These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: A method to describe enzyme-catalyzed reactions by combining steady state and time course enzyme kinetic parameters.
    Author: Walsh R, Martin E, Darvesh S.
    Journal: Biochim Biophys Acta; 2010 Jan; 1800(1):1-5. PubMed ID: 19840832.
    Abstract:
    BACKGROUND: Complete analysis of single substrate enzyme-catalyzed reactions has required a separate use of two distinct approaches. Steady state approximations are employed to obtain substrate affinity and initial velocity information. Alternatively, first order exponential decay models permit simulation of the time course data for the reactions. Attempts to use integrals of steady state equations to describe reaction time courses have so far met with little success. METHODS: Here we use equations based on steady state approximations to directly model time course plots. RESULTS: Testing these expressions with the enzyme beta-galactosidase, which adheres to classical Michaelis-Menten kinetics, produced a good fit between observed and calculated values. GENERAL SIGNIFICANCE: This study indicates that, in addition to providing information on initial kinetic parameters, steady state approximations can be employed to directly model time course kinetics. Integrated forms of the Michaelis-Menten equation have previously been reported in the literature. Here we describe a method to directly apply steady state approximations to time course analysis for predicting product formation and simultaneously obtain multiple kinetic parameters.
    [Abstract] [Full Text] [Related] [New Search]