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PMID: 6409097 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Kinetic parameters from progress curves of competing substrates. Application to beta-lactamases.

The Biochemical journal ·Vol. 211 ·No. 2 ·1983-05-01 ·Pages 511-3

Waley SG

Abstract

The use of two substrates, one of them a reporter substrate, is often convenient. The time course of an enzymic reaction with competing substrates is given explicitly in the present paper. Kinetic parameters can be readily obtained. The method is applied to the hydrolysis of benzylpenicillin, with cephalosporin C as the reporter substrate, catalysed by a Pseudomonas beta-lactamase.

MeSH Terms

Binding, Competitive Cephalosporins/metabolism Hydrolysis Kinetics Models, Chemical Penicillin G/metabolism Pseudomonas aeruginosa/enzymology beta-Lactamases/metabolism

Chemicals

Cephalosporins cephalosporin C beta-Lactamases Penicillin G

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Waley S G

References (9)

9 references, click to expand

Cephalosporinase and penicillinase activities of a beta-lactamase from Pseudomonas pyocyanea.
Biochem J. 1965 Sep;96(3):739-52 PMID: 5862414
Characterization of an ammonium transport system in filamentous fungi with methylammonium-14C as the substrate.
J Biol Chem. 1970 Sep 10;245(17):4241-50 PMID: 5498410
A spectrophotometric assay of beta-lactamase action on penicillins.
Biochem J. 1974 Jun;139(3):789-90 PMID: 4368359
Mutant of Pseudomonas aeruginosa 18S that synthesizes type Id beta-lactamase constitutively.
J Bacteriol. 1976 Sep;127(3):1585-6 PMID: 821939
A competition time-course method for following enzymic reactions applied to the hydrolysis of acetamide catalysed by an aliphatic amidase.
FEBS Lett. 1979 Oct 1;106(1):185-8 PMID: 115712
Use of alternative substrates to probe multisubstrate enzyme mechanisms.
Methods Enzymol. 1979;63:486-500 PMID: 502867
Isolation and properties of an inducible and a constitutive beta-lactamase from Pseudomonas aeruginosa.
J Gen Microbiol. 1982 Jan;128(1):155-9 PMID: 6806437
A quick method for the determination of inhibition constants.
Biochem J. 1982 Sep 1;205(3):631-3 PMID: 7150236
The acyl-enzyme mechanism of beta-lactamase action. The evidence for class C Beta-lactamases.
Biochem J. 1982 Nov 1;207(2):315-22 PMID: 6818947

Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj2110511

Published

1983-05-01

Pages

511-3

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1154387

Subset

External Links

PubMed source DOI: 10.1042/bj2110511 PMC Full Text View journal details

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Kinetic parameters from progress curves of competing substrates. Application to beta-lactamases.

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