Lacticin 481 synthetase phosphorylates its substrate during lantibiotic production

被引：110

作者：

Chatterjee, C ^{[1
]}

Miller, LM ^{[1
]}

Leung, YL ^{[1
]}

Xie, LL ^{[1
]}

Yi, MS ^{[1
]}

Kelleher, NL ^{[1
]}

van der Donk, WA ^{[1
]}

机构：

[1] Univ Illinois, Dept Chem, Urbana, IL 61801 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2005年 / 127卷 / 44期

关键词：

D O I：

10.1021/ja0543043

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Lacticin 481 synthetase (LctM) catalyzes the ATP-dependent conversion of a ribosomally synthesized peptide to a polycyclic thioether antibiotic. It is a bifunctional enzyme that dehydrates four Ser/Thr residues to the corresponding dehydro amino acids and catalyzes the conjugate addition of Cys residues to these dehydro residues in a regio- and stereoselective process. We show here that incubation of truncated substrates with LctM results in products that are phosphorylated in the region of dehydration. Furthermore, synthetic peptides containing phosphorylated Ser and/or Thr residues are accepted by the enzyme as substrates resulting in the elimination of phosphate and dehydro amino acid production. This activity is only observed if ADP is added as cosubstrate. These results argue strongly that the enzyme utilizes ATP to phosphorylate the Ser/Thr residues that are targeted for dehydration. ATP does not appear to be required for peptide translocation or cyclization. Copyright © 2005 American Chemical Society.

引用

页码：15332 / 15333

页数：2

共 25 条

[1] Contribution of phosphate intrinsic binding energy to the enzymatic rate acceleration for triosephosphate isomerase [J].