Enzyme kinetics far from the standard quasi-steady-state and equilibrium approximations

  • Authors:
  • S. Schnell;P. K. Maini

  • Affiliations:
  • Centre for Mathematical Biology Mathematical Institute 2429 St Giles', Oxford OX1 3LB, U.K.;Centre for Mathematical Biology Mathematical Institute 2429 St Giles', Oxford OX1 3LB, U.K.

  • Venue:
  • Mathematical and Computer Modelling: An International Journal
  • Year:
  • 2002

Quantified Score

Hi-index 0.98

Visualization

Abstract

Analytic approximations of the time-evolution of the single enzyme-substrate reaction are valid for all but a small region of parameter space in the positive initial enzyme-initial substrate concentration plane. We find velocity equations for the substrate decomposition and product formation with the aid of the total quasi-steady-state approximation and an aggregation technique for cases where neither the more normally employed standard nor reverse quasi-steady-state approximations are valid. Applications to determining reaction kinetic parameters are discussed.