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加利车霉素苔色酸酯C2-O-甲基转移酶CalO6的特性分析

Characterization of the calicheamicin orsellinate C2-O-methyltransferase CalO6.

作者信息

Singh Shanteri, Nandurkar Nitin S, Thorson Jon S

机构信息

Center for Pharmaceutical Research and Innovation, Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY 40536 (USA).

出版信息

Chembiochem. 2014 Jul 7;15(10):1418-21. doi: 10.1002/cbic.201402119.

Abstract

Although bacterial iterative type I polyketide synthases are now known to participate in the biosynthesis of a small set of diverse natural products, the subsequent downstream modification of the resulting polyketide products is poorly understood. We report the functional characterization of the putative orsellinic acid C2-O-methyltransferase, which is involved in calicheamicin biosynthesis. This study suggests that C2-O-methylation precedes C3-hydroxylation/methylation and C5-iodination and requires a coenzyme A- or acyl carrier protein-bound substrate.

摘要

尽管现在已知细菌迭代型I聚酮合酶参与了一小部分多样天然产物的生物合成,但对于由此产生的聚酮产物随后的下游修饰却知之甚少。我们报道了推定的苔色酸C2-O-甲基转移酶的功能特性,该酶参与了刺孢霉素的生物合成。这项研究表明,C2-O-甲基化先于C3-羟基化/甲基化和C5-碘化,并且需要辅酶A或酰基载体蛋白结合的底物。

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