1975
DOI: 10.1016/0005-2744(75)90304-6
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Glutamate dehydrogenase from Escherichia coli: Induction, purification and properties of the enzyme

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Cited by 60 publications
(37 citation statements)
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“…2 x 106, which is about 6-7 times greater than the molecular weight of the enzyme from many other bacterial sources. The molecular weight and physical properties of glutamate dehydrogenase from B. megaterium were similar to those of many bacterial glutamate dehydrogenases (Coulton & Kapoor, 1973;Johnson & Westlake, 1972;Veronese et al, 1975; Vol. 173 Sakamoto et al, 1975), whereas those of glutamate synthase were similar to the enzyme from E. coli (Mantsala & Zalkin, 1976a) and A. aerogenes (Trotta et al, 1974).…”
Section: Kinetic and Molecular Propertiesmentioning
confidence: 72%
“…2 x 106, which is about 6-7 times greater than the molecular weight of the enzyme from many other bacterial sources. The molecular weight and physical properties of glutamate dehydrogenase from B. megaterium were similar to those of many bacterial glutamate dehydrogenases (Coulton & Kapoor, 1973;Johnson & Westlake, 1972;Veronese et al, 1975; Vol. 173 Sakamoto et al, 1975), whereas those of glutamate synthase were similar to the enzyme from E. coli (Mantsala & Zalkin, 1976a) and A. aerogenes (Trotta et al, 1974).…”
Section: Kinetic and Molecular Propertiesmentioning
confidence: 72%
“…Hill coefficients (n H ) in the same experiments were 1.3 and 1.5 for the Gdh1p and Gdh3p enzyme, respectively. In this regard, hexameric glutamate dehydrogenases from other organisms are known to be allosteric enzymes activated by different molecules (AMP, ADP, GTP, ATP, NADP ϩ , succinate, aspartate, and asparagine) (33,(37)(38)(39). The effect of these compounds was assayed for the yeast NADP-GDH isoenzymes, but none of them behaved as an allosteric effector (data not shown).…”
Section: Nadp-gdh Purification From Mutant and Wild-typementioning
confidence: 98%
“…The reductive transfer of the glutamine amide group to the 2-position of 2-oxoglutarate, thereby forming two molecules of glutamate, is catalyzed by GOGAT. Both GDH and GOGAT of enterobacteria are specific for NADPH over NADH (18)(19)(20). Net glutamate production from 2-oxoglutarate can hereby be achieved not only by GDH alone but also by GS-GOGAT coupled together.…”
Section: Central Nitrogen Assimilation In a Nutshellmentioning
confidence: 99%
“…The monomer is encoded by the gdhA gene, which translates to a polypeptide of 447 amino acids (48.4 kDa) (57,58). So-called biosynthetic GDH catalyzes the reductive amination of 2-oxoglutarate to glutamate using NADPH as the single reducing agent (19,20). The production of glutamate is favored, since the apparent equilibrium constant for the biosynthetic reaction amounts to 2,850 mM Ϫ1 at an ionic strength (I) of 0 and a temperature of 27°C, although it decreases with increasing ionic strength to a value of 285 mM Ϫ1 at an I of 0.5 and goes down to 90 mM Ϫ1 at an I of 0.5 and a temperature of 37°C (59).…”
Section: Glutamate Dehydrogenasementioning
confidence: 99%
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