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

[ Vol. 22 , Issue. 1 ]


Yue-Yue Wang, Long-Fei Bai, Xin-Xin Ran, Xin-Hang Jiang, Hui Wu, Wei Zhang, Mei-Ying Jin, Yong-Quan Li and Hui Jiang   Pages 2 - 7 ( 6 )


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.


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


College of Life Sciences, Zhejiang University, Hangzhou, Zhejiang, 310058, China.

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