Temperature-jump studies on glutamate dehydrogenase
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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...
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Mutants of Salmonella typhimurium defective in glutamate dehydrogenase activity were isolated in parent strains lacking glutamate synthase activity by localizcd mutagenesis or by a general mutagenesis combined with a cycloserine enrichment for glutamate auxotrophs. Two mutants with temperature-sensitive phenotypes had glutamate dehydrogenase activities that were more thermolabile than that of a...
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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...
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About 2 years ago the author reported that the activity of purified preparations of succinic dehydrogenase is enhanced by phosphate buffer (2). This enhancement was dependent upon the phosphate concentration and appeared to be relatively specific for phosphate, since other buffers, such as Tris,l imidazole, histidine, glycylglycine, and arsenate did not induce it (2, 3). Arsenate, in fact, inte...
متن کاملOx liver glutamate dehydrogenase
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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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1972
ISSN: 0306-3283
DOI: 10.1042/bj1280098pa