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Literature summary for 2.3.1.39 extracted from

  • Arthur, C.J.; Williams, C.; Pottage, K.; Ploskon, E.; Findlow, S.C.; Burston, S.G.; Simpson, T.J.; Crump, M.P.; Crosby, J.
    Structure and malonyl CoA-ACP transacylase binding of Streptomyces coelicolor fatty acid synthase acyl carrier protein (2009), ACS Chem. Biol., 4, 625-636.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor
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Subunits

Subunits Comment Organism
More acyl carrier protein of fatty acid synthase interacts with malonyl-CoA-ACP-transacylase through the negatively charged helix II of acyl carrier protein. The affinity of polyketide synthase acyl carrier protein for malonyl-CoA-ACP-transacylase is lower than the affinity of the fatty acid synthase acyl carrier protein, and polyketide synthase acyl carrier protein may bind to malonyl-CoA-ACP-transacylase in a different manner Streptomyces coelicolor