Rethinking ramoplanin: The role of substrate binding in inhibition of peptidoglycan biosynthesis

被引：38

作者：

Helm, JS ^{[1
]}

Chen, L ^{[1
]}

Walker, S ^{[1
]}

机构：

[1] Princeton Univ, Dept Chem, Princeton, NJ 08544 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2002年 / 124卷 / 47期

关键词：

D O I：

10.1021/ja021097n

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Ramoplanin is a cyclicdepsipeptide antibiotic that inhibits peptidoglycan biosynthesis. It was proposed in 1990 to block the MurG step of peptidoglycan synthesis by binding to the substrate of MurG, Lipid I. The proposed mechanism of MurG inhibition has become widely accepted even though it was never directly tested. In this paper, we disprove the accepted mechanism for how ramoplanin functions, and we present an alternative mechanism. This work has implications for the design of ramoplanin derivatives and may influence how other proposed substrate binding antibiotics are studied. Copyright © 2002 American Chemical Society.

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页码：13970 / 13971

页数：2

相关论文

共 25 条

[1] Specificity of induction of glycopeptide resistance genes in Enterococcus faecalis [J].

Baptista, M ;

Depardieu, F ;

Courvalin, P ;

Arthur, M .

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 1996, 40 (10) :2291-2295

[2] Vancomycin, teicoplanin, and ramoplanin: Synthetic and mechanistic studies [J].

Boger, DL .

MEDICINAL RESEARCH REVIEWS, 2001, 21 (05) :356-381

[3] Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic [J].

Breukink, E ;

Wiedemann, I ;

van Kraaij, C ;

Kuipers, OP ;

Sahl, HG ;

de Kruijff, B .

SCIENCE, 1999, 286 (5448) :2361-2364

[4] A-16686, A NEW ANTIBIOTIC FROM ACTINOPLANES .1. FERMENTATION, ISOLATION AND PRELIMINARY PHYSICOCHEMICAL CHARACTERISTICS [J].

CAVALLERI, B ;

PAGANI, H ;

VOLPE, G ;

SELVA, E ;

PARENTI, F .

JOURNAL OF ANTIBIOTICS, 1984, 37 (04) :309-317

[5] Intrinsic lipid preferences and kinetic mechanism of Escherichia coli MurG [J].

Chen, L ;

Men, H ;

Ha, S ;

Ye, XY ;

Brunner, L ;

Hu, Y ;

Walker, S .

BIOCHEMISTRY, 2002, 41 (21) :6824-6833

[6] RAMOPLANIN (A-16686), A NEW GLYCOLIPODEPSIPEPTIDE ANTIBIOTIC .3. STRUCTURE ELUCIDATION [J].

CIABATTI, R ;

KETTENRING, JK ;

WINTERS, G ;

TUAN, G ;

ZERILLI, L ;

CAVALLERI, B .

JOURNAL OF ANTIBIOTICS, 1989, 42 (02) :254-267

[7] INVITRO ACTIVITY OF RAMOPLANIN AGAINST VANCOMYCIN-RESISTANT GRAM-POSITIVE ORGANISMS [J].

COLLINS, LA ;

ELIOPOULOS, GM ;

WENNERSTEN, CB ;

FERRARO, MJ ;

MOELLERING, RC .

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 1993, 37 (06) :1364-1366

[8] Functional analysis of the lipoglycodepsipeptide antibiotic ramoplanin [J].

Cudic, P ;

Behenna, DC ;

Kranz, JK ;

Kruger, RG ;

Wand, AJ ;

Veklich, YI ;

Weisel, JW ;

McCafferty, DG .

CHEMISTRY & BIOLOGY, 2002, 9 (08) :897-906

[9] Complexation of peptidoglycan intermediates by the lipoglycodepsipeptide antibiotic ramoplanin: Minimal structural requirements for intermolecular complexation and fibril formation [J].

Cudic, P ;

Kranz, JK ;

Behenna, DC ;

Kruger, RG ;

Tadesse, H ;

Wand, AJ ;

Veklich, YI ;

Weisel, JW ;

McCafferty, DG .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (11) :7384-7389

[10] Vancomycin derivatives that inhibit peptidoglycan biosynthesis without binding D-Ala-D-Ala [J].

Ge, M ;

Chen, Z ;

Onishi, HR ;

Kohler, J ;

Silver, LL ;

Kerns, R ;

Fukuzawa, S ;

Thompson, C ;

Kahne, D .

SCIENCE, 1999, 284 (5413) :507-511