Kinetics of suicide substrates.

The Biochemical journal ·Vol. 185 ·No. 3 ·1980-03-01 ·Pages 771-3

Waley SG

Abstract

When suicide substrates inactivate enzymes during catalysis, formation of product and inactivation of enzyme proceed concurrently. The steady-state hypothesis is applicable when catalytic quantities of enzyme are used. Equations for the rate of inactivation have been derived and integrated to obtain equations describing progress curves.

MeSH Terms

Enzyme Inhibitors Kinetics Models, Chemical

Chemicals

Enzyme Inhibitors

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Waley S G

References (7)

7 references, click to expand

Mode of inhibition of beta-hydroxydecanoyl thioester dehydrase by 3-decynoyl-N-acetylcysteamine.
J Biol Chem. 1970 Sep 10;245(17):4293-6 PMID: 5498414
The substrate analog, bromopyruvate, as both a substrate and alkylating agent for 2-keto-3-deoxy-6-phosphogluconic aldolase. Kinetic and stereochemical studies.
J Biol Chem. 1972 Jul 10;247(13):4186-91 PMID: 5035689
Mechanism-based irreversible enzyme inhibitors.
Methods Enzymol. 1977;46:28-41 PMID: 909415
Estimation of Michaelis constant and maximum velocity from the direct linear plot.
Biochim Biophys Acta. 1978 Mar 14;523(1):268-72 PMID: 629990
Suicide substrates for the alanine racemase of Escherichia coli B.
Biochemistry. 1978 Apr 4;17(7):1313-21 PMID: 350267
beta-elimination of beta-halo substrates by D-amino acid transaminase associated with inactivation of the enzyme. Trapping of a key intermediate in the reaction.
Biochemistry. 1978 Aug 8;17(16):3377-84 PMID: 687590
Suicide substrates for flavoprotein enzymes.
Methods Enzymol. 1978;53:437-48 PMID: 713849

Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1850771

Published

1980-03-01

Pages

771-3

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1161457

Subset

External Links

PubMed source DOI: 10.1042/bj1850771 PMC Full Text View journal details

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