A novel glycan polymerase that synthesizes uncross‐linked peptidoglycan in Escherichia coli

FEBS Letters

Suzuki, Hideho¹  Hara, Hiroshi¹ 

[1] Laboratory of Genetics, Department of Biology, Faculty of Science, University of Tokyo, Tokyo 113, Japan

关键词: In vitro peptidoglycan synthesis;    Lipid intermediate;    Glycan polymerase;    Peptidoglycan cross-linking;    Penicillin-binding protein;    Moenomycin;    PBP;    penicillin-binding protein;    DMSO;    dimethyl sulfoxide;    Pipes;    piperazine-N;    N′-bis(2-ethanesulfonic acid);    DTT;    dithiothreitol;   

DOI  :  10.1016/0014-5793(84)80226-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A simple and efficient procedure to assay peptidoglycan synthesis in vitro was established. By this procedure, a novel activity for glycan polymerization in Escherichia coli was found in the fraction containing no detectable penicillin-binding protein (PBP). This polymerase activity was relatively insensitive to moenomycin, showed requirement for Ca²⁺ or Mn²⁺ but not for Mg²⁺, and led to production of uncross-linked glycan chains. These properties distinguished the glycan polymerase from the activities shown by the fractions containing PBPs. The glycan polymerase catalyzing polymerization of glycan units from lipid intermediates was purified and identified as a protein of 34 kDa.

【 授权许可】

Unknown