ExplorEnz: EC 2.3.1.246

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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]

[EC 2.3.1.246 created 2015]