Structural highlights
Function
DPGC_STRTO Involved in the biosynthesis of the nonproteinogenic amino acid monomer (S)-3,5-dihydroxyphenylglycine (Dpg) responsible of the production of vancomycin and teicoplanin antibiotics. Catalyzes the unusual conversion 3,5-dihydroxyphenylacetyl-CoA (DPA-CoA) to 3,5-dihydroxyphenylglyoxylate. DpgC performed a net four-electron oxidation of the benzylic carbon of DPA-CoA and the hydrolysis of the thioester bond to generate free CoA (PubMed:18004875, PubMed:17507985). DpgC has the ability to process a diverse range of substituted phenylacetyl-CoA substrates (PubMed:18004875).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
See Also
References
- ↑ Widboom PF, Fielding EN, Liu Y, Bruner SD. Structural basis for cofactor-independent dioxygenation in vancomycin biosynthesis. Nature. 2007 May 17;447(7142):342-5. PMID:17507985 doi:http://dx.doi.org/10.1038/nature05702
- ↑ Fielding EN, Widboom PF, Bruner SD. Substrate recognition and catalysis by the cofactor-independent dioxygenase DpgC. Biochemistry. 2007 Dec 11;46(49):13994-4000. Epub 2007 Nov 16. PMID:18004875 doi:10.1021/bi701148b
