The monofunctional glycosyltransferase of Escherichia coli is a member of a new class of peptidoglycan-synthesising enzymes - Overexpression and determination of the glycan-polymerising activity

被引：45

作者：

DiBerardino, M ^{[1
]}

Dijkstra, A ^{[1
]}

Stuber, D ^{[1
]}

Keck, W ^{[1
]}

Gubler, M ^{[1
]}

机构：

[1] F HOFFMANN LA ROCHE & CO LTD, PHARMA RES DEPT, CH-4070 BASEL, SWITZERLAND

来源：

FEBS LETTERS | 1996年 / 392卷 / 02期

关键词：

Escherichia coli; monofunctional glycosyltransferase; penicillin-binding protein; peptidoglycan synthesis; cell wall;

D O I：

10.1016/0014-5793(96)00809-5

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：

Using conserved fingerprints in the glycosyltransferase (GTase) domain of high-molecular-weight penicillin-binding proteins (PBP), a gene (mgt) encoding a putative monofunctional glycosyltransferase has been identified in Haemophilus influenzae and in other bacterial species. Here we report the cloning of the homologous Esclterichia coli gene and show that the solubilised membrane fraction of E. coli cells overexpressing the mgt gene contain a significantly increased peptidoglycan synthesis activity. In contrast to the high-molecular-weight PBPs, this activity is not inhibited by Flavomycin.

引用

页码：184 / 188

页数：5

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