EC 2.3.1.246 - 3,5-dihydroxyphenylacetyl-CoA synthase

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IntEnz Enzyme Nomenclature
EC 2.3.1.246

Names

Accepted name:
3,5-dihydroxyphenylacetyl-CoA synthase
Other name:
DpgA
Systematic name:
malonyl-CoA:malonyl-CoA malonyltransferase (3,5-dihydroxyphenylacetyl-CoA-forming)

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Pfeifer, V., Nicholson, G. J., Ries, J., Recktenwald, J., Schefer, A. B., Shawky, R. M., Schroder, J., Wohlleben, W., Pelzer, S.
    A polyketide synthase in glycopeptide biosynthesis: the biosynthesis of the non-proteinogenic amino acid (S)-3,5-dihydroxyphenylglycine.
    J. Biol. Chem. 276 : 38370-38377 (2001). [PMID: 11495926]
  2. Chen, H., Tseng, C. C., Hubbard, B. K., Walsh, C. T.
    Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine.
    Proc. Natl. Acad. Sci. U.S.A. 98 : 14901-14906 (2001). [PMID: 11752437]
  3. Tseng, C. C., McLoughlin, S. M., Kelleher, N. L., Walsh, C. T.
    Role of the active site cysteine of DpgA, a bacterial type III polyketide synthase.
    Biochemistry 43 : 970-980 (2004). [PMID: 14744141]
  4. Wu, H. C., Li, Y. S., Liu, Y. C., Lyu, S. Y., Wu, C. J., Li, T. L.
    Chain elongation and cyclization in type III PKS DpgA.
    Chembiochem 13 : 862-871 (2012). [PMID: 22492619]

[EC 2.3.1.246 created 2015]