Type II thioesterase restores activity of a NRPS module stalled with an aminoacyl-S-enzyme that cannot be elongated

被引：90

作者：

Yeh, E

Kohli, RM

Bruner, SD

Walsh, CT

机构：

[1] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

[2] Boston Coll, Dept Chem, Chestnut Hill, MA 02467 USA

来源：

CHEMBIOCHEM | 2004年 / 5卷 / 09期

关键词：

biosynthesis; natural products; nonribosomal pepticle synthetases; type II thioesterase;

D O I：

10.1002/cbic.200400077

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Fidelity and efficiency. Nonribosomal peptide synthetases, which contain domains for the activation (A), thiolation (T), and condensation (C) of amino acids (AA), are high-efficiency, high-fidelity assembly lines for synthesizing peptide natural products. Errors in a single step can have serious consequences for product formation. Type II thioesterases (TEII) might play a critical role in ensuring efficiency and accuracy in these systems, essential features in any attempt to engineer NRPSs to produce novel products.

引用

收藏

页码：1290 / 1293

页数：4

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