Journal
Article title
Title variants
Languages of publication
Abstracts
It is not always clear that some equations affected by complicated factors can, actually, be interpreted as a ratio of two polynomials of first degree and so that they can be, in general, represented by rectangular hyperbolas. In this paper we present an easy procedure to rearrange those equations into Michaelis-Menten-type equations and so to make the aspects of these rectangular hyperbolas more clear, particularly for researchers familiar with general biochemistry. As an example, the method is applied to transform the classical rate equation of the Cleland×s Ordered Uni Bi enzyme mechanism.
Journal
Year
Volume
Issue
Pages
259-268
Physical description
Dates
published
2000
received
1999-11-3
Contributors
author
- Instituto de Investigaciones Biomédicas Alberto Sols, UAM-CSIC, Departamento de Bioquímica, Facultad de Medicina, Arzobispo Morcillo 4, E-28029 Madrid, Spain
author
- Instituto de Investigaciones Biomédicas Alberto Sols, UAM-CSIC, Departamento de Bioquímica, Facultad de Medicina, Arzobispo Morcillo 4, E-28029 Madrid, Spain
author
- Instituto de Investigaciones Biomédicas Alberto Sols, UAM-CSIC, Departamento de Bioquímica, Facultad de Medicina, Arzobispo Morcillo 4, E-28029 Madrid, Spain
References
- 1. Fontes, R., Ribeiro, J.M. & Sillero, A. (1999) Inhibition and activation of enzymes. The effect of a modifier on the reaction rate and on kinetic parameters. Acta Biochim. Polon. 47, 233-258.
- 2. Cleland, W.W. (1963) The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. Biochim. Biophys. Acta 67, 104-137.
- 3. Fontes, R., Ribeiro, J.M. & Sillero, A. (1994) A tridimensional representation of enzyme inhibition useful for diagnostic purposes. J. Enzym. Inhib. 8, 73-85.
- 4. Lineweaver, H. & Burk, D. (1934) The determination of enzyme dissociation constants. J. Am. Chem. Soc. 56, 658-666.
- 5. Hanes, C.S. (1932) CLXVII. Studies on plant amylases. I. The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley. Biochem. J. 26, 1406-1421.
- 6. Eadie, G.S. (1942) The inhibition of cholinesterase by physostigmine and prostigmine. J. Biol. Chem. 146, 85-93.
- 7. Hofstee, B.H.J. (1952) On the evaluation of the constants Vm and KM in enzyme reactions. Science 116, 329-331.
Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv47i1p259kz