The Theory of Alternative Substrates in Enzyme Kinetics and Its Application to Yeast Hexokinase
Open Access
- 1 November 1972
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 31 (1) , 14-24
- https://doi.org/10.1111/j.1432-1033.1972.tb02494.x
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- The kinetics of enzyme-catalyzed reactions with two or more substrates or products: II. Inhibition: Nomenclature and theoryPublished by Elsevier ,2003
- Use of isotope competition and alternative substrates for studying the kinetic mechanism of enzyme action. I. Experiments with hexokinase and alcohol dehydrogenaseBiochemistry, 1970
- Kinetic Analysis of the Glucosephosphate Isomerase/Glucose-6-Phosphate Dehydrogenase System from Yeastin vitroHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1970
- Étude directe, par dialyse sur Sephadex G‐25, de la formation d'un complexe entre l'hexokinase de levure et ses substratsEuropean Journal of Biochemistry, 1969
- Kinetic Study of Yeast Hexokinase. 1. Steady-State KineticsEuropean Journal of Biochemistry, 1968
- The Statistical Analysis of Enzyme Kinetic DataPublished by Wiley ,1967
- Equilibrium Reaction Rates and Enzyme Mechanisms.Acta Chemica Scandinavica, 1963
- On the Determination of Rate Constants for Coenzyme Mechanisms1Journal of the American Chemical Society, 1958
- The determination of constants in a general coenzyme reaction mechanism by initial rate measurements in the steady stateTransactions of the Faraday Society, 1958
- The Relationship between Michaelis Constants, Maximum Velocities and the Equilibrium Constant for an Enzyme-catalyzed ReactionJournal of the American Chemical Society, 1953