In vitro synthesis of cross-linked murein and its attachment to sacculi by PBP1A from Escherichia coli

被引：89

作者：

Born, Petra

Breukink, Eefjan

Vollmer, Waldemar

机构：

[1] Univ Tubingen, D-72076 Tubingen, Germany

[2] Univ Utrecht, Inst Biomembranes, Dept Biochem Membranes, Ctr Biomembranes & Lipid Enzymol, NL-3584 CH Utrecht, Netherlands

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2006年 / 281卷 / 37期

关键词：

D O I：

10.1074/jbc.M604083200

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：

The penicillin-binding protein (PBP) 1A is a major murein (peptidoglycan) synthase in Escherichia coli. The murein synthesis activity of PBP1A was studied in vitro with radioactive lipid II substrate. PBP1A produced murein glycan strands by transglycosylation and formed peptide cross-links by transpeptidation. Time course experiments revealed that PBP1A, unlike PBP1B, required the presence of polymerized glycan strands carrying monomeric peptides for cross-linking activity. PBP1A was capable of attaching nascent murein synthesized from radioactive lipid II to nonlabeled murein sacculi. The attachment of the new material occurred by transpeptidation reactions in which monomeric tri- and tetrapeptides in the sacculi were the acceptors.

引用

收藏

页码：26985 / 26993

页数：9

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