Human erythrocyte NADH: (acceptor) oxidoreductase. Kinetic properties and competitive substrate inhibition by ferricyanide.
The kinetic mechanism of human erythrocyte membrane NADH: (acceptor) oxidoreductase (EC 1.6.99.3) was studied by product and substrate inhibition kinetics. With ferricyanide as the substrate, the enzyme reaction follows an ordered bi-bi reaction mechanism. The Michaelis-Menten constants for NADH and ferricyanide are 0.014 and 0.049 mM, respectively. The competitive substrate inhibition effect of ferricyanide was due to its direct binding to the enzyme and forming an inactive binary complex. The dissociation constant of the complex was determined to be 0.37 mM.
D001667:Binding, Competitive; D004910:Erythrocyte Membrane / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology*; D005292:Ferricyanides / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D009247:NADH, NADPH Oxidoreductases / Q000037:antagonists & inhibitors / Q000097:blood*
D005292:Ferricyanides; D009247:NADH, NADPH Oxidoreductases