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 |
1.13.11.80 |
Accepted name: |
(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase |
Reaction: |
(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA |
Glossary: |
(3,5-dihydroxyphenyl)acetyl-CoA = 2-(3,5-dihydroxyphenyl)acetyl-CoA |
Other name(s): |
DpgC |
Systematic name: |
(3,5-dihydroxyphenyl)acetyl-CoA:oxygen oxidoreductase |
Comments: |
The enzyme, characterized from bacteria Streptomyces toyocaensis and Amycolatopsis orientalis, is involved in the biosynthesis of (3,5-dihydroxyphenyl)glycine, a component of the glycopeptide antibiotic vancomycin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Chen, H., Tseng, C.C., Hubbard, B.K. and Walsh, C.T. Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine. Proc. Natl. Acad. Sci. USA 98 (2001) 14901–14906. [DOI] [PMID: 11752437] |
2. |
Widboom, P.F., Fielding, E.N., Liu, Y. and Bruner, S.D. Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis. Nature 447 (2007) 342–345. [DOI] [PMID: 17507985] |
3. |
Fielding, E.N., Widboom, P.F. and Bruner, S.D. Substrate recognition and catalysis by the cofactor-independent dioxygenase DpgC. Biochemistry 46 (2007) 13994–14000. [DOI] [PMID: 18004875] |
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[EC 1.13.11.80 created 2015] |
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EC |
2.3.1.246 |
Accepted name: |
3,5-dihydroxyphenylacetyl-CoA synthase |
Reaction: |
4 malonyl-CoA = (3,5-dihydroxyphenylacetyl)-CoA + 3 CoA + 4 CO2 + H2O |
Other name(s): |
DpgA |
Systematic name: |
malonyl-CoA:malonyl-CoA malonyltransferase (3,5-dihydroxyphenylacetyl-CoA-forming) |
Comments: |
The enzyme, characterized from the bacterium Amycolatopsis mediterranei, is involved in biosynthesis of the nonproteinogenic amino acid (S)-3,5-dihydroxyphenylglycine, a component of the vancomycin-type antibiotic balhimycin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Pfeifer, V., Nicholson, G.J., Ries, J., Recktenwald, J., Schefer, A.B., Shawky, R.M., Schroder, J., Wohlleben, W. and Pelzer, S. A polyketide synthase in glycopeptide biosynthesis: the biosynthesis of the non-proteinogenic amino acid (S)-3,5-dihydroxyphenylglycine. J. Biol. Chem. 276 (2001) 38370–38377. [DOI] [PMID: 11495926] |
2. |
Chen, H., Tseng, C.C., Hubbard, B.K. and Walsh, C.T. Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine. Proc. Natl. Acad. Sci. USA 98 (2001) 14901–14906. [DOI] [PMID: 11752437] |
3. |
Tseng, C.C., McLoughlin, S.M., Kelleher, N.L. and Walsh, C.T. Role of the active site cysteine of DpgA, a bacterial type III polyketide synthase. Biochemistry 43 (2004) 970–980. [DOI] [PMID: 14744141] |
4. |
Wu, H.C., Li, Y.S., Liu, Y.C., Lyu, S.Y., Wu, C.J. and Li, T.L. Chain elongation and cyclization in type III PKS DpgA. ChemBioChem 13 (2012) 862–871. [DOI] [PMID: 22492619] |
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[EC 2.3.1.246 created 2015] |
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EC |
2.6.1.103 |
Accepted name: |
(S)-3,5-dihydroxyphenylglycine transaminase |
Reaction: |
(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + L-glutamate
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Glossary: |
(S)-3,5-dihydroxyphenylglycine = (2S)-2-amino-2-(3,5-dihydroxyphenyl)acetic acid
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Other name(s): |
HpgT |
Systematic name: |
(S)-3,5-dihydroxyphenylglycine:2-oxoglutarate aminotransferase |
Comments: |
A pyridoxal-5′-phosphate protein. The enzyme from the bacterium Amycolatopsis orientalis catalyses the reaction in the reverse direction as part of the biosynthesis of the (S)-3,5-dihydroxyphenylglycine constituent of the glycopeptide antibiotic chloroeremomycin. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Sandercock, A.M., Charles, E.H., Scaife, W., Kirkpatrick, P.N., O'Brien, S.W., Papageorgiou, E.A., Spencer, J.B. and Williams, D.H. Biosynthesis of the di-meta-hydroxyphenylglycine constituent of the vancomycin-group antibiotic chloroeremomycin. Chem. Comm. (2001) 1252–1253. |
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[EC 2.6.1.103 created 2013] |
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