An easy procedure to transform the ratio of two polynomials of first degree into Michaelis-Menten-type equations. Application to the ordered Uni Bi enzyme mechanism.

• Authors: Rui Fontes , João Meireles Ribeiro , Antonio Sillero
• Languages of publication: EN

Abstracts

EN

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.

Keywords

EN

rectangular hyperbolas; enzyme inhibition; enzyme equations; enzyme kinetics; graphical presentations

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2000
• Volume: 47
• Issue: 1
• Pages: 259-268

Dates

published

2000

received

1999-11-3

Contributors

author

Rui Fontes

• Instituto de Investigaciones Biomédicas Alberto Sols, UAM-CSIC, Departamento de Bioquímica, Facultad de Medicina, Arzobispo Morcillo 4, E-28029 Madrid, Spain

author

João Meireles Ribeiro

• Instituto de Investigaciones Biomédicas Alberto Sols, UAM-CSIC, Departamento de Bioquímica, Facultad de Medicina, Arzobispo Morcillo 4, E-28029 Madrid, Spain

author

Antonio Sillero

• 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.