JOURNAL ARTICLE

Pyruvate Decarboxylase from Zea mays L.

Pat J. Langston-UnkeferThomas C. M. Lee

Year: 1985 Journal:   PLANT PHYSIOLOGY Vol: 79 (2)Pages: 436-440   Publisher: Oxford University Press

Abstract

A significant lag phase was observed in the accumulation of product for the reaction catalyzed by pyruvate decarboxylase (PDC) purified from mature maize kernels. The effects of pH, pyruvate, potassium chloride, PDC concentration, and Mg(2+)-thiamine pyrophosphate upon this lag and upon the observed cooperativity were investigated. PDC preincubated with Mg(2+)-thiamine pyrophosphate for six days had Michaelis-Menten kinetics, a Hill number of 1, and no apparent lag phase. The degree of saturation of PDC with Mg(2+)-thiamine pyrophosphate appears to have a central role in controlling the lag phase and the degree of cooperativity.

Keywords:
Thiamine Pyrophosphate Thiamine pyrophosphate Cooperativity Chemistry Pyruvate carboxylase Pyruvate decarboxylase Biochemistry Potassium Zea mays Kinetics Lag Enzyme Biology Cofactor Organic chemistry

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0.48
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Citation History

Topics

Biochemical Acid Research Studies
Life Sciences →  Biochemistry, Genetics and Molecular Biology →  Biochemistry
Amino Acid Enzymes and Metabolism
Life Sciences →  Biochemistry, Genetics and Molecular Biology →  Biochemistry
Metabolism and Genetic Disorders
Life Sciences →  Biochemistry, Genetics and Molecular Biology →  Clinical Biochemistry

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