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鉴定 TrdL 为 10-羟基脱氢酶并从 tirandamycin 生物合成途径中生成新类似物。

Characterization of TrdL as a 10-hydroxy dehydrogenase and generation of new analogues from a tirandamycin biosynthetic pathway.

机构信息

CAS Key Laboratory of Marine Bio-resources Sustainable Utilization, RNAM Center for Marine Microbiology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, 164 West Xingang Road, Guangzhou 510301, PR China.

出版信息

Org Lett. 2011 May 6;13(9):2212-5. doi: 10.1021/ol200447h. Epub 2011 Apr 1.

DOI:10.1021/ol200447h
PMID:21456513
Abstract

TrdL, encoding a flavin-dependent oxidoreductase in the tirandamycin gene cluster, was inactivated to afford a ΔtrdL mutant, the fermentation of which yielded a new intermediate, tirandamycin E (5), and an additional early intermediate, tirandamycin F (6), if XAD-16 resin was introduced. TrdL was overexpressed in E. coli, and the protein was shown to efficiently catalyze the transformations from 5 to tirandamycin A (1) and from 6 to tirandamycin D (4), demonstrating its function as a 10-hydroxy dehydrogenase.

摘要

TrdL,编码替拉霉素基因簇中的黄素依赖氧化还原酶,被失活以获得ΔtrdL 突变体,如果引入 XAD-16 树脂,其发酵会产生新的中间产物替拉霉素 E(5)和另一个早期中间产物替拉霉素 F(6)。TrdL 在大肠杆菌中过表达,并且该蛋白被证明能够有效地催化从 5 到替拉霉素 A(1)和从 6 到替拉霉素 D(4)的转化,证明其作为 10-羟基脱氢酶的功能。

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