Kinetics of the binding of pyridoxal 5'-phosphate to glutamate decarboxylase.
TLDR
The rate of binding of pyridoxal 5'-phosphate to apoglutamate decarboxylase has been measured as a function of coenzyme concentration at 20°, pH 4.9, and first order kinetics is observed for at least three half-lives.About:
This article is published in Journal of Biological Chemistry.The article was published on 1971-01-25 and is currently open access. It has received 7 citations till now. The article focuses on the topics: Pyridoxal & Glutamate decarboxylase.read more
Citations
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Journal ArticleDOI
Bovine liver glutamate dehydrogenase. Equilibria and kinetics of imine formation by lysine-97 with pyridoxal 5'-phosphate.
Piszkiewicz D,Smith El +1 more
Journal ArticleDOI
The role of Zn2+ in pyridoxal phosphate mediated regulation of glutamic acid decarboxylase in brain.
TL;DR: It is suggested that zinc may play a role in pyridoxal phosphate-mediated regulation of glutamic acid decarboxylase, a major inhibitory neurotransmitter in the CNS.
Journal ArticleDOI
Kinetics and mechanism of the binding of pyridoxal 5'-phosphate to apoglutamate decarboxylase. Evidence for a rate-determining conformation change.
TL;DR: The rate constant for the binding of the coenzyme under optimum conditions is at least 100-fold smaller than that predicted from model reactions.
Journal ArticleDOI
Glutamate decarboxylase: inhibition by monocarboxylic acids.
TL;DR: Aliphatic monocarboxylic acids are demonstrated to be substrate competitive inhibitors of bacterial glutamate decarboxylase and it would appear that the protonated form of valeric acid is the ionic form which interacts most effectively with the enzyme.
Journal ArticleDOI
The effect of anions on the interaction of pyridoxal phosphate with glutamate apodecarboxylase.
TL;DR: Multiple inhibition studies show that phosphate, sulfate, and acetate as inhibitors of pyridoxal-P binding are all competing for the same site, which appears to bind divalent anions tighter than monovalent anions and is sterically hindered for binding long chain carboxylic acids and phenylphosphate.
References
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Book ChapterDOI
Chemical structure in relation to biological activities of vitamin B6.
TL;DR: This chapter examines some of the questions about structural features required for vitamin B6 activity in living organisms and what chemical features determine the ability of the coenzyme to participate in catalysis of the reactions for which it is essential.
Journal ArticleDOI
The Interaction of Pyridoxamine 5-Phosphate with Aspartate Aminotransferase
TL;DR: The effect of pH on the stability of the apoenzyme-pyridoxamine 5-phosphate complex was examined and it was shown that at neutral pH the complex is characterized by an association constant of 1.5 x 107 m-1.
Related Papers (5)
Kinetics and mechanism of the binding of pyridoxal 5'-phosphate to apoglutamate decarboxylase. Evidence for a rate-determining conformation change.
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Horse liver alcohol dehydrogenase. A study of the essential lysine residue.
Soo-Se Chen,Paul C. Engel +1 more