EC Number   |
General Information |
Reference |
|---|
    1.4.1.2 | evolution |
BpNADGDH gives over 65% identity scores with fungal NAD-dependent GDHs |
763046 |
| 1.4.1.2 | evolution |
GDHs are members of a superfamily of ELFV (Glu/Leu/Phe/Val) amino acid dehydrogenases and are subdivided into three subclasses, based on coenzyme specificity: NAD+-specific, NAD+/NADP+ dual-specific, and NADP+-specific. The mitochondrial AtGDH1 isozyme from Arabidopsis thaliana is NAD+-specific. Arabidopsis thaliana expresses three GDH isozymes (AtGDH1-3) targeted to mitochondria, of which AtGDH2 has an extra EF-hand motif and is stimulated by calcium, while AtGDH1's sensitivity to calcium is negligible. In vivo the AtGDH1-3 enzymes form homo- and heterohexamers of varied composition. Phylogenetic analysis of GDHs in plants. Plants have distinct isozymes of GDH that are either NAD or NADP-specific. NAD-specific GDHs are localized in mitochondria, whereas NADP-specific GDHs exist in chloroplasts. The sequence region 257-264 in AtGDH1 and AtGDH2, which directly precedes the EF-hand motif in AtGDH2 (residues 265-277), is the most altered region of AtGDH2 in comparison with AtGDH1 |
763098 |
| 1.4.1.2 | evolution |
in 39 wild isolates of Lactococcus lactis from raw milk cheeses, only 25% of the isolates are glutamate dehydrogenase positive with NAD+ as the preferred cofactor. Lactococcus lactis IFPL953 shows the highest NAD-GDH activity |
-, 762994 |
| 1.4.1.2 | evolution |
NAD+-dependent, NADP+-dependent and dual-specificity GDHs, EC 1.4.1.2-1.4.1.4 are closely related and a few site-directed mutations can reverse specificity, overview. Specificity for NAD+ or for NADP+ has probably emerged repeatedly during evolution, using different structural solutions on different occasions. an acidic P7 residue usually hydrogen bonds to the 2'- and 3'-hydroxyls, may permit binding of NAD+ only, NADP+ only, or in higher animals both |
726044 |
| 1.4.1.2 | evolution |
the enzyme belongs to the family of amino acid dehydrogenases |
724249 |
| 1.4.1.2 | malfunction |
a gdh1-2-3 triple mutant exhibits major differences to the wild-type in gene transcription and metabolite concentrations, and these differences appear to originate in the roots, metabolic profile of the gdh1-2-3 triple mutant, overview |
726164 |
| 1.4.1.2 | malfunction |
the disruption of GDH2 was not deleterious to glutamate homeostasis. Mutant gdh2DELTA cells present wild-type growth and do not display any deficiencies due to glutamate homeostasis impairment neither under glucose nor under non-fermentable carbon sources. Deletion of GDH2 gene in a gdh3DELTA background increases the resistance under thermal or oxidative stress by decreasing ROS accumulation. The apoptosis is suppressed by GDH2 deletion through the elevated levels of glutamate and glutathione present in the double mutant. Under the tested conditions, deletion of GDH2 compensates the depletion of intracellular glutamate and glutathione (GSH) followed by stress-induced apoptotic cell death reinforcing further the idea that Gdh2p is responsible only for glutamate catabolism and not its production |
-, 763438 |
| 1.4.1.2 | malfunction |
when one or two of the three root isoenzymes are missing from the mutants, the remaining isoenzymes compensate for this deficiency |
726245 |
| 1.4.1.2 | metabolism |
GDH contributes to Glu homeostasis and plays a significant role at the junction of carbon and nitrogen assimilation pathways |
763098 |
| 1.4.1.2 | metabolism |
NAD+-GDH plays an important role in nitrogen assimilation rather than glutamate catabolism, and is involved in the additional nitrogen assimilatory pathway via glutamate dehydrogenase, GDH. The specific activity of the deaminating NAD+-GDH reaction is mostly independent of nitrogen availability, overview, overview |
711601 |
