Home LiteratureArticle Details

PMID: 3143353 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Kinetic characterization of the acyl-enzyme mechanism for beta-lactamase I.

The Biochemical journal ·Vol. 254 ·No. 3 ·1988-09-15 ·Pages 923-5

Martin MT, Waley SG

Abstract

beta-Lactamase I catalyses the hydrolysis of penicillins by an acyl-enzyme mechanism. A procedure was developed for determining the rate constants for the acylation and deacylation steps for the good substrates benzylpenicillin and phenoxymethylpenicillin; this depends on determining the fraction of enzyme that is present as acyl-enzyme in the steady state.

MeSH Terms

Acylation Binding Sites Hydrogen-Ion Concentration Hydrolysis Kinetics Penicillin G/metabolism Penicillin V/metabolism Penicillinase/metabolism

Chemicals

Penicillinase Penicillin G Penicillin V

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Martin M T

Sir William Dunn School of Pathology, University of Oxford, U.K.

Waley S G

References (14)

14 references, click to expand

Diffusion-limited component of reactions catalyzed by Bacillus cereus beta-lactamase I.
Biochemistry. 1984 Mar;23(6):1275-82 PMID: 11491129
A spectrophotometric assay of beta-lactamase action on penicillins.
Biochem J. 1974 Jun;139(3):789-90 PMID: 4368359
A direct spectrophotometric assay and determination of Michaelis constants for the beta-lactamase reaction.
Anal Biochem. 1975 Jan;63(1):17-26 PMID: 803320
Separation, purification and properties of beta-lactamase I and beta-lactamase II from Bacillus cereus 569/H/9.
Biochem J. 1974 Oct;143(1):115-27 PMID: 4219278
6 beta-Bromopenicillanic acid inactivates beta-lactamase I.
Biochem J. 1979 Jan 1;177(1):365-7 PMID: 218563
Production of a variant of beta-lactamase II with selectively decreased cephalosporinase activity by a mutant of Bacillus cereus 569/H/9.
Biochem J. 1980 Oct 1;191(1):111-6 PMID: 6781486
The preparation and some properties of penicillenic acid derivatives relevant to penicillin hypersensitivity.
J Exp Med. 1962 Apr 1;115:803-19 PMID: 14483914
Direct determination of acetyl-enzyme intermediate in the acetylcholinesterase-catalyzed hydrolysis of acetylcholine and acetylthiocholine.
J Biol Chem. 1984 Sep 10;259(17):11010-3 PMID: 6469995
Single-turnover and steady-state kinetics of hydrolysis of cephalosporins by beta-lactamase I from Bacillus cereus.
Biochem J. 1985 Oct 1;231(1):83-8 PMID: 3933490
Tertiary structural similarity between a class A beta-lactamase and a penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase.
Nature. 1986 Mar 27-Apr 2;320(6060):378-80 PMID: 3485771
Progress-curve analysis in enzyme kinetics. Numerical solution of integrated rate equations.
Biochem J. 1986 Apr 15;235(2):613-5 PMID: 3741409
Bacterial resistance to beta-lactam antibiotics: crystal structure of beta-lactamase from Staphylococcus aureus PC1 at 2.5 A resolution.
Science. 1987 May 8;236(4802):694-701 PMID: 3107125
beta-lactamase I from Bacillus cereus. Structure and site-directed mutagenesis.
Biochem J. 1987 Dec 15;248(3):657-62 PMID: 3124817
Half-time analysis of the integrated Michaelis equation. Simulation and use of the half-time plot and its direct linear variant in the analysis of some alpha-chymotrypsin, papain- and fumarase-catalysed reactions.
Biochem J. 1982 May 1;203(2):351-60 PMID: 7115291

Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj2540923

Published

1988-09-15

Pages

923-5

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1135174

Subset

External Links

PubMed source DOI: 10.1042/bj2540923 PMC Full Text View journal details

Analysis Services

Kinetic characterization of the acyl-enzyme mechanism for beta-lactamase I.

Contact

WeChat Official Account