EC Number   |
General Information |
Reference |
|---|
   4.2.1.93 | evolution |
domain architectures of the NAD(P)HX dehydratase enzymes of prokaryotes, yeast, andmammals, and of dehydratase homologue in plants |
-, 728528 |
| 4.2.1.93 | evolution |
the enzyme belongs to the ribokinase superfamily |
-, 748172 |
| 4.2.1.93 | malfunction |
human cells deficient in the NAD(P)HX dehydratase accumulate NADHX and show decreased viability. In addition, those cells consume more glucose and produce more lactate than the wild-type, potentially indicating impaired mitochondrial function. NADHX accumulation affects cellular functions causing the rapid and severe neurodegeneration leading to early death in NADHX repair-deficient children |
747751 |
| 4.2.1.93 | malfunction |
NAD(P)HX dehydratase deficiency in yeast leads to an important, temperature-dependent NADHX accumulation in quiescent cells with a concomitant depletion of intracellular NAD+ and serine pools, (S)-, (R)-, and cyclic NADHX level increases in the enzyme-deficient ykl151cDELTA strain versus wild-type strain are all significant in postdiauxic phase, phenotype, detailed overview. Impact of intracellular NADHX accumulation on gene expression and amino acid levels in yeast, e.g. decreased CHA1 (a deaminase involved in serine and threonine catabolism) expression |
-, 747751 |
| 4.2.1.93 | malfunction |
the Bacillus subtilis168 osmosensitive mutant, defective in the yxkO gene, gene yxkO knockout phenotype, overview. Changes in the protein value caused by yxkO disruption are also recorded for GroEL. In the mutant, the increase of protein level occurred in non-stressed conditions, as well when compared to the wild-type due to extension of the lag phase and the decline of the renewing of isocitrate dehydrogenase levels in the mutant according to wild-type after stress exposure, which denotes to failure of stress adaptation and triggers increased levels of GroEL as a result of the devastating effects of both stresses on cellular proteins. Identification of differences in protein levels under osmotic stress and ethanol stress, overview |
-, 749142 |
| 4.2.1.93 | metabolism |
hydration of NAD(P)H to NAD(P)HX, which inhibits several dehydrogenases, is corrected by an ATP-dependent dehydratase and an epimerase recently identified as the products of the vertebrate Carkd (carbohydrate kinase domain) and Aibp (apolipoprotein AI-binding protein) genes respectively. The NAD(P)HX epimerase, encoded by the Aibp gene, catalyses the R to S epimerization of NAD(P)HX |
747020 |
| 4.2.1.93 | metabolism |
the metabolite repair system formed by the two enzymes NAD(P)HX dehydratase and NAD(P) HX epimerase allows reconversion of both the S- and R-epimers of NADHX and NADPHX to the normal cofactors. The NAD(P)HX dehydratase and epimerase are two members of a list of enzymes that have been recognized to participate in a process called metabolite repair or metabolite proofreading and in which a panoply of protective enzymatic activities are required to prevent the accumulation of noncanonical, potentially toxic metabolites that are formed continuously via enzymatic side reactions or spontaneous chemical reactions |
-, 747751 |
| 4.2.1.93 | metabolism |
the metabolite repair system formed by the two enzymes NAD(P)HX dehydratase and NAD(P)HX epimerase allows reconversion of both the S- and R-epimers of NADHX and NADPHX to the normal cofactors. The NAD(P)HX dehydratase and epimerase are two members of a list of enzymes that have been recognized to participate in a process called metabolite repair or metabolite proofreading and in which a panoply of protective enzymatic activities are required to prevent the accumulation of noncanonical, potentially toxic metabolites that are formed continuously via enzymatic side reactions or spontaneous chemical reactions |
747751 |
| 4.2.1.93 | metabolism |
the stereospecific dehydratase is involved in a potential NAD(P)H repair pathway in plants. Dehydratase NNRD and an epimerase (NNRE), fused to a vitamin B6 salvage enzyme, act concomitantly to restore NAD(P)HX to NAD(P)H, but the proteins do not physically interact |
-, 730041 |
| 4.2.1.93 | more |
Arabidopsis thaliana NNRD and NNRE function in non-stoichiometric oligomeric states. Homology models of the three-dimensional structure of NNRD from Arabidopsis thaliana |
-, 748172 |
