Enzymes
| UniProtKB help_outline | 38,274 proteins |
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- Name help_outline (6R)-NADPHX Identifier CHEBI:64077 Charge -4 Formula C21H28N7O18P3 InChIKeyhelp_outline SZKXTJUOKARGIY-MTKBYBFRSA-J SMILEShelp_outline NC(=O)C1=CN([C@H](O)CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](OP([O-])([O-])=O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (6S)-NADPHX Identifier CHEBI:64076 Charge -4 Formula C21H28N7O18P3 InChIKeyhelp_outline SZKXTJUOKARGIY-VPHRTNKSSA-J SMILEShelp_outline NC(=O)C1=CN([C@@H](O)CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](OP([O-])([O-])=O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:32227 | RHEA:32228 | RHEA:32229 | RHEA:32230 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair.
Marbaix A.Y., Noel G., Detroux A.M., Vertommen D., Van Schaftingen E., Linster C.L.
The reduced forms of NAD and NADP, two major nucleotides playing a central role in metabolism, are continuously damaged by enzymatic or heat-dependent hydration. We report the molecular identification of the eukaryotic dehydratase that repairs these nucleotides and show that this enzyme (Carkd in ... >> More
The reduced forms of NAD and NADP, two major nucleotides playing a central role in metabolism, are continuously damaged by enzymatic or heat-dependent hydration. We report the molecular identification of the eukaryotic dehydratase that repairs these nucleotides and show that this enzyme (Carkd in mammals, YKL151C in yeast) catalyzes the dehydration of the S form of NADHX and NADPHX, at the expense of ATP, which is converted to ADP. Surprisingly, the Escherichia coli homolog, YjeF, a bidomain protein, catalyzes a similar reaction, but using ADP instead of ATP. The latter reaction is ascribable to the C-terminal domain of YjeF. This represents an unprecedented example of orthologous enzymes using either ADP or ATP as phosphoryl donor. We also show that eukaryotic proteins homologous to the N-terminal domain of YjeF (apolipoprotein A-1-binding protein (AIBP) in mammals, YNL200C in yeast) catalyze the epimerization of the S and R forms of NAD(P)HX, thereby allowing, in conjunction with the energy-dependent dehydratase, the repair of both epimers of NAD(P)HX. Both enzymes are very widespread in eukaryotes, prokaryotes, and archaea, which together with the ADP dependence of the dehydratase in some species indicates the ancient origin of this repair system. << Less
J. Biol. Chem. 286:41246-41252(2011) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.