Biochemical characterization of a malonyl specific acyltransferase domain of FK506 biosynthetic polyketide synthase
Biochemical characterization of a malonyl specific acyltransferase domain of FK506 biosynthetic polyketide synthase
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DOI：
10.2174/0929866521666140926113322
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发表时间：
2015
期刊：
影响因子：
--
通讯作者：
Hui Jiang
中科院分区：
文献类型：
--
作者：
Yue-Yue Wang;Yong-Quan Li;Hui Jiang
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.
