.1.281     
Accepted name: phenylpyruvate C3-methyltransferase
Reaction: S-adenosyl-L-methionine + 3-phenylpyruvate = S-adenosyl-L-homocysteine + (3S)-2-oxo-3-phenylbutanoate
Glossary: 3-phenylpyruvate = 2-oxo-3-phenylpropanoate
(3S)-2-oxo-3-phenylbutanoate = (3S)-β-methyl-phenylpyruvate
Other name(s): phenylpyruvate Cβ-methyltransferase; phenylpyruvate methyltransferase; mppJ (gene name)
Systematic name: S-adenosyl-L-methionine:2-oxo-3-phenylpropanoate C3-methyltransferase
Comments: The enzyme from the bacterium Streptomyces hygroscopicus NRRL3085 is involved in synthesis of the nonproteinogenic amino acid (2S,3S)-β-methyl-phenylalanine, a building block of the antibiotic mannopeptimycin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Huang, Y.T., Lyu, S.Y., Chuang, P.H., Hsu, N.S., Li, Y.S., Chan, H.C., Huang, C.J., Liu, Y.C., Wu, C.J., Yang, W.B. and Li, T.L. In vitro characterization of enzymes involved in the synthesis of nonproteinogenic residue (2S,3S)-β-methylphenylalanine in glycopeptide antibiotic mannopeptimycin. ChemBioChem 10 (2009) 2480–2487. [DOI] [PMID: 19731276]
[EC 2.1.1.281 created 2013]
 
 
EC 2.3.1.140     
Accepted name: rosmarinate synthase
Reaction: caffeoyl-CoA + (R)-3-(3,4-dihydroxyphenyl)lactate = CoA + rosmarinate
For diagram of rosmarinate biosynthesis, click here
Glossary: (R)-3-(3,4-dihydroxyphenyl)lactate = (2R)-3-(3,4-dihydroxyphenyl)-2-hydroxypropanoate
rosmarinate = (2R)-3-(3,4-dihydroxyphenyl)-2-{[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy}propanoate
Other name(s): rosmarinic acid synthase; caffeoyl-coenzyme A:3,4-dihydroxyphenyllactic acid caffeoyltransferase; 4-coumaroyl-CoA:4-hydroxyphenyllactic acid 4-coumaroyl transferase; RAS (gene name)
Systematic name: caffeoyl-CoA:(R)-3-(3,4-dihydroxyphenyl)lactate 2′-O-caffeoyl-transferase
Comments: Involved, with EC 1.1.1.237 (hydroxyphenylpyruvate reductase) in the biosynthesis of rosmarinic acid. Characterized from the plant Melissa officinalis L. (lemon balm).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 117590-80-4
References:
1.  Petersen, M. and Alfermann, A.W. Two new enzymes of rosmarinic acid biosynthesis from cell cultures of Coleus blumei: hydroxyphenylpyruvate reductase and rosmarinic acid synthase. Z. Naturforsch. C: Biosci. 43 (1988) 501–504.
2.  Petersen, M. S. Characterization of rosmarinic acid synthase from cell cultures of Coleus blumei. Phytochemistry 30 (1991) 2877–2881.
3.  Weitzel, C. and Petersen, M. Cloning and characterisation of rosmarinic acid synthase from Melissa officinalis L. Phytochemistry 72 (2011) 572–578. [DOI] [PMID: 21354582]
[EC 2.3.1.140 created 1992, modified 2013]
 
 
EC 2.5.1.77      
Transferred entry: 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase. Now EC 2.5.1.147, 5-amino-6-(D-ribitylamino)uracil—L-tyrosine 4-methylphenol transferase and EC 4.3.1.32, 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase.
[EC 2.5.1.77 created 2010, deleted 2018]
 
