Characterization and Kinetics of Isoenzymes of Pyruvate Kinase from Developing Castor Bean Endosperm

Robert J. Ireland; Vincenzo De Luca; David T. Dennis

doi:10.1104/pp.65.6.1188

Characterization and Kinetics of Isoenzymes of Pyruvate Kinase from Developing Castor Bean Endosperm

PLANT PHYSIOLOGY ◽

10.1104/pp.65.6.1188 ◽

1980 ◽

Vol 65 (6) ◽

pp. 1188-1193 ◽

Cited By ~ 37

Author(s):

Robert J. Ireland ◽

Vincenzo De Luca ◽

David T. Dennis

Keyword(s):

Pyruvate Kinase ◽

Castor Bean ◽

Kinetics Of

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Kinetics of a self-amplifying substrate cycle: ADP–ATP cycling assay

Biochemical Journal ◽

10.1042/bj3500237 ◽

2000 ◽

Vol 350 (1) ◽

pp. 237-243 ◽

Cited By ~ 1

Author(s):

Edelmira VALERO ◽

Ramón VARÓN ◽

Francisco GARCÍA-CARMONA

Keyword(s):

Lactate Dehydrogenase ◽

Kinetic Study ◽

Pyruvate Kinase ◽

Adenylate Kinase ◽

Reaction Medium ◽

Spectrophotometric Assay ◽

Background Signal ◽

Cyclic System ◽

Exponential Increase ◽

Kinetics Of

A kinetic study of an ATP–ADP amplification cyclic system involving the enzymes adenylate kinase, pyruvate kinase and l-lactate dehydrogenase has been made. The stoichiometry of the cycle is 2:1, because two molecules of ADP are synthesized from one each of ATP and AMP, and one molecule of ADP is converted back into one of ATP at each turn of the cycle. This results in a continuous exponential increase in the concentrations of ATP and ADP in the reaction medium, according to the equations obtained. This is therefore a substrate cycle that amplifies itself, the cycling rate increasing continuously with time. The background signal of the reagent was reduced by using apyrase to degrade ATP and ADP in the reagent, permitting detection limits as low as 16pmol of ATP and/or ADP in a continuous spectrophotometric assay.

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A kinetic study of rabbit muscle pyruvate kinase

Biochemical Journal ◽

10.1042/bj1310223 ◽

1973 ◽

Vol 131 (2) ◽

pp. 223-236 ◽

Cited By ~ 48

Author(s):

S. Ainsworth ◽

N. Macfarlane

Keyword(s):

Reaction Mechanism ◽

Kinetic Study ◽

Pyruvate Kinase ◽

Random Order ◽

Experimental Results ◽

Rabbit Muscle ◽

Dead End ◽

Inhibition Constants ◽

Muscle Pyruvate Kinase ◽

Kinetics Of

The paper reports a study of the kinetics of the reaction between phosphoenolpyruvate, ADP and Mg2+ 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, Mg2+, pyruvate and MgATP, and that dead-end complexes, between pyruvate, ADP and Mg2+, 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.

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Partial purification and some regulatory properties of pyruvate kinase from germinating castor bean endosperm

Plant and Cell Physiology ◽

10.1093/oxfordjournals.pcp.a075321 ◽

1976 ◽

Vol 17 (4) ◽

pp. 653-660 ◽

Cited By ~ 11

Author(s):

Hitoshi Nakayama ◽

Michiko Fujii ◽

Kazuo Miura

Keyword(s):

Pyruvate Kinase ◽

Castor Bean ◽

Partial Purification ◽

Regulatory Properties

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Effects of phenylalanine and alanine on the kinetics of bovine pyruvate kinase isoenzymes

Biochemistry ◽

10.1021/bi00689a017 ◽

1975 ◽

Vol 14 (18) ◽

pp. 4041-4045 ◽

Cited By ~ 26

Author(s):

Janet M. Cardenas ◽

J. Jeffrey Strandholm ◽

Joan M. Miller

Keyword(s):

Pyruvate Kinase ◽

Pyruvate Kinase Isoenzymes ◽

Kinetics Of

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A study of the allosteric kinetics of Phycomyces pyruvate kinase as judged by the effect of l-alanine and fructose 1,6-bisphosphate

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology ◽

10.1016/0167-4838(86)90118-4 ◽

1986 ◽

Vol 874 (2) ◽

pp. 193-204 ◽

Cited By ~ 5

Author(s):

Pilar del Valle ◽

Dolores de Arriaga ◽

Felix Busto ◽

Joaquín Soler

Keyword(s):

Pyruvate Kinase ◽

Fructose 1,6 Bisphosphate ◽

Kinetics Of

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An allele (Pk-1 b ) from wild-caught mice that affects the activity and kinetics of erythrocyte and liver pyruvate kinase

Biochemical Genetics ◽

10.1007/bf00484008 ◽

1981 ◽

Vol 19 (7-8) ◽

pp. 771-781 ◽

Cited By ~ 10

Author(s):

Karen J. Moore ◽

Grahame Bulfield

Keyword(s):

Pyruvate Kinase ◽

Kinetics Of

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Purification of Leucoplast Pyruvate Kinase from Developing Castor Bean Endosperm

PLANT PHYSIOLOGY ◽

10.1104/pp.94.4.1528 ◽

1990 ◽

Vol 94 (4) ◽

pp. 1528-1534 ◽

Cited By ~ 20

Author(s):

William C. Plaxton ◽

David T. Dennis ◽

Vicki L. Knowles

Keyword(s):

Pyruvate Kinase ◽

Castor Bean

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On the Role of Magnesium in the Reaction of the Pyruvate Kinase from Salmonella typhimurium

Zeitschrift für Naturforschung C ◽

10.1515/znc-1986-11-1211 ◽

1986 ◽

Vol 41 (11-12) ◽

pp. 1018-1022

Author(s):

Concepcion Garcia-Olalla ◽

Amando Garrido-Pertierra

Keyword(s):

Salmonella Typhimurium ◽

Pyruvate Kinase ◽

Binding Sites ◽

Physiological Significance ◽

Hill Coefficient ◽

Magnesium Concentration ◽

Pyruvate Kinases ◽

Kinetics Of ◽

Binding Behaviour

Abstract The kinetics of the two purified forms of pyruvate kinase from Salmonella typhimurium LT-2 were studied in assays at pH 6.8 where the relationships between the initial velocities of the catalysed reactions and Mg2+ are non-hyperbolic. The analysis show that Mg2+ display positive homotropic interactions in their binding behaviour with Hill coefficient values of 2.5 and 1.2 for the form I and II, respectively. The binding sites of the cation to the pyruvate kinases seem to be independent to those for phosphoenolpyruvate and adenosine 5′-diphosphate; changes in the magnesium concentration might be of physiological significance in relation to a rapid regeneration of adenosine 5′-triphosphate by means of the pyruvate kinase reaction.

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