2014•Protein and Peptide LettersRequires access

Biochemical Characterization of a Malonyl-Specific Acyltransferase Domain of FK506 Biosynthetic Polyketide Synthase

Yueyue Wang, Long-Fei Bai, Xin-Xin Ran, Xinhang Jiang, Hui Wu, Wei Zhang, Mei-Ying Jin, Yong‐Quan Li, Hui Jiang

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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Key concepts: Acyltransferase, Polyketide synthase, Acyltransferases, Polyketide, Chemistry, Malonyl-CoA, Biochemistry, Characterization (materials science)