Studies on the Nature of the Binding of Thiamine Pyrophosphate to Enzymes
A. V. Morey,Elliot Juni +1 more
TLDR
Thiazole pyrophosphate, a potent inhibitor of resolved yeast pyruvate decarboxylase, acts by binding to coenzyme sites on the enzyme and question the validity of calculating dissociation constants for cofactors which do not dissociate from their enzymes.About:
This article is published in Journal of Biological Chemistry.The article was published on 1968-06-10 and is currently open access. It has received 38 citations till now. The article focuses on the topics: Pyruvate decarboxylase & Pyruvate oxidase.read more
Citations
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Journal ArticleDOI
Pyruvate decarboxylase from Zymomonas mobilis. Isolation and partial characterization
TL;DR: Pyruvate decarboxylase (EC 4.1.1) from the ethanol producing bacterium Zymomonas mobilis was purified to homogeneity and showed a single band in sodium dodecylsulfate gel electrophoresis which indicated that the enzyme consists of four probably identical subunits.
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Studies on the reconstitution of apotransketolase with thiamine pyrophosphate and analogs of the coenzyme
TL;DR: The binding of thiltmine pyrophosphate to apotransketolase from baker’s yeast has been studied by measuring the cofactor-dependent activity after passage through a column of Sephadex G-25 or dialysis, indicating reversible binding.
Journal ArticleDOI
The Pyruvate Formate-lyase System of Streptococcus faecalis I. PURIFICATION AND PROPERTIES OF THE FORMATE-PYRUVATE EXCHANGE ENZYME
TL;DR: The enzyme exchanging formate with the carboxyl of pyruvate was purified 195-fold from extracts of Streptococcus faecalis by a procedure involving protamine treatment, dialysis, and gradient centrifugation.
Journal ArticleDOI
Transketolase kinetics. The slow reconstitution of the holoenzyme is due to rate-limiting dimerization of the subunits.
Journal ArticleDOI
Pyruvate Decarboxylase I. PROTEIN DISSOCIATION INTO SUBUNITS UNDER CONDITIONS IN WHICH THIAMINE PYROPHOSPHATE IS RELEASED
TL;DR: Thiamine-PP in addition to its catalytic role also functions in the formation of a stable dimer which is the active holoenzyme, suggesting a monomer-dimer equilibrium which favors the monomer.
References
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The formation of sedoheptulose phosphate from pentose phosphate
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Isoleucine and valine metabolism in Escherichia coli. X. The enzymatic formation of acetohydroxybutyrate.
Leavitt Ri,H. E. Umbarger +1 more
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Carboxylases of animal tissues
Journal ArticleDOI
ISOLATION AND PROPERTIES OF THE α-CARBOXYLASE OF WHEAT GERM
Thomas P. Singer,Jack Pensky +1 more
TL;DR: The present report is an account of the purification and properties of this enzyme from wheat germ, which can be prepared in a highly purified state by a relatively simple procedure, and the final product is considerably more active than the best preparations obtained from yeast.
Related Papers (5)
Structure and Mechanism of Action of the Active Center of Yeast Pyruvate Decarboxylase
Mechanism of action of transketolase. I. Properties of the crystalline yeast enzyme.
Asoke G. Datta,Efraim Racker +1 more