The Enzyme Database

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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 1.2.7.8     
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 1.3.3.10     
Accepted name: tryptophan α,β-oxidase
Reaction: L-tryptophan + O2 = α,β-didehydrotryptophan + H2O2
Other name(s): L-tryptophan 2′,3′-oxidase; L-tryptophan α,β-dehydrogenase
Systematic name: L-tryptophan:oxygen α,β-oxidoreductase
Comments: Requires heme. The enzyme from Chromobacterium violaceum is specific for tryptophan derivatives possessing its carboxyl group free or as an amide or ester, and an unsubstituted indole ring. Also catalyses the α,β dehydrogenation of L-tryptophan side chains in peptides. The product of the reaction can hydrolyse spontaneously to form (indol-3-yl)pyruvate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 156859-19-7
References:
1.  Genet, R., Denoyelle, C. and Menez, A. Purification and partial characterization of an amino acid α,β-dehydrogenase, L-tryptophan 2′,3′-oxidase from Chromobacterium violaceum. J. Biol. Chem. 269 (1994) 18177–18184. [PMID: 8027079]
2.  Genet, R., Benetti, P.H., Hammadi, A. and Menez, A. L-Tryptophan 2′,3′-oxidase from Chromobacterium violaceum. Substrate specificity and mechanistic implications. J. Biol. Chem. 270 (1995) 23540–23545. [DOI] [PMID: 7559518]
[EC 1.3.3.10 created 2000 as EC 1.4.3.17, transferred 2003 to EC 1.3.3.10]
 
 
EC 1.4.1.19     
Accepted name: tryptophan dehydrogenase
Reaction: L-tryptophan + NAD(P)+ + H2O = (indol-3-yl)pyruvate + NH3 + NAD(P)H + H+
Other name(s): NAD(P)+-L-tryptophan dehydrogenase; L-tryptophan dehydrogenase; L-Trp-dehydrogenase; TDH
Systematic name: L-tryptophan:NAD(P)+ oxidoreductase (deaminating)
Comments: Activated by Ca2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 94047-13-9
References:
1.  Vackova, K., Mehta, A. and Kutacek, M. Tryptophan aminotransferase and tryptophan dehydrogenase - activities in some cell compartments of spinach leaves - the effect of calcium-ions on tryptophan dehydrogenase. Biol. Plant. 27 (1985) 154–158.
[EC 1.4.1.19 created 1989]
 
 
EC 1.14.13.168     
Accepted name: indole-3-pyruvate monooxygenase
Reaction: (indol-3-yl)pyruvate + NADPH + H+ + O2 = (indol-3-yl)acetate + NADP+ + H2O + CO2
For diagram of indoleacetic acid biosynthesis, click here
Glossary: (indol-3-yl)pyruvate = 3-(1H-indol-3-yl)-2-oxopropanoate, (indol-3-yl)acetate = 2-(1H-indol-3-yl)acetate = indole-3-acetate
Other name(s): YUC2 (gene name); spi1 (gene name)
Systematic name: indole-3-pyruvate,NADPH:oxygen oxidoreductase (1-hydroxylating, decarboxylating)
Comments: This plant enzyme, along with EC 2.6.1.99 L-tryptophan—pyruvate aminotransferase, is responsible for the biosynthesis of the plant hormone indole-3-acetate from L-tryptophan.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Mashiguchi, K., Tanaka, K., Sakai, T., Sugawara, S., Kawaide, H., Natsume, M., Hanada, A., Yaeno, T., Shirasu, K., Yao, H., McSteen, P., Zhao, Y., Hayashi, K., Kamiya, Y. and Kasahara, H. The main auxin biosynthesis pathway in Arabidopsis. Proc. Natl. Acad. Sci. USA 108 (2011) 18512–18517. [DOI] [PMID: 22025724]
2.  Zhao, Y. Auxin biosynthesis: a simple two-step pathway converts tryptophan to indole-3-acetic acid in plants. Mol. Plant 5 (2012) 334–338. [DOI] [PMID: 22155950]
[EC 1.14.13.168 created 2012]
 
 
EC 2.1.1.47     
Accepted name: indolepyruvate C-methyltransferase
Reaction: S-adenosyl-L-methionine + (indol-3-yl)pyruvate = S-adenosyl-L-homocysteine + (R)-3-(indol-3-yl)-2-oxobutanoate
Other name(s): ind1 (gene name); indolepyruvate methyltransferase; indolepyruvate 3-methyltransferase; indolepyruvic acid methyltransferase; S-adenosyl-L-methionine:indolepyruvate C-methyltransferase
Systematic name: S-adenosyl-L-methionine:(indol-3-yl)pyruvate C3-methyltransferase
Comments: The enzyme, characterized from the bacterium Streptomyces griseus, is involved in the biosynthesis of the antibacterial drug indolmycin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 54576-88-4
References:
1.  Hornemann, U., Speedie, M.K., Hurley, L.H. and Floss, H.G. Demonstration of a C-methylating enzyme in cell free extracts of indolmycin-producing Streptomyces griseus. Biochem. Biophys. Res. Commun. 39 (1970) 594–599. [DOI] [PMID: 5490210]
2.  Hornemann, U., Hurley, L.H., Speedie, M.K. and Floss, H.G. The biosynthesis of indolmycin. J. Am. Chem. Soc. 93 (1971) 3028–3035. [PMID: 5095271]
3.  Speedie, M.K., Hornemann, U. and Floss, H.G. Isolation and characterization of tryptophan transaminase and indolepyruvate C-methyltransferase. Enzymes involved in indolmycin biosynthesis in Streptomyces griseus. J. Biol. Chem. 250 (1975) 7819–7825. [PMID: 809439]
4.  Du, Y.L., Alkhalaf, L.M. and Ryan, K.S. In vitro reconstitution of indolmycin biosynthesis reveals the molecular basis of oxazolinone assembly. Proc. Natl. Acad. Sci. USA 112 (2015) 2717–2722. [DOI] [PMID: 25730866]
[EC 2.1.1.47 created 1976, modified 2016]
 
 
EC 2.6.1.27     
Accepted name: tryptophan transaminase
Reaction: L-tryptophan + 2-oxoglutarate = (indol-3-yl)pyruvate + L-glutamate
For diagram of reaction, click here and for mechanism, click here
Other name(s): L-phenylalanine-2-oxoglutarate aminotransferase; tryptophan aminotransferase; 5-hydroxytryptophan-ketoglutaric transaminase; hydroxytryptophan aminotransferase; L-tryptophan aminotransferase; L-tryptophan transaminase
Systematic name: L-tryptophan:2-oxoglutarate aminotransferase
Comments: A pyridoxal-phosphate protein. Also acts on 5-hydroxytryptophan and, to a lesser extent, on the phenyl amino acids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9022-98-4
References:
1.  George, H. and Gabay, S. Brain aromatic aminotransferase. I. Purification and some properties of pig brain L-phenylalanine-2-oxoglutarate aminotransferase. Biochim. Biophys. Acta 167 (1968) 555–566. [DOI] [PMID: 5722279]
2.  O'Neil, S.R. and DeMoss, R.D. Tryptophan transaminase from Clostridium sporogenes. Arch. Biochem. Biophys. 127 (1968) 361–368. [DOI] [PMID: 5697992]
3.  Tangen, O., Fonnum, F. and Haavaldsen, R. Separation and purification of aromatic amino acid transaminases from rat brain. Biochim. Biophys. Acta 96 (1965) 82–90. [DOI] [PMID: 14285270]
[EC 2.6.1.27 created 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 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 4.1.1.74     
Accepted name: indolepyruvate decarboxylase
Reaction: 3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO2
Glossary: thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium
Other name(s): indol-3-yl-pyruvate carboxy-lyase; 3-(indol-3-yl)pyruvate carboxy-lyase
Systematic name: 3-(indol-3-yl)pyruvate carboxy-lyase [(2-indol-3-yl)acetaldehyde-forming]
Comments: Thiamine diphosphate- and Mg2+-dependent. More specific than EC 4.1.1.1 pyruvate decarboxylase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9074-92-4
References:
1.  Koga, J. Structure and function of indolepyruvate decarboxylase, a key enzyme in indole-3-pyruvic acid biosynthesis. Biochim. Biophys. Acta 1249 (1995) 1–13. [DOI] [PMID: 7766676]
[EC 4.1.1.74 created 1999]
 
 


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