EC |
1.1.3.19 |
Accepted name: |
4-hydroxymandelate oxidase (decarboxylating) |
Reaction: |
(S)-4-hydroxymandelate + O2 = 4-hydroxybenzaldehyde + CO2 + H2O2 |
Glossary: |
(S)-4-hydroxymandelate = (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate |
Other name(s): |
L-4-hydroxymandelate oxidase (decarboxylating); (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate:oxygen 1-oxidoreductase; (S)-4-hydroxymandelate:oxygen 1-oxidoreductase; 4-hydroxymandelate oxidase |
Systematic name: |
(S)-4-hydroxymandelate:oxygen 1-oxidoreductase (decarboxylating) |
Comments: |
A flavoprotein (FAD), requires Mn2+. The enzyme from the bacterium Pseudomonas putida is involved in the degradation of mandelate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 60976-30-9 |
References: |
1. |
Bhat, S.G. and Vaidyanathan, C.S. Purification and properties of L-4-hydroxymandelate oxidase from Pseudomonas convexa. Eur. J. Biochem. 68 (1976) 323–331. [DOI] [PMID: 976259] |
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[EC 1.1.3.19 created 1984, modified 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 |
1.13.11.46 |
Accepted name: |
4-hydroxymandelate synthase |
Reaction: |
4-hydroxyphenylpyruvate + O2 = (S)-4-hydroxymandelate + CO2 |
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For diagram of 4-hydroxyphenylpyruvate metabolites, click here |
Glossary: |
(S)-4-hydroxymandelate = (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate
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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, PDB, 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. |
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[EC 1.13.11.46 created 2001] |
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EC |
1.14.16.6 |
Accepted name: |
mandelate 4-monooxygenase |
Reaction: |
(S)-2-hydroxy-2-phenylacetate + a 5,6,7,8-tetrahydropteridine + O2 = (S)-4-hydroxymandelate + a 4a-hydroxy-5,6,7,8-tetrahydropteridine |
Glossary: |
(S)-4-hydroxymandelate = (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate |
Other name(s): |
L-mandelate 4-hydroxylase; mandelic acid 4-hydroxylase |
Systematic name: |
(S)-2-hydroxy-2-phenylacetate,tetrahydropteridine:oxygen oxidoreductase (4-hydroxylating) |
Comments: |
Requires Fe2+. The enzyme has been characterized from the bacterium Pseudomonas putida. The 4a-hydroxytetrahydropteridine formed can dehydrate to 6,7-dihydropteridine, both spontaneously and by the action of EC 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase. The 6,7-dihydropteridine must be enzymically reduced back to tetrahydropteridine, by EC 1.5.1.34, 6,7-dihydropteridine reductase, before it slowly rearranges into the more stable but inactive compound 7,8-dihydropteridine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 39459-82-0 |
References: |
1. |
Bhat, S.G. and Vaidyanathan, C.S. Purifications and properties of L-mandelate-4-hydroxylase from Pseudomonas convexa. Arch. Biochem. Biophys. 176 (1976) 314–323. [DOI] [PMID: 9909] |
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[EC 1.14.16.6 created 1984, modified 2020] |
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