Cloning and characterization of a bacterial iterative type I polyketide synthase gene encoding the 6-methylsalicyclic acid synthase
Cloning and characterization of a bacterial iterative type I polyketide synthase gene encoding the 6-methylsalicyclic acid synthase
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DOI：
10.1016/j.bbrc.2006.04.069
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发表时间：
2006-06-23
影响因子：
3.1
通讯作者：
Liu, Wen
中科院分区：
文献类型：
--
作者：
Shao, Lei;Qu, Xu-Dong;Liu, Wen
不寻常聚酮合成酶（pks）是在细菌中发现的一个新家族，其结构为I型，但以迭代方式作用于芳香聚酮生物合成。本文报道了利用快速PCR方法从氯霉素（CHL）产生菌链霉菌（Streptomyces抗生素）DSM 40725中克隆出迭代I型PKS基因chlB1，并鉴定了该基因产物作为6-甲基水杨酸合成酶（6-MSAS）的功能。对各种迭代I型pks的序列分析表明，产物的芳香族或脂肪族结构可能本质上是由双键几何形状控制的配对KR-DH结构域的催化特征决定的。ChlB1作为6-MSAS的发现不仅丰富了目前对细菌中芳香族聚酮生物合成的认识，而且将有助于通过与工程pks组合生物合成产生新的聚酮类似物。(c) 2006爱思唯尔公司版权所有。
Unusual polyketide synthases (PKSs), that are structurally type I but act in an iterative manner for aromatic polyketide biosynthesis, are a new family found in bacteria. Here we report the cloning of the iterative type I PKS gene chlB1 from the chlorothricin (CHL) producer Streptomyces antibioticus DSM 40725 by a rapid PCR approach, and characterization of the function of the gene product as a 6-methylsalicyclic acid synthase (6-MSAS). Sequence analysis of various iterative type I PKSs suggests that the resulting aromatic or aliphatic structure of the products might be intrinsically determined by a catalytic feature of the paired KR-DH domains in the control of the double bond geometry. The finding of ChlB1 as a 6-MSAS not only enriches the current knowledge of aromatic polyketide biosynthesis in bacteria, but will also contribute to the generation of novel polyketide analogs via combinatorial biosynthesis with engineered PKSs. (c) 2006 Elsevier Inc. All rights reserved.