A kinetic study of rabbit muscle pyruvate kinase.

The Biochemical journal ·Vol. 131 ·No. 2 ·1973-02-00 ·Pages 223-36

Ainsworth S, MacFarlane N

Abstract

The paper reports a study of the kinetics of the reaction between phosphoenolpyruvate, ADP and Mg(2+) catalysed by rabbit muscle pyruvate kinase. The experimental results indicate that the reaction mechanism is equilibrium random-order in type, that the substrates and products are phosphoenolpyruvate, ADP, Mg(2+), pyruvate and MgATP, and that dead-end complexes, between pyruvate, ADP and Mg(2+), form randomly and exist in equilibrium with themselves and other substrate complexes. Values were determined for the Michaelis, dissociation and inhibition constants of the reaction and are compared with values ascertained by previous workers.

MeSH Terms

Adenosine Diphosphate Animals Binding Sites Chromatography, Gel Chromatography, Ion Exchange Computers Kinetics Magnesium Mathematics Models, Biological Muscles/enzymology Phosphoenolpyruvate Protein Binding Pyruvate Kinase/metabolism Rabbits Spectrophotometry, Ultraviolet

Chemicals

Adenosine Diphosphate Phosphoenolpyruvate Pyruvate Kinase Magnesium

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Ainsworth S

MacFarlane N

References (28)

28 references, click to expand

EFFECTS OF TEMPERATURE, SUBSTRATE, AND ACTIVATING CATIONS ON THE CONFORMATIONS OF PYRUVATE KINASE IN AQUEOUS SOLUTIONS.
J Am Chem Soc. 1965 Feb 20;87:897-900 PMID: 14284619
The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations.
Biochim Biophys Acta. 1963 Jan 8;67:104-37 PMID: 14021667
Statistical estimations in enzyme kinetics.
Biochem J. 1961 Aug;80:324-32 PMID: 13785321
Glutamic dehydrogenase. III. The order of substrate addition in the enzymatic reaction.
J Biol Chem. 1959 Nov;234:2891-6 PMID: 13825045
Kinetic analysis of enzyme reactions. II. The potassium activation and calcium inhibition of pyruvic phosphoferase.
J Biol Chem. 1953 Feb;200(2):669-82 PMID: 13034826
The role of metal ions in the pyruvic kinase reaction.
Biochemistry. 1965 Aug;4(8):1518-25 PMID: 5863318
Ultraviolet absorption spectra of adenosine-5'-triphosphate and related 5'-ribonucleotides.
Arch Biochem Biophys. 1956 Jun;62(2):253-64 PMID: 13328113
A direct spectrophotometric assay for pyruvate kinase.
Anal Biochem. 1967 May;19(2):272-9 PMID: 4292753
PRODUCT INHIBITION STUDIES ON YEAST AND LIVER ALCOHOL DEHYDROGENASES.
Biochemistry. 1963 Sep-Oct;2:935-41 PMID: 14087384
Kinetic and magnetic resonance studies of the pyruvate kinase reaction. II. Complexes of enzyme, metal, and substrates.
J Biol Chem. 1966 Mar 10;241(5):1178-93 PMID: 5933875
Effect of temperature and effectors on the conformations of yeast pyruvate kinase.
Biochemistry. 1970 Feb 17;9(4):939-45 PMID: 5417407
Physical properties of crystalline fluorokinase.
Arch Biochem Biophys. 1958 Dec;78(2):494-6 PMID: 13618031
Stereochemistry of pyruvate kinase, pyruvate carboxylase, and malate enzyme reactions.
J Biol Chem. 1970 Nov 25;245(22):6052-6 PMID: 5484463
Adipose-tissue pyruvate kinase. Properties and interconversion of two active forms.
Biochem J. 1968 Nov;110(1):67-77 PMID: 4972650
[Phosphoenolpyruvate as substrate of alkaline phosphatase: competition with pyruvate kinase].
Hoppe Seylers Z Physiol Chem. 1965;341(1):44-75 PMID: 5876232
Computer programmes for processing enzyme kinetic data.
Nature. 1963 May 4;198:463-5 PMID: 14021666
Kinetic studies on the mechanism of the malate dehydrogenase reaction.
J Biol Chem. 1968 May 10;243(9):2413-23 PMID: 4296842
Some reactions of adenosine and inosine phosphates in animal tissues.
Biochim Biophys Acta. 1953 Sep-Oct;12(1-2):172-80 PMID: 13115426
The correlation of reaction kinetics and substrate binding with the mechanism of pyruvate kinase.
J Biol Chem. 1961 Aug;236:2277-83 PMID: 13741081
Stereochemistry of the enzymatic carboxylation of phosphoenolpyruvate.
J Biol Chem. 1969 Nov 25;244(22):6130-3 PMID: 5389102
Studies on the enolization of pyruvate by pyruvate kinase.
J Biol Chem. 1960 Apr;235:1170-7 PMID: 14438835
The statistical analysis of enzyme kinetic data.
Adv Enzymol Relat Areas Mol Biol. 1967;29:1-32 PMID: 4881884
POTENTIOMETRIC STUDIES OF THE SECONDARY PHOSPHATE IONIZATIONS OF AMP, ADP, AND ATP, AND CALCULATIONS OF THERMODYNAMIC DATA FOR THE HYDROLYSIS REACTIONS.
Biochemistry. 1963 May-Jun;2:501-8 PMID: 14069537
Yeast pyruvate kinase. II. Kinetic properties.
J Biol Chem. 1969 Sep 25;244(18):4819-22 PMID: 5824555
A kinetic study of Baker's-yeast pyruvate kinase activated by fructose 1,6-diphosphate.
Biochem J. 1972 Oct;129(5):1035-47 PMID: 4571175
The interpretation of kinetic data for enzyme-catalysed reactions involving three substrates.
Biochem J. 1969 Sep;114(3):547-56 PMID: 5820641
KINETIC AND MAGNETIC RESONANCE STUDIES OF THE PYRUVATE KINASE REACTION. I. DIVALENT METAL COMPLEXES OF PYRUVATE KINASE.
J Biol Chem. 1965 Jan;240:238-46 PMID: 14253420
Equilibrium and kinetic studies of the pyruvic kinase reaction.
J Biol Chem. 1959 Aug;234(8):2151-7 PMID: 13673030

Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj1310223

Published

1973-02-00

Pages

223-36

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1177461

Subset

External Links

PubMed source DOI: 10.1042/bj1310223 PMC Full Text View journal details

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A kinetic study of rabbit muscle pyruvate kinase.

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