Disease relevance of gdhA

• Evaluation of cysteine 283 and glutamic acid 284 in the coenzyme binding site of Salmonella typhimurium glutamate dehydrogenase by site-directed mutagenesis and reaction with the nucleotide analogue 2-[4-bromo-2,3-dioxobutyl)thio)-1,N6-ethenoadenosine 2',5'-bisphosphate [1].
• Purification and properties of glutamate synthase and glutamate dehydrogenase from Bacillus megaterium [2].
• Purification and properties of NADP-dependent glutamate dehydrogenase from Ruminococcus flavefaciens FD-1 [3].
• The glutamate dehydrogenase structural gene of Escherichia coli [4].

High impact information on gdhA

• 840000 and 270000 for glutamate synthase and glutamate dehydrogenase respectively [2].
• Glutamate synthase contained NH3-dependent activity (different from authentic glutamate dehydrogenase), which was enhanced 4-fold during treatment at pH 4.6 NH3-dependent activity was generally about 2% of the glutamine-dependent activity [2].
• The argP mutation, but not the glnE mutation, was associated with reduced glutamate dehydrogenase activity and a concomitant NH4+ assimilation defect in the gltBD strain [5].
• Truncated NAC polypeptides, generated by the introduction of stop codons within the nac open reading frame, were tested for the ability to activate hut and repress gdh in vivo [6].
• The first residue in the N-terminal amino acid sequence from R. flavefaciens GDH was alanine, suggesting that the protein may be modified posttranslationally [3].

Biological context of gdhA

• One pathway involves the NADP-linked glutamate dehydrogenase, which catalyzes the amination of 2-oxoglutarate to form glutamate [7].

Associations of gdhA with chemical compounds

• The binding of glutamate dehydrogenase isolated from halobacterium of the Dead Sea on a column of Sepharose linked to this NADP+ derivative could be drastically enhanced by addition of sulfate (1M) and provided a tool for partially purifying the enzyme from a crude extract [8].

References