 
EC 2.5.1.111     
Accepted name: 4-hydroxyphenylpyruvate 3-dimethylallyltransferase
Reaction: dimethylallyl diphosphate + 4-hydroxyphenylpyruvate = diphosphate + 3-dimethylallyl-4-hydroxyphenylpyruvate
For diagram of 4-hydroxyphenylpyruvate metabolites, click here
Glossary: 3-dimethylallyl-4-hydroxyphenylpyruvate = 3-[4-hydroxy-3-(3-methylbut-2-en-1-yl)phenyl]-2-oxopropanoate
Other name(s): CloQ; 4HPP dimethylallyltransferase; NovQ
Systematic name: dimethylallyl diphosphate:4-hydroxyphenylpyruvate 3-dimethylallyltransferase
Comments: The enzyme is involved in the biosynthesis of the 3-dimethylallyl-4-hydroxyphenylpyruvate moiety of the aminocoumarin antibiotics clorobiocin and novobiocin [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Pojer, F., Wemakor, E., Kammerer, B., Chen, H., Walsh, C.T., Li, S.M. and Heide, L. CloQ, a prenyltransferase involved in clorobiocin biosynthesis. Proc. Natl. Acad. Sci. USA 100 (2003) 2316–2321. [DOI] [PMID: 12618544]
2.  Keller, S., Pojer, F., Heide, L. and Lawson, D.M. Crystallization and preliminary X-ray analysis of the aromatic prenyltransferase CloQ from the clorobiocin biosynthetic cluster of Streptomyces roseochromogenes. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62 (2006) 1153–1155. [DOI] [PMID: 17077503]
3.  Metzger, U., Keller, S., Stevenson, C.E., Heide, L. and Lawson, D.M. Structure and mechanism of the magnesium-independent aromatic prenyltransferase CloQ from the clorobiocin biosynthetic pathway. J. Mol. Biol. 404 (2010) 611–626. [DOI] [PMID: 20946900]
4.  Ozaki, T., Mishima, S., Nishiyama, M. and Kuzuyama, T. NovQ is a prenyltransferase capable of catalyzing the addition of a dimethylallyl group to both phenylpropanoids and flavonoids. J. Antibiot. (Tokyo) 62 (2009) 385–392. [DOI] [PMID: 19557032]
[EC 2.5.1.111 created 2013]
 
 
EC 2.6.1.5     
Accepted name: tyrosine transaminase
Reaction: L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate
For diagram of reaction, click here, for mechanism, click here , for diagram of phenylalanine and tyrosine biosynthesis, click here and for diagram of the methionine-salvage pathway, click here
Other name(s): tyrosine aminotransferase; glutamic-hydroxyphenylpyruvic transaminase; glutamic phenylpyruvic aminotransferase; L-phenylalanine 2-oxoglutarate aminotransferase; L-tyrosine aminotransferase; phenylalanine aminotransferase; phenylalanine transaminase; phenylalanine-α-ketoglutarate transaminase; phenylpyruvate transaminase; phenylpyruvic acid transaminase; tyrosine-α-ketoglutarate aminotransferase; tyrosine-α-ketoglutarate transaminase; tyrosine-2-ketoglutarate aminotransferase; TyrAT
Systematic name: L-tyrosine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. L-Phenylalanine can act instead of L-tyrosine. The mitochondrial enzyme may be identical with EC 2.6.1.1 (aspartate transaminase). The three isoenzymic forms are interconverted by EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33 (fruit bromelain). The enzyme can also catalyse the final step in the methionine-salvage pathway of Klebsiella pneumoniae [8].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9014-55-5
References:
1.  Canellakis, Z.N. and Cohen, P.P. Purification studies of tyrosine-α-ketoglutaric acid transaminase. J. Biol. Chem. 222 (1956) 53–62. [PMID: 13366978]
2.  Canellakis, Z.N. and Cohen, P.P. Kinetic and substrate specificity study of tyrosine-α-ketoglutaric acid transaminase. J. Biol. Chem. 222 (1956) 63–71. [PMID: 13366979]
3.  Jacoby, G.A. and La Ru, B.N. Studies on the specificity of tyrosine-α-ketoglutarate transaminase. J. Biol. Chem. 239 (1964) 419–424. [PMID: 14171223]
4.  Kenney, F.T. Properties of partially purified tyrosine-α-ketoglutarate transaminase from rat liver. J. Biol. Chem. 234 (1959) 2707–2712. [PMID: 14408534]
5.  Miller, J.E. and Litwack, G. Purification, properties, and identity of liver mitochondrial tyrosine aminotransferase. J. Biol. Chem. 246 (1971) 3234–3240. [PMID: 4396841]
6.  Rowsell, E.V. Transaminations with L-glutamate and α-oxoglutarate in fresh extracts of animal tissues. Biochem. J. 64 (1956) 235–245. [PMID: 13363833]
7.  SentheShanmuganathan, S. The purification and properties of the tyrosine-2-oxoglutarate transaminase of Saccharomyces cerevisiae. Biochem. J. 77 (1960) 619–625. [PMID: 13750129]
8.  Heilbronn, J., Wilson, J. and Berger, B.J. Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae. J. Bacteriol. 181 (1999) 1739–1747. [PMID: 10074065]
[EC 2.6.1.5 created 1961]
 
