Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.4.1.2 (glutamate dehydrogenase)
4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Pulse radiolysis and 60Co gamma radiolysis were used to study the effects of ionizing radiations on the activity of glutamate dehydrogenase. Hydroxyl radicals are considerably more effective than hydrated electrons in causing loss of enzymatic activity. Evidence is also presented that the free radical anions (SCN)-.2, (Br)-.2, and (I)-.2 react with the enzyme and cause a loss of enzymatic activity. The results implicate the possible involvement of cysteine, tyrosine, and tryptophan residues in the activity of glutamate dehydrogenase.
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PMID:The radiation inactivation of glutamate dehydrogenase. 682 10

Increasing concentrations of anions of the Hofmeister series decrease the activity of highly purified glutamate dehydrogenase (EC 1.4.1.2.) from Pisum sativum L. The extent of the inactivation, as estimated by the ion concentration which causes a 50% transformation of the native form to the low activity form of the enzyme (approximately "halfmaximal activity"), follows the ranking Cl(-)<F(-)<Br(-)<NO 3 (-) <SCN(-). Sulfate has a slightly activating effect. At salt concentrations higher than 1 M (with SCN(-) higher than 200 mM), the activity decreases to a value from 3-6% of the initial activity and remains then stable over a wide range of higher anion concentrations. From kinetic investigations it is seen that the treatment of the enzyme with anions decreases the affinity for the cosubstrate NAD(+) and the substrate L-glutamate (K M-values increased) and also increases the dissociation constant for NAD(+). The salt induced inactivation is reversible by dilution. From a mathematical treatment of the kinetic data of the inactivation, it is seen that increasing concentrations of the anions exert cooperative effects on the inactivation process.
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PMID:The effect of neutral salt anions on the oxidative deamination activity of plant glutamate dehydrogenase. 2441 11