The Mechanism of Glutamate Dehydrogenase Reaction
نویسندگان
چکیده
منابع مشابه
Kinetic 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...
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Leucine is the only physiologic amino acid that can stimulate insulin release by itself, and a great deal of evidence suggests that leucine does this by allosterically activating glutamate dehydrogenase (GDH). GDH catalyzes the oxidative deamination of endogenous glutamate, which is present at a high concentration in the pancreatic b-cell. Studies that support this role of leucine include the f...
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1. The reaction of glutamate dehydrogenase with N-acetylimidazole and with tetranitromethane leads to modification of tyrosine residues. 2. Modification of 1 tyrosine residue/subunit does not affect the enzymic activity but decreases the response of the enzyme to the allosteric inhibitor, GTP. 3. The physical properties of the enzyme (sedimentation coefficient and optical rotatory dispersion) r...
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This work is a kinetic investigation of the reaction mechanism of malate dehydrogenase, prepared from washed mince of whole bovine heart by a variation on previous methods. The forward and reverse reactions catalyzed by this enzyme have been studied at pH 8.0 in the presence and in the absence of one product at a time, with the use of a recording fluorometer to measure changes in the concentrat...
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The stereospecificity of the chicken heart mitochondrial malate dehydrogenase as well as the ability of this enzyme to form various abortive complexes has been further investigated. The enzyme was found to be specific for the A-hydrogen of NADH. Complex formation of the enzyme with oxalacetate and oxidized coenzymes is pH-dependent and is promoted at alkaline pH values. The enol form of oxalace...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1972
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(20)81786-4