Pyruvate Decarboxylase from Zea mays L.
- 1 October 1985
- journal article
- research article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 79 (2) , 436-440
- https://doi.org/10.1104/pp.79.2.436
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 Mg2+-thiamine pyrophosphate upon this lag and upon the observed cooperativity were investigated. PDC preincubated with Mg2+-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 Mg2+-thiamine pyrophosphate appears to have a central role in controlling the lag phase and the degree of cooperativity.This publication has 17 references indexed in Scilit:
- Regulation of Cytoplasmic and Vacuolar pH in Maize Root Tips under Different Experimental ConditionsPlant Physiology, 1982
- Transketolase kinetics. The slow reconstitution of the holoenzyme is due to rate-limiting dimerization of the subunits.Journal of Biological Chemistry, 1981
- [8] Hysteretic enzymesPublished by Elsevier ,1980
- The Mechanism of Substrate Activation of Pyruvate Decarboxylase: A First ApproachEuropean Journal of Biochemistry, 1978
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- Regulatory Properties of the Pyruvate-Dehydrogenase Complex from Escherichia coli. Thiamine Pyrophosphate as an EffectorEuropean Journal of Biochemistry, 1974
- Transients and cooperativity. A slow transition model for relating transients and cooperative kinetics of enzymes.1972
- Kinetic aspects of regulation of metabolic processes. The hysteretic enzyme concept.1970
- Kinetic analysis of coupled enzyme assaysBiochemistry, 1969
- Studies on the Nature of the Binding of Thiamine Pyrophosphate to EnzymesJournal of Biological Chemistry, 1968