Results 251 to 260 of about 158,395 (286)

Glutamate dehydrogenase-malate dehydrogenase complex

Archives of Biochemistry and Biophysics, 1979
Abstract Kinetic and Sephadex gel filtration epxeriments indicate that in the presence of palmitoyl-CoA, glutamate dehydrogenase forms a complex with mitochondrial malate dehydrogenase. In this complex, palmitoyl-CoA is bound to glutamate dehydrogenase but is not bound to malate dehydrogenase.
L A, Fahien, E, Kmiotek, L, Smith
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Glutamate Dehydrogenase

2018
International ...
Tipton, K.F., Couée, Ivan
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Glutamate dehydrogenase of Tetrahymena

Biochimica et Biophysica Acta (BBA) - Enzymology, 1974
Abstract Glutamate dehydrogenase [ l -glutamate: NAD(P) oxidoreductase (deaminating), EC 1.4.1.3] located in the mitochondria and able to utilize NAD, NADP, NADH or NADPH as substrate, has been purified 67-fold from Tetrahymena pyriformis . The activity with the four pyridine nucleotide substrates was catalyzed by a single enzyme as indicated by the
A B, Hooper, K R, Terry, K D, Kemp
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Studies of Glutamate Dehydrogenase

European Journal of Biochemistry, 1973
Specific interaction between α‐NADH and glutamate dehydrogenase is demonstrated by difference spectroscopy, circular dichroism and fluorescence measurements. Quantitative binding studies in the preparative ultracentrifuge yield six identical α‐NADH binding sites per oligomer with a dissociation constant of 20 μM.
R, Koberstein, J, Krause, H, Sund
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Bovine Liver Glutamate Dehydrogenase

1976
Publisher 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.
H, Eisenberg, R, Josephs, E, Reisler
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Myocardial Glutamate Dehydrogenase Activity

1986
Glutamic dehydrogenase (GDH) has not been thought to play an important role in cardiac metabolism in the past. Aspartate aminotransferase was shown to mediate glutamate utilization by mitochondria and there was thought to be little GDH activity in heart mitochondria.1 However, the studies of Godinot et al showed that this enzyme could be purified from ...
H G, McDaniel, R L, Jenkins
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Allosteric Transitions of Glutamate Dehydrogenase

Nature, 1968
L-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, Malcolm, G K, Radda
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Kinetic mechanism of glutamate dehydrogenase

Biochemistry, 1980
Initial 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.
J E, Rife, W W, Cleland
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Chymotryptic activation of glutamate dehydrogenase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
Treatment 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 ...
G A, Place, R J, Beynon
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