EC |
1.1.1.379 |
Accepted name: |
(R)-mandelate dehydrogenase |
Reaction: |
(R)-mandelate + NAD+ = phenylglyoxylate + NADH + H+ |
Glossary: |
(R)-mandelate = D-mandelate |
Other name(s): |
ManDH2; D-ManDH2; D-mandelate dehydrogenase (ambiguous) |
Systematic name: |
(R)-mandelate:NAD+ 2-oxidoreductase |
Comments: |
The enzyme, found in bacteria and fungi, can also accept a number of substituted mandelate derivatives, such as 3-hydroxymandelate, 4-hydroxymandelate, 2-methoxymandelate, 4-hydroxy-3-methoxymandelate and 3-hydroxy-4-methoxymandelate. The enzyme has no activity with (S)-mandelate (cf. EC 1.1.99.31, (S)-mandelate dehydrogenase) [1,2]. The enzyme transfers the pro-R-hydrogen from NADH [2]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Baker, D.P. and Fewson, C.A. Purification and characterization of D(–)-mandelate dehydrogenase from Rhodotorula graminis. Microbiology 135 (1989) 2035–2044. |
2. |
Baker, D.P., Kleanthous, C., Keen, J.N., Weinhold, E. and Fewson, C.A. Mechanistic and active-site studies on D(–)-mandelate dehydrogenase from Rhodotorula graminis. Biochem. J. 281 (1992) 211–218. [PMID: 1731758] |
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[EC 1.1.1.379 created 2014] |
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EC |
1.1.3.46 |
Accepted name: |
4-hydroxymandelate oxidase |
Reaction: |
(S)-4-hydroxymandelate + O2 = 2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
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Glossary: |
(S)-4-hydroxymandelate = (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate
2-(4-hydroxyphenyl)-2-oxoacetate = 4-hydroxyphenylglyoxylate = (4-hydroxyphenyl)(oxo)acetate
L-(4-hydroxyphenyl)glycine = (S)-4-hydroxyphenylglycine
L-(3,5-dihydroxyphenyl)glycine = (S)-3,5-dihydroxyphenylglycine
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Other name(s): |
4HmO; HmO |
Systematic name: |
(S)-4-hydroxymandelate:oxygen 1-oxidoreductase |
Comments: |
A flavoprotein (FMN). The enzyme from the bacterium Amycolatopsis orientalis is involved in the biosynthesis of L-(4-hydroxyphenyl)glycine and L-(3,5-dihydroxyphenyl)glycine, two non-proteinogenic amino acids occurring in the vancomycin group of antibiotics. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
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. |
Li, T.L., Choroba, O.W., Charles, E.H., Sandercock, A.M., Williams, D.H. and Spencer, J.B. Characterisation of a hydroxymandelate oxidase involved in the biosynthesis of two unusual amino acids occurring in the vancomycin group of antibiotics. Chem. Commun. (Camb.) (2001) 1752–1753. [PMID: 12240298] |
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[EC 1.1.3.46 created 2014] |
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EC |
1.1.99.31 |
Accepted name: |
(S)-mandelate dehydrogenase |
Reaction: |
(S)-mandelate + acceptor = phenylglyoxylate + reduced acceptor |
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For diagram of reaction, click here |
Glossary: |
(S)-mandelate = (S)-2-hydroxy-2-phenylacetate
phenylglyoxylate = benzoylformate = 2-oxo-2-phenylacetate
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Other name(s): |
MDH (ambiguous) |
Systematic name: |
(S)-mandelate:acceptor 2-oxidoreductase |
Comments: |
