Calculating reaction rate constants and estimating the efficacy of selective enzyme inhibitors.
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.
Eikemo
Hilde
H
Department of Pharmacology and Center for Heart Failure Research, University of Oslo, N-0316 Oslo, Norway. hilde.eikemo@medisin.uio.no
Skomedal
Tor
T
Levy
Finn Olav
FO
Osnes
Jan-Bjørn
JB
D024722:Cardiac Myosins / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000378:metabolism* / Q000494:pharmacology*; D007700:Kinetics; D008387:Marine Toxins; D032383:Myocytes, Cardiac / Q000187:drug effects; D018994:Myosin Light Chains / Q000378:metabolism; D010080:Oxazoles / Q000378:metabolism / Q000494:pharmacology; D010744:Phosphoric Monoester Hydrolases / Q000037:antagonists & inhibitors; D010766:Phosphorylation; D013995:Time
D004791:Enzyme Inhibitors; D008387:Marine Toxins; D018994:Myosin Light Chains; D010080:Oxazoles; C107184:myosin light chain 2; C059041:calyculin A; D010744:Phosphoric Monoester Hydrolases; D024722:Cardiac Myosins