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  • Title: Biochemical characterization of a malonyl-specific acyltransferase domain of FK506 biosynthetic polyketide synthase.
    Author: Wang YY, Bai LF, Ran XX, Jiang XH, Wu H, Zhang W, Jin MY, Li YQ, Jiang H.
    Journal: Protein Pept Lett; 2015; 22(1):2-7. PubMed ID: 25267255.
    Abstract:
    Acyltransferases (ATs) play an essential role in the polyketide biosynthesis through transferring acyl units into acyl carrier proteins (ACPs) via a self-acylation reaction and a transacylation reaction. Here we used AT10FkbA of FK506 biosynthetic polyketide synthase (PKS) from Streptomyces tsukubaensis YN06 as a model to study the specificity of ATs for acyl units. Our results show that AT10FkbA can form both malonyl-O-AT10FkbA and methylmalonyl-O-AT10FkbA in the self-acylation reaction, however, only malonyl-O-AT10FkbA but not methylmalonyl-O-AT10FkbA can transfer the acyl unit into ACPs in the transacylation reaction. Unlike some ATs that are known to control the acyl specificity in self-acylation reactions, AT10FkbA controls the acyl specificity in transacylation reactions.
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