The Enzyme Database

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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]
[EC 1.1.3.19 created 1984, modified 2014]
 
 
EC 1.1.3.46     
Accepted name: 4-hydroxymandelate oxidase
Reaction: (S)-4-hydroxymandelate + O2 = 2-(4-hydroxyphenyl)-2-oxoacetate + H2O2
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
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
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]
[EC 1.1.3.46 created 2014]
 
 
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 1.14.16.6     
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]
[EC 1.14.16.6 created 1984, modified 2020]
 
 


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