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

Acta Biochimica Polonica

Volumn 47, Issue 1, 2000, Pages 259-268

  Fontes, Rui ^a,b   Ribeiro, João Meireles ^a,c   Sillero, Antonio ^a,d  

^a CSIC   (Spain)

^b University of Porto   (Portugal)

^c UNIVERSITY OF EXTREMADURA   (Spain)

^d AUTONOMOUS UNIVERSITY OF MADRID   (Spain)

Author keywords

Enzyme equations; Enzyme inhibition; Enzyme kinetics; Graphical presentations; Rectangular hyperbolas

Indexed keywords

ENZYME;

ARTICLE; CHEMICAL MODEL; KINETICS; MATHEMATICS; METABOLISM;

ENZYMES; KINETICS; MATHEMATICS; MODELS, CHEMICAL;

EID: 0033649138     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.2000_4083     Document Type: Article

References (7)

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. M in enzyme reactions. Science 116, 329-331.