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

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

Volume: 22 Issue: 1

Author(s): 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

Affiliation:

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

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 AT10_FkbA 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 AT10_FkbA can form both malonyl-O-AT10_FkbA and methylmalonyl-O-AT10_FkbA in the self-acylation reaction, however, only malonyl-O-AT10_FkbA but not methylmalonyl-O-AT10_FkbA 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, AT10_FkbA controls the acyl specificity in transacylation reactions.

Cite this article as:

Wang Yue-Yue, Bai Long-Fei, Ran Xin-Xin, Jiang Xin-Hang, Wu Hui, Zhang Wei, Jin Mei-Ying, Li Yong-Quan and Jiang Hui, Biochemical Characterization of a Malonyl-Specific Acyltransferase Domain of FK506 Biosynthetic Polyketide Synthase, Protein & Peptide Letters 2015; 22 (1) . https://dx.doi.org/10.2174/0929866521666140926113322

DOI https://dx.doi.org/10.2174/0929866521666140926113322	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305