BIOMAT Database Logo BIOMAT Database Logo

Simplifications of the derivations and forms of steady-state equations for non-equilibrium random substrate-modifier and allosteric enzyme mechanisms. 1976

E P Whitehead

The steady-state equations for "random" enzymic mechanisms (ones with alternative routes for substrate and enzyme to form enzyme-substrate complexes) are non-Michaelian and very complicated when a quasi-equilibrium approximation cannot be used. General methods for simplifying their forms and derivations are given and applied to several single-substrate mechanisms of general or topical interest. The special simplifications resulting from partial ordering of reaction mechanism, from gross inequalities of rate constants, and from special relationships between catalytic and dissociation rate constants, are considered with reference to allosteric mechanisms. Some equations mentioned, but not given here, and more detailed working out of some of those given, have been deposited as Supplementary Publication SUP 50069 (18 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms given in Biochem. J. (1976) 153, 5.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008956 Models, Chemical Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment. Chemical Models,Chemical Model,Model, Chemical
D004798 Enzymes Biological molecules that possess catalytic activity. They may occur naturally or be synthetically created. Enzymes are usually proteins, however CATALYTIC RNA and CATALYTIC DNA molecules have also been identified. Biocatalyst,Enzyme,Biocatalysts
D000494 Allosteric Regulation The modification of the reactivity of ENZYMES by the binding of effectors to sites (ALLOSTERIC SITES) on the enzymes other than the substrate BINDING SITES. Regulation, Allosteric,Allosteric Regulations,Regulations, Allosteric

Related Publications

E P Whitehead
Steady state kinetics of an enzyme reaction with one substrate and one modifier.
June 1968, The Bulletin of mathematical biophysics,
E P Whitehead
Generation of steady-state rate equations for enzyme and carrier-transport mechanisms: a microcomputer program.
January 1989, Methods in enzymology,
E P Whitehead
A guide for interpreting substrate nonlinear steady-state enzyme kinetic data using random models.
October 1972, Archives of biochemistry and biophysics,
E P Whitehead
INTEGRATED STEADY-STATE RATE EQUATIONS FOR ENZYME-CATALYZED REACTIONS.
April 1964, Biochimica et biophysica acta,
E P Whitehead
The degree of steady-state rate equations for multi-subunit allosteric enzymes [proceedings].
January 1977, Biochemical Society transactions,
E P Whitehead
The general modifier ("allosteric") unireactant enzyme mechanism: redundant conditions for reduction of the steady state velocity equation to one that is first degree in substrate and effector.
December 1988, Journal of theoretical biology,
E P Whitehead
The computerized derivation of steady-state rate equations for enzyme kinetics.
October 1984, The Biochemical journal,
E P Whitehead
Kinetics of three substrate enzyme systems. Treatment of partially random mechanisms using equilibrium assumptions.
May 1973, Journal of theoretical biology,
E P Whitehead
A simple method for derivation of rate equations for enzyme-catalyzed reactions under the rapid equilibrium assumption or combined assumptions of equilibrium and steady state.
February 1968, The Journal of biological chemistry,
E P Whitehead
Computer program for the equations describing the steady state of enzyme reactions.
April 1997, Computer applications in the biosciences : CABIOS,
Copied contents to your clipboard!