EC Number   |
General Information |
Reference |
|---|
    1.1.1.41 | evolution |
efficacy of association mapping for dissecting natural variation in primary metabolic pathways, the considerable genetic diversity observed in maize CCM genes underlies heritable phenotypic variation in enzyme activities and can be useful to identify putative functional sites |
713380 |
| 1.1.1.41 | evolution |
evolutionary relationships of IDHs, overview |
-, 741414 |
| 1.1.1.41 | evolution |
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and is clustered into a unique clade among the type II subfamily |
-, 741414 |
| 1.1.1.41 | evolution |
evolutionary relationships of IDHs, overview. The enzyme belongs to the IDH enzyme family and the subclade of monomeric enzymes |
-, 741414 |
| 1.1.1.41 | evolution |
evolutionary relationships of IDHs, phylogenetic analysis, overview. The enzyme belongs to the IDH enzyme family and the subclade of type II homodimeric enzymes |
-, 741414 |
| 1.1.1.41 | evolution |
OtIDH may be an ancestral form of type II IDHs (all other reported members are NADP+-linked enzymes) and may have evolved into NADP+-dependent IDH for adaptation to the increased demand of NADPH under carbon starvation |
740425 |
| 1.1.1.41 | evolution |
phylogenetic analyses divide the IDH protein family into two subgroups: types I and II. Based on cofactor usage, IDHs are either NAD+-specific (NAD-IDH) or NADP+-specific (NADP-IDH). NADP-IDH evolved from NAD-IDH. Type I IDHs include NAD-IDHs and NADP-IDHs. Type II NAD-IDHs is identified from the marine bacterium Congregibacter litoralis KT71, i.e ClIDH. Evolutionary relationships between 151 IDHs from different organisms, overview |
-, 741236 |
| 1.1.1.41 | evolution |
the ancient NAD-dependent IDHs might be the underlying origin of phosphorylation mechanism used by their bacterial NADP-dependent homologues |
723607 |
| 1.1.1.41 | evolution |
the recombinant ZmIDH is mainly NAD+-dependent and its catalytic efficiency (kcat/Km) is relative low when compared to the prokaryotic NADP+-IDHs |
-, 722295 |
| 1.1.1.41 | malfunction |
IDH activity is increased in patients with prolonged cell phone daily use over 4 h/day. Its level correlates negatively with either the motility ratio percentages or the progressive motility percentages in the study groups. NAD+-IDH in human seminal plasma can be one of seminal plasma biomarkers reflecting the mitochondrial function of spermatozoa. Alteration of its level reflect the defective motility of sperms among some cases of cellular phone users |
740114 |
