Metallo-β-lactamase: Structure and mechanism

Zhigang Wang; Walter Fast; Ann M. Valentine; Stephen J. Benkovic

doi:10.1016/S1367-5931(99)00017-4

Metallo-β-lactamase: Structure and mechanism

Zhigang Wang
, Walter Fast
, Ann M. Valentine
, Stephen J. Benkovic

Chemistry

Research output: Contribution to journal › Review article › peer-review

290 Scopus citations

Abstract

This past year has produced determinations of X-ray crystal structures for three metallo-β-lactamases and the elucidation of the catalytic mechanisms for a monozine and a dizinc enzyme. These advances shed light on how such a diverse group of enzymes are evolving to inactivate so efficiently a broad spectrum of β-lactam antibiotics.

Original language	English (US)
Pages (from-to)	614-622
Number of pages	9
Journal	Current Opinion in Chemical Biology
Volume	3
Issue number	5
DOIs	https://doi.org/10.1016/S1367-5931(99)00017-4
State	Published - Oct 1 1999

All Science Journal Classification (ASJC) codes

Analytical Chemistry
Biochemistry

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10.1016/S1367-5931(99)00017-4

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title = "Metallo-β-lactamase: Structure and mechanism",

abstract = "This past year has produced determinations of X-ray crystal structures for three metallo-β-lactamases and the elucidation of the catalytic mechanisms for a monozine and a dizinc enzyme. These advances shed light on how such a diverse group of enzymes are evolving to inactivate so efficiently a broad spectrum of β-lactam antibiotics.",

author = "Zhigang Wang and Walter Fast and Valentine, \{Ann M.\} and Benkovic, \{Stephen J.\}",

note = "Funding Information: Financial support for the work cited from the authors{\textquoteright} lab was provided by National Institutes of Health grant G.M. 56879-01 (to Stephen J Benkovic) and National Institutes of Health postdoctoral fellowships G.M. 18061 (to Zhigang Wang) and G.M. 20154 (to Ann M Valentine). We thank James Spencer at the Division of Protein Structure, National Institute of Medical Research, UK for providing us with the p rotein d ata b ank coordinates of the S. maltophilia metallo-β-lactamase crystal structure (1SML). ",

year = "1999",

month = oct,

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doi = "10.1016/S1367-5931(99)00017-4",

language = "English (US)",

volume = "3",

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journal = "Current Opinion in Chemical Biology",

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TY - JOUR

T1 - Metallo-β-lactamase

T2 - Structure and mechanism

AU - Wang, Zhigang

AU - Fast, Walter

AU - Valentine, Ann M.

AU - Benkovic, Stephen J.

N1 - Funding Information: Financial support for the work cited from the authors’ lab was provided by National Institutes of Health grant G.M. 56879-01 (to Stephen J Benkovic) and National Institutes of Health postdoctoral fellowships G.M. 18061 (to Zhigang Wang) and G.M. 20154 (to Ann M Valentine). We thank James Spencer at the Division of Protein Structure, National Institute of Medical Research, UK for providing us with the p rotein d ata b ank coordinates of the S. maltophilia metallo-β-lactamase crystal structure (1SML).

PY - 1999/10/1

Y1 - 1999/10/1

N2 - This past year has produced determinations of X-ray crystal structures for three metallo-β-lactamases and the elucidation of the catalytic mechanisms for a monozine and a dizinc enzyme. These advances shed light on how such a diverse group of enzymes are evolving to inactivate so efficiently a broad spectrum of β-lactam antibiotics.

AB - This past year has produced determinations of X-ray crystal structures for three metallo-β-lactamases and the elucidation of the catalytic mechanisms for a monozine and a dizinc enzyme. These advances shed light on how such a diverse group of enzymes are evolving to inactivate so efficiently a broad spectrum of β-lactam antibiotics.

UR - https://www.scopus.com/pages/publications/0032868673

UR - https://www.scopus.com/pages/publications/0032868673#tab=citedBy

U2 - 10.1016/S1367-5931(99)00017-4

DO - 10.1016/S1367-5931(99)00017-4

M3 - Review article

C2 - 10508665

AN - SCOPUS:0032868673

SN - 1367-5931

VL - 3

SP - 614

EP - 622

JO - Current Opinion in Chemical Biology

JF - Current Opinion in Chemical Biology

IS - 5

ER -

Metallo-β-lactamase: Structure and mechanism

Abstract

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