 
EC 2.6.1.24     
Accepted name: diiodotyrosine transaminase
Reaction: 3,5-diiodo-L-tyrosine + 2-oxoglutarate = 4-hydroxy-3,5-diiodophenylpyruvate + L-glutamate
For diagram of reaction, click here and for reaction mechanism, click here
Other name(s): diiodotyrosine aminotransferase; halogenated tyrosine aminotransferase; halogenated tyrosine transaminase
Systematic name: 3,5-diiodo-L-tyrosine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. Also acts on 3,5-dichloro-, 3,5-dibromo- and 3-iodo-L-tyrosine, thyroxine and triiodothyronine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-18-5
References:
1.  Nakano, M. Purification and properties of halogenated tyrosine and thyroid hormone transaminase from rat kidney mitochondria. J. Biol. Chem. 242 (1967) 73–81. [PMID: 4381052]
2.  Nakano, M. and Danowski, T.S. Thyroid-hormone transaminase and oxidase in rat-kidney mitochondria. Biochim. Biophys. Acta 85 (1964) 18–28. [PMID: 14159298]
[EC 2.6.1.24 created 1972 (EC 2.6.1.25 created 1972, incorporated 1972)]
 
 
EC 2.6.1.28     
Accepted name: tryptophan—phenylpyruvate transaminase
Reaction: L-tryptophan + phenylpyruvate = (indol-3-yl)pyruvate + L-phenylalanine
For diagram of reaction, click here and for mechanism, click here
Other name(s): L-tryptophan-α-ketoisocaproate aminotransferase
Systematic name: L-tryptophan:phenylpyruvate aminotransferase
Comments: Valine, leucine and isoleucine can replace tryptophan as amino donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-87-5
References:
1.  Koide, Y., Honma, M. and Shimomura, T. L-Tryptophan-α-ketoisocaproate aminotransferase from Pseudomonas sp. Agric. Biol. Chem. 44 (1980) 2013–2019.
2.  Sukanya, N.K. and Vaidyanathan, C.S. Aminotransferases of Agrobacterium tumefaciens. Transamination between tryptophan and phenylpyruvate. Biochem. J. 92 (1964) 594–598. [PMID: 5837443]
[EC 2.6.1.28 created 1972]
 
 
EC 2.6.1.49     
Accepted name: dihydroxyphenylalanine transaminase
Reaction: L-dopa + 2-oxoglutarate = 3,4-dihydroxyphenylpyruvate + L-glutamate
For diagram of reaction, click here and for mechanism, click here
Glossary: L-dopa = 3,4-dihydroxy-L-phenylalanine
Other name(s): dopa transaminase; dihydroxyphenylalanine aminotransferase; aspartate-DOPP transaminase (ADT); L-dopa transaminase; dopa aminotransferase; glutamate-DOPP transaminase (GDT); phenylalanine-DOPP transaminase (PDT); DOPA 2-oxoglutarate aminotransferase; DOPAATS
Systematic name: 3,4-dihydroxy-L-phenylalanine:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37277-98-8
References:
1.  Fonnum, F. and Larsen, K. Purification and properties of dihydroxyphenylalanine transaminase from guinea pig brain. J. Neurochem. 12 (1965) 589–598. [DOI] [PMID: 5829872]
2.  Ranjith, N.K., Sasikala, Ch. and Ramana, Ch.V. Catabolism of L-phenylalanine and L-tyrosine by Rhodobacter sphaeroides OU5 occurs through 3,4-dihydroxyphenylalanine. Res. Microbiol. 158 (2007) 506–511. [DOI] [PMID: 17616348]
[EC 2.6.1.49 created 1972]
 
 
EC 2.6.1.58     
Accepted name: phenylalanine(histidine) transaminase
Reaction: L-phenylalanine + pyruvate = phenylpyruvate + L-alanine
For diagram of reaction, click here and for mechanism, click here
Other name(s): phenylalanine (histidine) aminotransferase; phenylalanine(histidine):pyruvate aminotransferase; histidine:pyruvate aminotransferase; L-phenylalanine(L-histidine):pyruvate aminotransferase
Systematic name: L-phenylalanine:pyruvate aminotransferase
Comments: L-Histidine and L-tyrosine can act instead of L-phenylalanine; in the reverse reaction, L-methionine, L-serine and L-glutamine can replace L-alanine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72560-98-6
References:
1.  Minatogawa, Y., Noguchi, T. and Kido, R. Species distribution and properties of hepatic phenylalanine (histidine):pyruvate aminotransferase. Hoppe-Seyler's Z. Physiol. Chem. 358 (1977) 59–67. [PMID: 14070]
[EC 2.6.1.58 created 1978]
 
 
EC 2.6.1.64     
Accepted name: glutamine—phenylpyruvate transaminase
Reaction: L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine
For diagram of reaction, click here and for mechanism, click here
Other name(s): glutamine transaminase K; glutamine-phenylpyruvate aminotransferase
Systematic name: L-glutamine:phenylpyruvate aminotransferase
Comments: A pyridoxal-phosphate protein. L-Methionine, L-histidine and L-tyrosine can act as donors. The enzyme has little activity on pyruvate and glyoxylate (cf. EC 2.6.1.15 glutamine—pyruvate transaminase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 68518-06-9
References:
1.  Cooper, A.J.L. Purification of soluble and mitochondrial glutamine transaminase K from rat kidney. Use of a sensitive assay involving transamination between L-phenylalanine and α-keto-γ-methiolbutyrate. Anal. Biochem. 89 (1978) 451–460. [DOI] [PMID: 727444]
2.  Cooper, A.J.L. and Meister, A. Isolation and properties of a new glutamine transaminase from rat kidney. J. Biol. Chem. 249 (1974) 2554–2561. [PMID: 4822504]
[EC 2.6.1.64 created 1984]
 
 
EC 2.6.1.70     
Accepted name: aspartate—phenylpyruvate transaminase
Reaction: L-aspartate + phenylpyruvate = oxaloacetate + L-phenylalanine
For diagram of reaction, click here and for mechanism, click here
Other name(s): aspartate-phenylpyruvate aminotransferase
Systematic name: L-aspartate:phenylpyruvate aminotransferase
Comments: The enzyme from Pseudomonas putida also acts on 4-hydroxy-phenylpyruvate and, more slowly, on L-glutamate and L-histidine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 99533-45-6
References:
1.  Holger, Z. and Kula, M.-R. Isolation and characterization of a highly inducible L-aspartate-phenylpyruvate transaminase from Pseudomonas putida. J. Biotechnol. 3 (1985) 19–31.
[EC 2.6.1.70 created 1989]
 
 
EC 2.6.1.79     
Accepted name: glutamate—prephenate aminotransferase
Reaction: L-arogenate + 2-oxoglutarate = prephenate + L-glutamate
For diagram of phenylalanine and tyrosine biosynthesis, click here
Other name(s): prephenate transaminase (ambiguous); PAT (ambiguous); L-glutamate:prephenate aminotransferase
Systematic name: L-arogenate:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. Aspartate can also act as the amino donor, but more slowly (cf. EC 2.6.1.78, aspartate—prephenate aminotransferase). The enzyme from higher plants shows a marked preference for prephenate as substrate compared to pyruvate, phenylpyruvate or 4-hydroxyphenylpyruvate [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bonner, C.A. and Jensen, R.A. Novel features of prephenate aminotransferase from cell cultures of Nicotiana silvestris. Arch. Biochem. Biophys. 238 (1985) 237–246. [DOI] [PMID: 3985619]
2.  Siehl, D.L., Connelly, J.A. and Conn, E.E. Tyrosine biosynthesis in Sorghum bicolor: characteristics of prephenate aminotransferase. Z. Naturforsch. 41 (1986) 79–86. [PMID: 2939644]
3.  Bonner, C. and Jensen, R. Prephenate aminotransferase. Methods Enzymol. 142 (1987) 479–487. [PMID: 3298985]
[EC 2.6.1.79 created 2005]
 
