Fast-Kinetic Studies of the Oxidative Deamination of Glutamate Catalyzed by Glutamate Dehydrogenase
نویسندگان
چکیده
منابع مشابه
Kinetic studies of dogfish liver glutamate dehydrogenase.
Initial-rate studies were made of the oxidation of L-glutamate by NAD+ and NADP+ catalysed by highly purified preparations of dogfish liver glutamate dehydrogenase. With NAD+ as coenzyme the kinetics show the same features of coenzyme activation as seen with the bovine liver enzyme [Engel & Dalziel (1969) Biochem. J. 115, 621--631]. With NADP+ as coenzyme, initial rates are much slower than wit...
متن کاملKinetic studies on the mechanism of the action of ADP on the glutamate dehydrogenase reaction.
ADP is known to activate the glutamate dehydrogenase (GluDH EC 1.4.1.3) reaction above pH 7 [2,3] whereas below this pH ADP is inhibitory. Therefore, it has been postulated that at low pH values, ADP instead of binding to an activator site binds to the inhibitor site which at high pH values is used by GTP [4] Since NAD’ shows a strong self-activating effect [5], the activation by ADP is depende...
متن کاملKinetic studies of dogfish liver glutamate dehydrogenase with diphosphopyridine nucleotide and the effect of added salts.
Kinetic studies have been performed with crystalline dogfish liver glutamate dehydrogenase with the diphosphopyridine nucleotides as cofactors. The kinetic constants for the various substrates have been determined. In its sensitivity to guanosine S-triphosphate, adenosine S&phosphate, and excess reduced diphosphopyridine nucleotide the enzyme is similar to that derived from other vertebrates. T...
متن کاملKinetic Studies of Dogfish Liver Glutamate Dehydrogenase with Diphosphopyridine Nucleotide and the Effect of Added Salts*
Kinetic studies have been performed with crystalline dogfish liver glutamate dehydrogenase with the diphosphopyridine nucleotides as cofactors. The kinetic constants for the various substrates have been determined. In its sensitivity to guanosine S-triphosphate, adenosine S&phosphate, and excess reduced diphosphopyridine nucleotide the enzyme is similar to that derived from other vertebrates. T...
متن کاملKinetic studies of glutamate dehydrogenase with glutamate and norvaline as substrates. Coenzyme activation and negative homotropic interactions in allosteric enzymes.
1. Kinetic studies of glutamate dehydrogenase were made with wide concentration ranges of the coenzymes NAD(+) and NADP(+) and the substrates glutamate and norvaline. Initial-rate parameters were evaluated. 2. Deviations from Michaelis-Menten behaviour towards higher activity were observed with increasing concentrations of either coenzyme with glutamate as substrate, but not with norvaline as s...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1972
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1972.tb02126.x