This enzyme is a member of the FMN-dependent α-hydroxy-acid oxidase/dehydrogenase family [1]. While all enzymes of this family oxidize the (S)-enantiomer of an α-hydroxy acid to an α-oxo acid, the ultimate oxidant (oxygen, intramolecular heme or some other acceptor) depends on the particular enzyme. This enzyme transfers the electron pair from FMNH2 to a component of the electron transport chain, most probably ubiquinone [1,2]. It is part of a metabolic pathway in Pseudomonads that allows these organisms to utilize mandelic acid, derivatized from the common soil metabolite amygdalin, as the sole source of carbon and energy [2]. The enzyme has a large active-site pocket and preferentially binds substrates with longer sidechains, e.g. 2-hydroxyoctanoate rather than 2-hydroxybutyrate [1]. It also prefers substrates that, like (S)-mandelate, have β unsaturation, e.g. (indol-3-yl)glycolate compared with (indol-3-yl)lactate [1]. Esters of mandelate, such as methyl (S)-mandelate, are also substrates [3]. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9067-95-2 |
References: |
1. |
Lehoux, I.E. and Mitra, B. (S)-Mandelate dehydrogenase from Pseudomonas putida: mechanistic studies with alternate substrates and pH and kinetic isotope effects. Biochemistry 38 (1999) 5836–5848. [DOI] [PMID: 10231535] |
2. |
Dewanti, A.R., Xu, Y. and Mitra, B. Role of glycine 81 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate specificity and oxidase activity. Biochemistry 43 (2004) 10692–10700. [DOI] [PMID: 15311930] |
3. |
Dewanti, A.R., Xu, Y. and Mitra, B. Esters of mandelic acid as substrates for (S)-mandelate dehydrogenase from Pseudomonas putida: implications for the reaction mechanism. Biochemistry 43 (2004) 1883–1890. [DOI] [PMID: 14967029] |
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[EC 1.1.99.31 created 2006] |
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EC |
1.2.1.58 |
Accepted name: |
phenylglyoxylate dehydrogenase (acylating) |
Reaction: |
phenylglyoxylate + NAD+ + CoA = benzoyl-S-CoA + CO2 + NADH |
Systematic name: |
phenylglyoxylate:NAD+ oxidoreductase |
Comments: |
Requires thiamine diphosphate as cofactor. The enzyme from the denitrifying bacterium Azoarcus evansii is specific for phenylglyoxylate. 2-Oxoisovalerate is oxidized at 15% of the rate for phenylglyoxylate. Also reduces viologen dyes. Contains iron-sulfur centres and FAD. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 205510-78-7 |
References: |
1. |
Hirsch, W., Schägger, H. and Fuchs, G. Phenylglyoxylate:NAD+ oxidoreductase (CoA benzoylating), a new enzyme of anaerobic phenylalanine metabolism in the denitrifying bacterium Axoarcus evansii. Eur. J. Biochem. 251 (1998) 907–915. [DOI] [PMID: 9490067] |
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[EC 1.2.1.58 created 1999] |
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EC |
1.17.5.1 |
Accepted name: |
phenylacetyl-CoA dehydrogenase |
Reaction: |
phenylacetyl-CoA + H2O + 2 quinone = phenylglyoxylyl-CoA + 2 quinol |
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For diagram of phenylacetyl-CoA metabolism, click here |
Other name(s): |
phenylacetyl-CoA:acceptor oxidoreductase |
Systematic name: |
phenylacetyl-CoA:quinone oxidoreductase |
Comments: |
The enzyme from Thauera aromatica is a membrane-bound molybdenum—iron—sulfur protein. The enzyme is specific for phenylacetyl-CoA as substrate. Phenylacetate, acetyl-CoA, benzoyl-CoA, propanoyl-CoA, crotonyl-CoA, succinyl-CoA and 3-hydroxybenzoyl-CoA cannot act as substrates. The oxygen atom introduced into the product, phenylglyoxylyl-CoA, is derived from water and not molecular oxygen. Duroquinone, menaquinone and 2,6-dichlorophenolindophenol (DCPIP) can act as acceptor, but the likely physiological acceptor is ubiquinone [1]. A second enzyme, EC 3.1.2.25, phenylacetyl-CoA hydrolase, converts the phenylglyoxylyl-CoA formed into phenylglyoxylate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 210756-43-7 |
References: |
1. |
