L-Glutamate dehydrogenase

L-glutamate dehydrogenase L-glutamate test for citric acid cycle... 

Transamination channels a-amino acid nitrogen into glutamate. L-Glutamate dehydrogenase (GDH) occupies a central position in nitrogen metabolism. 

L)-Phosphinotricin 67, which is the active component of naturally occurring antibiotic biolaphos, was synthesized from the corresponding keto acid 66 via reductive amination catalysed by L-glutamate dehydrogenase (EDH) (Equation 32)7 ... 

Terms in bold are defined in aminotransferases 660 transaminases 660 transamination 660 pyridoxal phosphate (PLP) 660 oxidative deamination 661 l-glutamate dehydrogenase 661 glutamine synthetase 662 glutaminase 663 creatine kinase 664... 

Glutamate can also be formed in yet another, albeit minor, pathway the reaction of a-ketoglutarate and NH4 to form glutamate in one step. This is catalyzed by L-glutamate dehydrogenase, an enzyme present in all organisms. Reducing power is furnished by NADPH ... 

Alvarez-Crespo et al. [69] L-Glutamate Chicken bouillon cubes L-Glutamate dehydrogenase/ entrapped in carbon paste NAD+ modified carbon paste electrode/+0.15 V vs. Ag/ AgCl o-Phenylenediamine polymerised on the electrode surface... 

The electroenzymatic reduction of NAD+ was successfully coupled with a synthesis reaction [122]. Hydrogenase from A. eutrophus was applied to regenerate NADH electrochemically during the transformation of a-ketoglutarate into L-glutamate catalyzed by an L-glutamate dehydrogenase (Fig. 27). 

BSA monomer, ovalbumin (chicken), P-lactoglobulin (bovine milk), serum albumin (human), carbonic anhydrase (bovine), L-glutamic dehydrogenase (bovine liver), a-chymotrypsin (bovine), a-chymotrypsinogen A (bovine), immunoglobulin (bovine milk), pepsin, trypsin (bovine), and heparin were from Sigma. RNase and lysozyme (egg white) were from Calbiochem. The recombinant human basic fibroblast... 

Figure 5. Methyl viologen-mediated electroreductive amination of a-ketoglutarate using ferre-doxin-NADP-reductase (FNR) as the regeneration enzyme and L-glutamate dehydrogenase (l-GluDH) as the production enzyme [35].

Figure 11. Hydrogenase-catalyzed NADH regeneration coupled to the reductive amination of a-ketoglutarate to L-glutmate catalyzed by L-glutamate dehydrogenase.

L-Glutamate Dehydrogenase Origin bovine liver Roche Diagnostics L-Glutamate Dehydrogenase (G1DH), lyo. 

M36. Murachi, T., and Tabata, M., Use of a bio-reactor consisting of sequentially aligned L-glutamate dehydrogenase and L-glutamate oxidase for the determination of ammonia by chemiluminescence. Biotechnol. Appl. Biochem. 9, 303-309 (1987). 

L-Glutamate dehydrogenases (EC 1.4.1.2-4) catalyze the interconversion of a-ketoglutarate and L-glutamic acid ... 

Enzyme Concentration and Purification. The number of existing enzymes is estimated to be more than 10,000 of which more than 100 have been purified in crystalline form and over 600 in fairly purified form. The molecular weight of enzymes varies from 12,700 (ribonuclease) to over 1,000,000 (L-glutamate dehydrogenase, d-carboxylase). All enzymes are proteins, conjugated proteins or metalloproteins containing one or more active sites per molecule. 

This behavior is not surprising in that many investigators have detected photoeffects under conventional spectrofluorometric conditions. Studies conducted on the UV-irradiation of lysozyme (13) and L-glutamate dehydrogenase (14) revealed a concomitant loss in enzyme activity and fluorescence emission with irradiation time. The primary photoeffects were destruc-... 

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. 

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