Reference : Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotid...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/10993/13754
Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair
English
Marbaix, Alexandre Y. [> >]
Noël, Gaëtane []
Detroux, Aline M. [> >]
Vertommen, Didier [> >]
Van Schaftingen, Emile [> >]
Linster, Carole mailto [University of Luxembourg > Luxembourg Centre for Systems Biomedicine (LCSB) > >]
2-Dec-2011
Journal of Biological Chemistry
American Society for Biochemistry and Molecular Biology
286
48
41246-52
Yes (verified by ORBilu)
International
0021-9258
1083-351X
Baltimore
MD
[en] 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.
http://hdl.handle.net/10993/13754
10.1074/jbc.C111.310847

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