Disease relevance of GLUD1

• NADH and glutamate are clearly observed in the active site, but the contacts differ slightly from those observed in Clostridium symbiosum GDH [1].
• The expression of the recombinant bovine brain GDH enzyme was achieved in E. coli [2].
• Selection, expression, and nucleotide sequencing of the glutamate dehydrogenase gene of Peptostreptococcus asaccharolyticus [3].
• It was concluded that glutamate dehydrogenase and gamma-glutamyl transpeptidase were the most sensitive indicators of liver cell damage in fascioliasis [4].
• Glutamate dehydrogenase in Reye's syndrome. Evidence for the presence of an altered enzyme in serum with increased susceptibility to inhibition by GTP [5].

High impact information on GLUD1

• Radiation inactivation of glutamate dehydrogenase hexamer: lack of energy transfer between subunits [6].
• The effects of ionizing radiation on glutamate dehydrogenase and on fluorescein isothiocyanate--tagged glutamate dehydrogenase were analyzed by target theory [6].
• Carbonyl oxygen exchange evidence of imine formation in the glutamate dehydrogenase reaction and identification of the "occult role" of NADPH [7].
• Partial amino-acid sequence of NAD-specific glutamate dehydrogenase of Neurospora crassa [8].
• Identification of an NAD+ binding site of brain glutamate dehydrogenase isoproteins by photoaffinity labeling [9].

Chemical compound and disease context of GLUD1

• Aspartate aminotransferase, glutamate dehydrogenase, gamma-glutamyl transferase and total bilirubin were elevated in the group with liver disease [10].
• In cattle treated with both trypanocides, weight loss and serum glutamate dehydrogenase levels were correlated with isometamidium concentrations [11].

Biological context of GLUD1

• Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme [12].
• A cDNA of bovine brain glutamate dehydrogenase (GDH) was isolated from a cDNA library by recombinant PCR [2].
• Glutamate dehydrogenase is found in all organisms and catalyses the oxidative deamination of l-glutamate to 2-oxoglutarate [13].
• This suggests that there was some selective advantage of the antenna itself and that animals evolved new functions for GDH through the addition of allosteric regulation [14].
• It is proposed that 5'-p-fluorosulfonylbenzoyl guanosine may be reacting within the allosteric GTP site of glutamate dehydrogenase and that this compound may have general applicability in the affinity labeling of regulatory and catalytic sites of proteins which normally bind guanosine nucleotides [15].

Anatomical context of GLUD1

• Because these are properties of glutamate dehydrogenase in mitochondria but not properties of the pure enzyme studied in the absence of Mg2+, Mg2+ could be a ligand that confers upon glutamate dehydrogenase the regulatory properties of this enzyme found in situ [16].
• A new carnitine palmitoyltransferase (CPT) was purified to homogeneity from bovine liver mitochondria which were 96% free of peroxisomal contamination, as judged by catalase and glutamate dehydrogenase activities [17].
• The results, obtained with different methods of tissue and antibody preparation, agree to show that the present form of glutamate dehydrogenase is restricted to mitochondria and preferentially localized in astrocytes [18].
• The interaction of phospholipid membranes and detergents with glutamate dehydrogenase [19].
• 1. The interaction of beef liver glutamate dehydrogenase with cardiolipin from both beef liver mitochondria and beef heart mitochondria, with phosphatidylcholine from both beef liver mitochondria and egg-yolk, and with beef brain phosphatidylserine was investigated by steady-state kinetic methods [20].

Associations of GLUD1 with chemical compounds

• Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation [13].
• However, only animal GDH utilizes both NAD(H) or NADP(H) with comparable efficacy and exhibits a complex pattern of allosteric inhibition by a wide variety of small molecules [13].
• Glutamate dehydrogenase (GDH) is found in all organisms and catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate [14].
• Nicotinamide adenine dinucleotide-specific glutamate dehydrogenase of Neurospora. IV. The COOH-terminal 669 residues of the peptide chain; comparison with other glutamate dehydrogenases [21].
• Effect of aspartate on complexes between glutamate dehydrogenase and various aminotransferases [22].

Other interactions of GLUD1

• The activities of serum aspartate aminotransferase (ASAT; p < 0.001), glutamate dehydrogenase (GLDH; p < 0.01) and gamma glutamyl transferase (gamma-GT; p < 0.01) increased with increasing OM intake and were not related to the mycotoxin contamination of the wheat [23].
• A bacterial glutamate-aspartate binding protein, as well as the enzymes glutamate dehydrogenase (EC 1.4.1.3), glutamine synthetase (EC 6.3.1.2), and gamma-glutamyl transpeptidase (EC 2.3.2.2), showed little or no cross-reactivity with the anti-GBP antibodies [24].
• Transferred nuclear Overhauser enhancement was used to examine the conformation of NAD+ and NADP+ bound to glucose-6-phosphate dehydrogenase and glutamate dehydrogenase and of NAD+ bound to lactate dehydrogenase [25].
• DPNH disrupts complexes with malate dehydrogenase and has little effect on those with the aminotransferase, while oxalacetate disrupts complexes with citrate synthase but has little effect on those with glutamate dehydrogenase [26].
• Cyanogen bromide and tryptic peptides of bovine nuclear and mitochondrial glutamate dehydrogenase were separated by HPLC reverse-phase chromatography using a linear gradient of 0-60% acetonitrile [27].

Analytical, diagnostic and therapeutic context of GLUD1

• The molecular mass of the expressed GDH enzyme was estimated as 50 kDa by SDS-PAGE and Western blot using monoclonal antibodies against bovine brain GDH [2].
• One binding protein was isolated by a simple ion exchange and gel filtration protocol and was shown by N-terminal protein sequence analysis to be glutamate dehydrogenase [28].
• The allosteric mechanism of bovine liver glutamate dehydrogenase. Evidence from circular-dichroism studies for a conformational change in the ternary complex enzyme-(oxidized nicotinamide-adenine dinucleotide)-glutarate [29].
• 1. A rapid procedure, involving ion-exchange chromatography on DEAE-cellulose and affinity chromatography on GTP-Sepharose, was used to purify glutamate dehydrogenase from ox brain and liver [30].
• 2. The circular dichroism of NAD+ bound to glutamate dehydrogenase is strongly negative at 260nm, probably owing to immobilization of the adenosine moiety [29].

References