Substrate Specificity of Crystalline Frog Liver Glutamate Dehydrogenase
نویسندگان
چکیده
منابع مشابه
The dependence of the substrate specificity on the conformation of crystalline glutamate dehydrogenase.
Glutamate dehydrogenase (L-glutamate-NAD(P) oxidoreductase EC 1.4.1.3) from bovine liver catalyzes the reversible oxidative deamination of various monocarboxylic amino acids, as well as of n-glutamate (1, 2). Several years ago, we reported that estrogenic steroids both inhibited the oxidation of L-glutamate (3) and stimulated the oxidation of L-alanine (4). Conversely, adenosine diphosphate was...
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In the course of preparing carbamyl phosphate synthetase from frog liver, a crystalline protein fraction was obtained which proved to be glutamate dehydrogenase. Because of the considerable interest in this enzyme and the striking differences in certain properties of this enzyme from different animal sources (l-6), it seemed of importance to study the kinetic properties of crystalline frog live...
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1. The effect of pyridoxal 5'-phosphate on the activity of ox liver glutamate dehydrogenase towards different amino acid substrates was investigated. 2. Both alanine and glutamate activities decreased steadily in the presence of pyridoxal 5'phosphate. 3. The alanine/glutamate activity ratio increased as a function of inactivation by pyridoxal 5'-phosphate, indicating that glutamate activity is ...
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The thionicotinamide analogues of NAD+ and NADP+ were shown to be good alternative coenzymes for bovine glutamate dehydrogenase, with similar affinity and approx. 40% of the maximum velocity obtained with the natural coenzymes. Both thionicotinamide analogues show non-linear Lineweaver-Burk plots, which with the natural coenzymes have been attributed to negative co-operativity. Since the reduce...
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The Lys80, Gly82 and Met101 residues of glutamate dehydrogenase from Bacillus subtilis were mutated into a series of single mutants. The wild-type enzyme was highly specific for 2-oxoglutarate, whereas G82K and M101S dramatically switched to increased specificity for oxaloacetate with kcat values 3.45 and 5.68 s-1, which were 265-fold and 473-fold higher respectively than those for 2-oxoglutarate.
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1965
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)97024-9