 
EC 2.6.1.107     
Accepted name: β-methylphenylalanine transaminase
Reaction: (2S,3S)-3-methylphenylalanine + 2-oxoglutarate = (3S)-2-oxo-3-phenylbutanoate + L-glutamate
Glossary: (3S)-2-oxo-3-phenylbutanoate = (3S)-β-methyl-phenylpyruvate
Other name(s): TyrB
Systematic name: (2S,3S)-3-methylphenylalanine:2-oxoglutarate aminotransferase
Comments: Requires pyridoxal phosphate. Isolated from the bacterium Streptomyces hygroscopicus NRRL3085. It is involved in the biosynthesis of the glycopeptide antibiotic mannopeptimycin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Huang, Y.T., Lyu, S.Y., Chuang, P.H., Hsu, N.S., Li, Y.S., Chan, H.C., Huang, C.J., Liu, Y.C., Wu, C.J., Yang, W.B. and Li, T.L. In vitro characterization of enzymes involved in the synthesis of nonproteinogenic residue (2S,3S)-β-methylphenylalanine in glycopeptide antibiotic mannopeptimycin. ChemBioChem 10 (2009) 2480–2487. [DOI] [PMID: 19731276]
[EC 2.6.1.107 created 2014]
 
 
EC 2.6.1.117     
Accepted name: L-glutamine—4-(methylsulfanyl)-2-oxobutanoate aminotransferase
Reaction: L-glutamine + 4-(methylsulfanyl)-2-oxobutanoate = 2-oxoglutaramate + L-methionine
Other name(s): mtnE (gene name); Solyc11g013170.1 (locus name)
Systematic name: L-glutamine:4-(methylsulfanyl)-2-oxobutanoate aminotransferase
Comments: A pyridoxal-phosphate protein. The enzyme, found in both prokaryotes and eukaryotes, catalyses the last reaction in a methionine salvage pathway. In mammals this activity is catalysed by the multifunctional glutamine transaminase K (cf. EC 2.6.1.64, glutamine—phenylpyruvate transaminase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Berger, B.J., English, S., Chan, G. and Knodel, M.H. Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis. J. Bacteriol. 185 (2003) 2418–2431. [PMID: 12670965]
2.  Ellens, K.W., Richardson, L.G., Frelin, O., Collins, J., Ribeiro, C.L., Hsieh, Y.F., Mullen, R.T. and Hanson, A.D. Evidence that glutamine transaminase and ω-amidase potentially act in tandem to close the methionine salvage cycle in bacteria and plants. Phytochemistry 113 (2015) 160–169. [PMID: 24837359]
[EC 2.6.1.117 created 2019]
 
 
EC 4.1.1.43     
Accepted name: phenylpyruvate decarboxylase
Reaction: phenylpyruvate = phenylacetaldehyde + CO2
Glossary: phenylpyruvate = 3-phenyl-2-oxopropanoate
Other name(s): phenylpyruvate carboxy-lyase; phenylpyruvate carboxy-lyase (phenylacetaldehyde-forming)
Systematic name: 3-phenyl-2-oxopropanoate carboxy-lyase (phenylacetaldehyde-forming)
Comments: The enzyme from the bacterium Azospirillum brasilense also acts on some other substrates, including (indol-3-yl)pyruvate, with much lower efficiency. However, it only possesses classical Michaelis-Menten kinetics with phenylpyruvate. Aliphatic 2-oxo acids longer that 2-oxohexanoate are not substrates. cf. EC 4.1.1.74, indolepyruvate decarboxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-45-5
References:
1.  Asakawa, T., Wada, H. and Yamano, T. Enzymatic conversion of phenylpyruvate to phenylacetate. Biochim. Biophys. Acta 170 (1968) 375–391. [DOI] [PMID: 4303395]
2.  Spaepen, S., Versees, W., Gocke, D., Pohl, M., Steyaert, J. and Vanderleyden, J. Characterization of phenylpyruvate decarboxylase, involved in auxin production of Azospirillum brasilense. J. Bacteriol. 189 (2007) 7626–7633. [PMID: 17766418]
[EC 4.1.1.43 created 1972]
 
 
EC 4.1.1.80     
Accepted name: 4-hydroxyphenylpyruvate decarboxylase
Reaction: 4-hydroxyphenylpyruvate = 4-hydroxyphenylacetaldehyde + CO2
For diagram of dopa biosynthesis, click here
Other name(s): 4-hydroxyphenylpyruvate carboxy-lyase
Systematic name: 4-hydroxyphenylpyruvate carboxy-lyase (4-hydroxyphenylacetaldehyde-forming)
Comments: Reacts with dopamine to give the benzylisoquinoline alkaloid skeleton.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 109300-96-1
References:
1.  Rueffer, M. and Zenk, M.H. Distant precursors of benzylisoquinoline alkaloids and their enzymatic formation. Z. Naturforsch. C: Biosci. 42 (1987) 319–332.
[EC 4.1.1.80 created 2002]
 
 
EC 4.1.1.84     
Accepted 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; D-dopachrome carboxy-lyase
Systematic name: D-dopachrome carboxy-lyase (5,6-dihydroxyindole-forming)
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: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry 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. [DOI] [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. [DOI] [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. [DOI] [PMID: 9480844]
[EC 4.1.1.84 created 2005]
 
 
EC 4.2.1.51     
Accepted name: prephenate dehydratase
Reaction: prephenate = phenylpyruvate + H2O + CO2
For diagram of phenylalanine and tyrosine biosynthesis, click here
Other name(s): prephenate hydro-lyase (decarboxylating)
Systematic name: prephenate hydro-lyase (decarboxylating; phenylpyruvate-forming)
Comments: This enzyme in the enteric bacteria also possesses chorismate mutase (EC 5.4.99.5) activity, and converts chorismate into prephenate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9044-88-6
References:
1.  Cerutti, P. and Guroff, G. Enzymatic formation of phenylpyruvic acid in Pseudomonas sp. (ATCC 11299A) and its regulation. J. Biol. Chem. 240 (1965) 3034–3048. [PMID: 14342329]
2.  Cotton, R.G.H. and Gibson, F. The biosynthesis of phenylalanine and tyrosine; enzymes converting chorismic acid into prephenic acid and their relationships to prephenate dehydratase and prephenate dehydrogenase. Biochim. Biophys. Acta 100 (1965) 76–88. [DOI] [PMID: 14323651]
3.  Schmidt, J.C. and Zalkin, H. Chorismate mutase-prephenate dehydratase. Partial purification and properties of the enzyme from Salmonella typhimurium. Biochemistry 8 (1969) 174–181. [PMID: 4887851]
[EC 4.2.1.51 created 1972]
 
 
EC 5.3.2.1     
Accepted name: phenylpyruvate tautomerase
Reaction: keto-phenylpyruvate = enol-phenylpyruvate
Other name(s): phenylpyruvic keto-enol isomerase
Systematic name: phenylpyruvate ketoenol-isomerase
Comments: Also acts on other arylpyruvates.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9023-54-5
References:
1.  Blasi, F., Fragonmele, F. and Covelli, I. Thyroidal phenylpyruvate tautomerase. Isolation and characterization. J. Biol. Chem. 244 (1969) 4864–4870. [PMID: 5824560]
2.  Knox, W.E. p-Hydroxyphenylpyruvate enol-keto tautomerase. Methods Enzymol. 2 (1955) 289–295.
3.  Knox, W.E. and Pitt, B.M. Enzymic catalysis of the keto-enol tautomerization of phenylpyruvic acids. J. Biol. Chem. 225 (1957) 675–688. [PMID: 13416270]
[EC 5.3.2.1 created 1961]
 
 
EC 5.4.99.5     
Accepted name: chorismate mutase
Reaction: chorismate = prephenate
For diagram of phenylalanine and tyrosine biosynthesis, click here and for mechanism of reaction, click here
Other name(s): hydroxyphenylpyruvate synthase
Systematic name: chorismate pyruvatemutase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9068-30-8
References:
1.  Cotton, R.G.H. and Gibson, F. The biosynthesis of phenylalanine and tyrosine; enzymes converting chorismic acid into prephenic acid and their relationships to prephenate dehydratase and prephenate dehydrogenase. Biochim. Biophys. Acta 100 (1965) 76–88. [DOI] [PMID: 14323651]
2.  Lorence, J.H. and Nester, E.W. Multiple molecular forms of chorismate mutase in Bacillus subtillis. Biochemistry 6 (1967) 1541–1543. [PMID: 4962500]
3.  Sprössler, B. and Lingens, F. Chorismat-Mutase aus Claviceps. I. Eigenschaften der Chorismat-Mutase aus verschiedenen Claviceps-Stämmen. Hoppe-Seyler's Z. Physiol. Chem. 351 (1970) 448–458. [PMID: 5443801]
4.  Woodin, T.S. and Nishioka, L. Evidence for three isozymes of chorismate mutase in alfalfa. Biochim. Biophys. Acta 309 (1973) 211–223. [DOI] [PMID: 4708674]
[EC 5.4.99.5 created 1972]
 
 


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