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PMID: 6333871 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The active site of the P99 beta-lactamase from Enterobacter cloacae.

The Biochemical journal ·Vol. 223 ·No. 1 ·1984-10-01 ·Pages 271-4

Joris B, Dusart J, Frere JM, van Beeumen J, Emanuel EL, Petursson S, Gagnon J, Waley SG

Abstract

Labelling the beta-lactamase of Enterobacter cloacae P99 with a poor substrate or a mechanism-based inactivator points to an active-site serine residue in a sequence closely resembling that of the ampC beta-lactamase. These results establish the P99 enzyme as a class-C beta-lactamase, and the concurrence of the two approaches helps to confirm the reliability of determining active-site sequences with the aid of mechanism-based inactivators.

MeSH Terms

Amino Acids/analysis Binding Sites Chromatography, High Pressure Liquid Enterobacter/enzymology Enterobacteriaceae/enzymology Peptide Fragments/analysis beta-Lactamases

Chemicals

Amino Acids Peptide Fragments beta-Lactamases

Authors & Affiliations

8 authors, click to expand affiliations / ORCID

Joris B

Dusart J

Frere J M

van Beeumen J

Emanuel E L

Petursson S

Gagnon J

Waley S G

References (17)

17 references, click to expand

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Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj2230271

Published

1984-10-01

Pages

271-4

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1144291

Subset

External Links

PubMed source DOI: 10.1042/bj2230271 PMC Full Text View journal details

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The active site of the P99 beta-lactamase from Enterobacter cloacae.

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