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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FK506 生物合成聚酮合酶的丙二酰基特异性酰基转移酶结构域的生化表征。
DOI：
10.2174/0929866521666140926113322
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发表时间：
2015
影响因子：
1.6
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
酰基转移酶（AT）通过自酰化反应和转酰基反应将酰基单位转移到酰基载体蛋白（ACP）中，在聚酮生物合成中发挥重要作用。在这里，我们使用来自筑波链霉菌 YN06 的 FK506 生物合成聚酮合酶 (PKS) 的 AT10FkbA 作为模型来研究 AT 对酰基单元的特异性。我们的结果表明，AT10FkbA在自酰化反应中可以形成丙二酰-O-AT10FkbA和甲基丙二酰-O-AT10FkbA，然而，在转酰化反应中，只有丙二酰-O-AT10FkbA而不是甲基丙二酰-O-AT10FkbA可以将酰基单元转移到ACP中。与已知控制自酰化反应中酰基特异性的一些 AT 不同，AT10FkbA 控制转酰基反应中酰基特异性。
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.