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Glutamate dehydrogenase of Sphagnum
Phytochemistry, 1997Abstract Glutamate dehydrogenase (GDH) of S. fallax was purified 2000-fold to apparent homogeneity. As estimated by gel filtration and SDS-PAGE, a native molecular weight of M r 210 000 and a subunit molecular weight of M r 52 000 were determined, indicating that the enzyme is tetrameric with subunits of identical molecular weights.
Jóska Gerendás +3 more
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Kinetic mechanism of glutamate dehydrogenase
Biochemistry, 1980Initial velocity patterns and dead-end inhibition studies with oxalylglycine suggest that the addition of NADPH, keto acid, and ammonia occurs with obligatory order. For monocarboxylic keto acids, the keto acid-ammonia initial velocity pattern is equilibrium ordered because koff is much greater than Vmax.
James E. Rife, W. W. Cleland
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Allosteric Transitions of Glutamate Dehydrogenase
Nature, 1968L-GLUTAMATE dehydrogenase from beef liver, GDH (EC 1.4.1.3), has a molecular weight of 310,000 (referred to as the oligomer) consisting of six identical subunits1 and six active sites2.
A. D. B. Malcolm, George K. Radda
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Folates as inhibitors of glutamate dehydrogenase
Biochimica et Biophysica Acta (BBA) - Enzymology, 1976Folates and tetrahydrofolates inhibit beef liver glutamate dehydrogenase (EC 1.4.1.2). Double reciprocal plats indicate a competitive inhibition for alpha-ketoglutarate-glutamate by folic acid and methotrexate and a complex or mixed type for NAD-NADH site. Pteroic acid is not inhibitory at the concentrations studied.
C.L. Krumdieck +2 more
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Alternative substrates for glutamate dehydrogenases
Biochemical and Biophysical Research Communications, 1975Summary The amide group of glutamine functions as a nitrogen donor in the reactions catalyzed by both the NADP-specific glutamate dehydrogenase of Neurospora crassa and the bovine liver enzyme, but not by the NAD-specific Neurospora enzyme. Asparagine serves as nitrogen source only for the NADP-specific Neurospora dehydrogenase.
Emil L. Smith, Kenneth M. Blumethal
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Chymotryptic activation of glutamate dehydrogenase
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983Treatment of bovine liver glutamate dehydrogenase (L-glutamate:NAD(P)+ oxidoreductase (deaminating), EC 1.4.1.3) with chymotrypsin generates a proteolytic derivative that is activated 3-4-fold over the native enzyme. Stable preparations of activated enzyme show altered kinetic parameters (5-fold increase in Km for glutamate, 3-fold increase in Vmax ...
Robert J. Beynon, Graham A. Place
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The Radiation Inactivation of Glutamate Dehydrogenase
Radiation Research, 1983Pulse 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
Radwan R. Abu El Failat +2 more
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1975
Publisher Summary This chapter discusses the types of investigations with major emphasis on recent studies that include elucidation of complete or partial amino acid sequences of the enzymes from several sources. L-Glutamate dehydrogenases catalyze the interconversion of α-ketoglutarate and L-glutamic acid.
Emil L. Smith +3 more
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Publisher Summary This chapter discusses the types of investigations with major emphasis on recent studies that include elucidation of complete or partial amino acid sequences of the enzymes from several sources. L-Glutamate dehydrogenases catalyze the interconversion of α-ketoglutarate and L-glutamic acid.
Emil L. Smith +3 more
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Bovine Liver Glutamate Dehydrogenase
1976Publisher Summary This chapter discusses the current ideas on the catalytic reaction of glutamate dehydrogenase, including its mechanism and regulation, substrate inhibition or activation, the binding of coenzymes to the enzyme, the effect of purine nucleotides, and the mechanism of ligand-induced structural changes.
Robert Josephs +2 more
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