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PMID: 2400403 Published · ppublish English Comment Journal Article Research Support, Non-U.S. Gov't

Kinetic parameters of the acyl-enzyme mechanism and conditions for quasi-equilibrium and for optimal catalytic characteristics.

The Biochemical journal ·Vol. 270 ·No. 2 ·1990-09-01 ·Pages 561-3

Brocklehurst K, Topham CM

Abstract

暂无摘要

MeSH Terms

Acylation Catalysis Enzymes/metabolism Kinetics Mathematics

Chemicals

Enzymes

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Brocklehurst K

Department of Biochemistry, Medical College of St. Bartholomew's Hospital, University of London, U.K.

Topham C M

References (18)

18 references, click to expand

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The pH-dependence of second-order rate constants of enzyme modification may provide free-reactant pKa values.
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The reaction of p-nitrophenyl esters with chymotrypsin and insulin.
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Effect of evolution on the kinetic properties of enzymes.
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Trypsin-like serine proteinase action: determination of the catalytic parameters KS, k+2 and k/3 under conditions where the substrate exceeds the enzyme concentration.
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THE inhibition of chymotrypsin by diethyl p-nitrophenyl phosphate.
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Evolution of enzyme catalytic power. Characteristics of optimal catalysis evaluated for the simplest plausible kinetic model.
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Accumulation of acyl-enzyme intermediates during turnover of penicillins by the class A beta-lactamase of Staphylococcus aureus PC1.
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Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj2700561

Published

1990-09-01

Pages

561-3

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1131762

Subset

Corrections

ErratumIn

CommentOn

PMID: 2158301

External Links

PubMed source DOI: 10.1042/bj2700561 PMC Full Text View journal details

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Kinetic parameters of the acyl-enzyme mechanism and conditions for quasi-equilibrium and for optimal catalytic characteristics.

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