Rhee, S.K. and Fuchs, G. Phenylacetyl-CoA:acceptor oxidoreductase, a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Eur. J. Biochem. 262 (1999) 507–515. [DOI] [PMID: 10336636] |
2. |
Schneider, S. and Fuchs, G. Phenylacetyl-CoA:acceptor oxidoreductase, a new α-oxidizing enzyme that produces phenylglyoxylate. Assay, membrane localization, and differential production in Thauera aromatica. Arch. Microbiol. 169 (1998) 509–516. [PMID: 9575237] |
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[EC 1.17.5.1 created 2004] |
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EC |
2.6.1.72 |
Accepted name: |
D-4-hydroxyphenylglycine transaminase |
Reaction: |
D-4-hydroxyphenylglycine + 2-oxoglutarate = 4-hydroxyphenylglyoxylate + L-glutamate |
Other name(s): |
D-hydroxyphenylglycine aminotransferase |
Systematic name: |
D-4-hydroxyphenylglycine:2-oxoglutarate aminotransferase |
Comments: |
A pyridoxal-phosphate protein. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 117444-05-0 |
References: |
1. |
Van den Tweel, W.J.J., Ogg, R.L.H.P. and de Bont, J.A.M. Transamination with a D-transaminase from Pseudomonas putida and conversion of p-hydroxyphenylglyoxylate to D-p-hydroxyphenylglycine. Patent EP0315786, Neth. Appl. NL (1987), 87, 02449. |
2. |
Van den Tweel, W.J.J., Smits, J.P., Ogg, R.L.H.P. and de Bont, J.A.M. The involvement of an enantioselective transaminase in the metabolism of D-3- and D-4-hydroxyphenylglycine in Pseudomonas putida. Appl. Microbiol. Biotechnol. 29 (1998) 224–230. |
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[EC 2.6.1.72 created 1990] |
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EC |
3.1.2.25 |
Accepted name: |
phenylacetyl-CoA hydrolase |
Reaction: |
phenylglyoxylyl-CoA + H2O = phenylglyoxylate + CoA |
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For diagram of phenylacetyl-CoA metabolism, click here |
Systematic name: |
phenylglyoxylyl-CoA hydrolase |
Comments: |
This is the second step in the conversion of phenylacetyl-CoA to phenylglyoxylate, the first step being carried out by EC 1.17.5.1, phenylacetyl-CoA dehydrogenase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 57219-72-4 |
References: |
1. |
Rhee, S.K. and Fuchs, G. Phenylacetyl-CoA:acceptor oxidoreductase, a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Eur. J. Biochem. 262 (1999) 507–515. [DOI] [PMID: 10336636] |
2. |
Schneider, S. and Fuchs, G. Phenylacetyl-CoA:acceptor oxidoreductase, a new α-oxidizing enzyme that produces phenylglyoxylate. Assay, membrane localization, and differential production in Thauera aromatica. Arch. Microbiol. 169 (1998) 509–516. [PMID: 9575237] |
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[EC 3.1.2.25 created 2004] |
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EC |
4.1.1.7 |
Accepted name: |
benzoylformate decarboxylase |
Reaction: |
phenylglyoxylate = benzaldehyde + CO2 |
Glossary: |
thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium
phenylglyoxylate = benzoylformate = 2-oxo-2-phenylacetate
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Other name(s): |
phenylglyoxylate decarboxylase; benzoylformate carboxy-lyase; benzoylformate carboxy-lyase (benzaldehyde-forming) |
Systematic name: |
phenylglyoxylate carboxy-lyase (benzaldehyde-forming) |
Comments: |
A thiamine-diphosphate protein. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-00-7 |
References: |
1. |
Gunsalus, C.F., Stanier, R.Y. and Gunsalus, I.C. The enzymatic conversion of mandelic acid to benzoic acid. III. Fractionation and properties of the soluble enzymes. J. Bacteriol. 66 (1953) 548–553. [PMID: 13108854] |
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[EC 4.1.1.7 created 1961] |
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