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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