Kinetic studies of glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle.
Initial rate studies at pH 7.6 with three aldehydes, product inhibition patterns with NADH and dead-end inhibition with adenosine diphosphoribose show that the kinetic mechanism of glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle cannot be ordered, and support an enzyme-substitution mechanism. Deviations from Michaelis-Menten behaviour are consistent with negative interactions in the binding of NAD+ and instability of the species E(NAD)3 and E(NAD)4. Inhibition with large concentrations of phosphate and arsenate indicates competition for a binding site for glyceraldehyde 3-phosphate, and is not found with glyceraldehyde as substrate.
D000247:Adenosine Diphosphate Sugars / Q000494:pharmacology; D000818:Animals; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D011817:Rabbits; D012266:Ribose / Q000494:pharmacology; D013379:Substrate Specificity
D000247:Adenosine Diphosphate Sugars; D012266:Ribose; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases