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Glutamate dehydrogenase properties

Inokuchi, R., Itagaki, T., Wiskich, J., Nakayama, K., and Okada, M. (1997). An NADP-glutamate dehydrogenase in the green alga Bryopsis maxima. Purification and properties. Plant Cell Physiol. 38, 327-335. [Pg.1435]

A related fluorescent nucleotide affinity label, 5 -p-fluorosulfonylbenzoyl-2-aza-1,7V -ethenoadenosine (5 -FSBaeA), in which a nitrogen replaces the carbon atom at the 2-position of 5 -FSBeA, has also been prepared (205, 206). 5 -FSBaeA has different spectral properties, with an emission peak at 490 nm and an excitation maximum at 356 nm. Thus, it can be used in a complementary manner to 5 -FSBeA as a covalently bound chromophore. 5 -FSBaeA reacts at a GTP regulatory site of glutamate dehydrogenase, and energy transfer experiments have led to an estimated distance between the catalytic and GTP sites in... [Pg.304]

With respect to amino acid metabolism some of the differences between host and parasite are somewhat subtle. Some parasite enzymes, for example, have properties which are clearly distinct from those of their mammalian counterparts, such as the cofactor dependence and regulation of glutamate dehydrogenases. The utilization of specific amino acids such as proline or the accumulation of others such as alanine reflects a difference in the relative importance of the pathways between parasite and host. Some differences are particularly striking, especially among anaerobic protozoa in... [Pg.83]

Analytical affinity chromatography of bovine 206 liver glutamate dehydrogenase and investigation of its ligand-binding properties Affinity chromatography of acetate kinase 207... [Pg.598]

Soluble copolymers of albumin and L-glutamate dehydrogenase have been prepared by glutaraldehyde cross-linking. The kinetic and electron microscopic properties of the soluble derivatives were compared with data available concerning the enzyme immobilized within proteic films. [Pg.651]

Matsuda et al. (27) showed that the adenylosuccinate synthetase basic isozyme has a lower Km for aspartate, is more sensitive to inhibition by fructose 1,6-bisphosphate, and less sensitive to inhibition by nucleotides than the acidic isozyme. These properties could indicate that the basic isozyme is regulated coordinately with glycolysis (or gluconeogenesis) as proposed for the operation of the purine nucleotide cycle in skeletal muscle. The enzyme could also be affected by the availability of aspartate, as was found in Ehrlich ascites cells. The increase in basic isozyme activity, under conditions used in this study where the animal must rely on protein for most of its energy, is consistent with the idea that it is involved in the purine nucleotide cycle. This probably is not as an alternative to glutamate dehydrogenase in urea synthesis but is simply in amino acid catabolism. The small... [Pg.128]

Ertan H. Some properties of glutamate dehydrogenase, utamine synthase and utamate synthase from Corynebacterium callunae. Arch Microbiol 1992 158 35-41. [Pg.467]

Glutamic dehydrogenase has been detected in bacteria, yeast, plants, and animal tissues. The enzyme has been purified extensively only from liver, and the properties of the ezyme from other sources are not known very precisely. It has been reported that glutamic dehydrogenase of plants requires DPN, while the enzyme of yeast and E. coli requires TPN. The mammalian enzyme uses both coenzymes. [Pg.294]

The reaction depends upon all of the components shown in equation (I). It has been proposed that an imino acid is an intermediate, but no evidence for the existence of such a compound has been reported. If a nonenzymatic reaction between ammonia and a-ketoglutarate were to form the true substrate, the apparent requirements for enzyme saturation should be equivalent for both compounds and the apparent requirement for each should depend on the concentration of the other, because the hypothetical imino acid would be formed in a second-order reaction of ammonia and the keto acid. Instead, a Km of 1.2 X 10 was found for a-ketoglutarate and 5.7 X 10 for NH4. Other Km values for this enzyme are 2 X 10 for glutamate, 2.5 X 10 for DPN, and 1.8 X 10 for DPNH. These values are influenced by ions in the medium and pH, and are not fixed properties of the enzyme. As with other enzymes that use both DPN and TPN, glutamic dehydrogenase also acts with desamino DPN and acetylpyridine DPN. [Pg.295]


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See also in sourсe #XX -- [ Pg.322 ]

See also in sourсe #XX -- [ Pg.322 ]

See also in sourсe #XX -- [ Pg.322 ]

See also in sourсe #XX -- [ Pg.885 ]




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