EC Number   |
General Information |
Reference |
|---|
    1.1.1.42 | evolution |
Arabidopsis thaliana has three NADP-ICDH genes At1g65930, At5g14590, and At1g54340, coding for the proteins NP_176768, NP_196963, and BT025983, respectively, that are located in different subcellular compartments, i.e. cytosol, chloroplasts, mitochondria, and peroxisomes |
-, 741388 |
| 1.1.1.42 | evolution |
based on the phylogenetic analysis, IDHs can be divided into three subfamilies: Type I IDHs, Type II IDHs and monomeric IDHs. The enzyme BlIDH from Bifidobacterium longum belongs to the type II subfamily. NAD+ use is an ancestral trait and NADP+ use by bacterial IDHs arose on or about the time that eukaryotic mitochondria first appeared, some 3.5 billion years ago |
-, 740551 |
| 1.1.1.42 | evolution |
phylogenetic analysis and evolutionary relationships between YlIDP and IDPs from other yeasts or yeast-related species |
-, 739874 |
| 1.1.1.42 | evolution |
the overall fold of the enzyme protein is resolved into large domain, small domain and a clasp domain. The monomeric structure reveals also a terminal domain involved in dimerization, a very unique domain when compared to other IDHs. The small domain and clasp domain show significant differences when compared to other IDHs of the same subfamily. The structure of TtIDH reveals the absence of helix at the clasp domain, which is mainly involved in oligomerization in other IDHs. Also, helices/beta sheets are absent in the small domain, when compared to other IDHs of the same subfamily. The overall TtIDH structure exhibits a closed conformation with the conserved catalytic triad residues Tyr144, Asp248, and Lys191. Oligomerization of the protein is determined using interface area and subunitsubunit interactions between protomers. The TtIDH structure with the terminal domain may be categorized as a first structure of a type IV subfamily |
739990 |
| 1.1.1.42 | evolution |
three NADP+-dependent isocitrate dehydrogenase (IDH) isozymes of a psychrophilic bacterium, Colwellia psychrerythraea strain 34H, are analyzed: two monomeric (IDH-IIa and IDH-IIb) and one dimeric (IDH-I) IDHs |
-, 740185 |
| 1.1.1.42 | malfunction |
autophagic response to ionizing radiation in A-172 glioma cells transfected with small interfering RNA (siRNA) targeting the IDPm gene. Autophagy in A-172 transfectant cells is associated with enhanced autophagolysosome formation and GFP-LC3 punctuation/aggregation. The inhibition of autophagy by chloroquine augments apoptotic cell death of irradiated A-172 cells transfected with IDPm siRNA. The activity of cytosolic NADP+-dependent isocitrate dehydrogenase (IDPc) is not affected by the transfection of IDPm siRNA. The decreased activity caused by knockdown of IDPm siRNA is also observed in U87MG glioma cell line. When cultured A172 cells are treated with gamma-radiation, an increase in cell death is observed, but A172 cells transfected with IDPm siRNA are significantly more sensitive than control cells in this respect |
739984 |
| 1.1.1.42 | malfunction |
enzyme deficiency increases cisplatin-induced oxidative damage in kidney tubule cells, inducing more severe nephrotoxicity |
760832 |
| 1.1.1.42 | malfunction |
enzyme knockout mice are more susceptible to high fat diet-induced obesity than wild type mice.Brown adipose tissue dysfunction in the enzyme knockout mice is due to mitochondrial dysfunction |
761047 |
| 1.1.1.42 | malfunction |
mitochondrial NADP+-dependent isocitrate dehydrogenase deficiency exacerbates mitochondrial and cell damage after kidney ischemia-reperfusion injury, Idh2 gene deletion exacerbates ROS production and oxidative stress after ischemia-reperfusion, and causes I/R-induced mitochondrial dysfunction and morphologic fragmentation, resulting in severe apoptosis in kidney tubule cells, it impairs reduction of NADP+ and GSSG within mitochondria |
-, 740583 |
| 1.1.1.42 | malfunction |
transfection of H9c2 clonal myoblastic cells with small interfering RNA (siRNA) specific for IDPm markedly attenuates IDPm expression and substantially induces apoptosis, senescence, and hypertrophy as indicated by increased atrial natriuretic peptide gene expression, a marker of cardiomyocyte hypertrophy, and a larger cell size. Knockdown of IDPm expression results in the modulation of cellular and mitochondrial redox status, mitochondrial function, and cellular oxidative damage. The suppression of IDP expression by siRNA induces apoptosis and hypertrophy of cultured cardiomyocytes through the disruption of cellular redox balance. IDPm knockdown alters cellular redox status and induces oxidative damage. Apoptosis induced by IDPm knockdown is ROS-mediated. Substantially increased desmin and vimentin abundance is observed in IDPm siRNA-transfected H9c2 cells compared to the control cells. Mitochondrial fission and fusion involve enzymatic reactions mediated by large dynamin-associated GTPases. IDPm knockdown induces mitochondrial damage by altering the redox status |
740117 |
