(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase
| 3,5-dihydroxyphenylacetyl-CoA 1,2-dioxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 3,5-dihydroxyphenylacetyl-CoA 1,2-dioxygenase hexamer, Streptomyces toyocaensis | |||||||||
| Identifiers | |||||||||
| EC number | 1.13.11.80 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase (EC 1.13.11.80, DpgC is an enzyme [1] catalyses the following chemical reaction
- (3,5-dihydroxyphenyl)acetyl-CoA + O2 ⇌ 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA.
This enzyme is involved in the biosynthesis of the nonproteinogenic amino acid (S)-3,5-dihydroxyphenylglycine (Dpg) responsible of the production of vancomycin and teicoplanin antibiotics. It catalyzes the unusual conversion 3,5-dihydroxyphenylacetyl-CoA (DPA-CoA) to 3,5-dihydroxyphenylglyoxylate.
References
- ↑ Fielding, E.N.; Widboom, P.F.; Bruner, S.D. (2007). "Substrate recognition and catalysis by the cofactor-independent dioxygenase DpgC". Biochemistry. 46 (49): 13994–14000. doi:10.1021/bi701148b. PMID 18004875.
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