Tailoring enzymes that modify nonribosomal peptides during and after chain elongation on NRPS assembly lines

被引：239

作者：

Walsh, CT ^{[1
]}

Chen, HW ^{[1
]}

Keating, TA ^{[1
]}

Hubbard, BK ^{[1
]}

Losey, HC ^{[1
]}

Luo, LS ^{[1
]}

Marshall, CG ^{[1
]}

Miller, DA ^{[1
]}

Patel, HM ^{[1
]}

机构：

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

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2001年 / 5卷 / 05期

关键词：

D O I：

10.1016/S1367-5931(00)00235-0

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：

Nonribosomal peptide synthetases are large enzyme complexes that synthesize a variety of peptide natural products through a thiotemplated mechanism. Assembly of the peptides proceeds through amino acid loading, amide-bond formation and chain translocation, and finally thioester lysis to release the product. The final products are often heavily modified, however, through methylation, epimerization, hydroxylation, heterocyclization, oxidative cross-linking and attachment of sugars. These activities are the province of specialized enzymes (either embedded in the multidomain nonribosomal peptide synthetase structure or standalone).

引用

页码：525 / 534

页数：10

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