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.
Keywords: Acyltransferase, FK506, malonyl-CoA, methylmalonyl-CoA, polyketide synthase.
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