Calculating reaction rate constants and estimating the efficacy of selective enzyme inhibitors

Anal Biochem. 2008 Dec 15;383(2):323-5. doi: 10.1016/j.ab.2008.09.011. Epub 2008 Sep 15.

Abstract

The dynamic steady state of a pair of forward and backward enzymatic reactions is dependent on the balance between the enzymes catalyzing the reactions. By selectively inhibiting one or more of the enzymes involved, this balance is shifted into a new steady state, making it possible to calculate the reaction rate constants after measurement of the reactants. Ideally, the inhibitors should completely eliminate either reaction, but this is often not the case. Here we present and discuss a method for calculating the reaction rate constants and, thus, for evaluating the efficacy of one or more inhibitors when introduced to a forward-backward pair of enzymatic reactions.

MeSH terms

  • Cardiac Myosins / metabolism
  • Enzyme Inhibitors / metabolism*
  • Enzyme Inhibitors / pharmacology*
  • Kinetics
  • Marine Toxins
  • Myocytes, Cardiac / drug effects
  • Myosin Light Chains / metabolism
  • Oxazoles / metabolism
  • Oxazoles / pharmacology
  • Phosphoric Monoester Hydrolases / antagonists & inhibitors
  • Phosphorylation
  • Time

Substances

  • Enzyme Inhibitors
  • Marine Toxins
  • Myosin Light Chains
  • Oxazoles
  • myosin light chain 2
  • calyculin A
  • Phosphoric Monoester Hydrolases
  • Cardiac Myosins