4.2.1.93: ATP-dependent NAD(P)H-hydrate dehydratase
This is an abbreviated version!
For detailed information about ATP-dependent NAD(P)H-hydrate dehydratase, go to the full flat file.
Word Map on EC 4.2.1.93
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4.2.1.93
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nadphx
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epimerase
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dehydrogenases
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febrile
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salvage
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neurometabolic
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epimer
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neurodevelopmental
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neurodegeneration
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protein-truncating
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reconvert
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apolipoprotein
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5'-phosphate
- 4.2.1.93
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nadphx
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epimerase
- dehydrogenases
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febrile
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salvage
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neurometabolic
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epimer
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neurodevelopmental
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neurodegeneration
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protein-truncating
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reconvert
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apolipoprotein
- 5'-phosphate
Reaction
Synonyms
(S)-NAD(P)HX dehydratase, ADP-dependent (S)-NAD(P)H-hydrate dehydratase, ADP/ATP-dependent NAD(P)H-hydrate dehydratase, At5g19150, ATP-dependent H4NAD(P)OH dehydratase, ATP-dependent NNRD, BSU38720, Carkd, More, NAD(P)H-hydrate dehydratase, NAD(P)HX dehydratase, NAD(P)X dehydratase, NAXD, NNRD, reduced nicotinamide adenine dinucleotide hydrate dehydratase, YKL151C, YxkO
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General Information
General Information on EC 4.2.1.93 - ATP-dependent NAD(P)H-hydrate dehydratase
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evolution
malfunction
metabolism
physiological function
additional information
domain architectures of the NAD(P)HX dehydratase enzymes of prokaryotes, yeast, andmammals, and of dehydratase homologue in plants
evolution
domain architectures of the NAD(P)HX dehydratase enzymes of prokaryotes, yeast, andmammals, and of dehydratase homologue in plants
evolution
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domain architectures of the NAD(P)HX dehydratase enzymes of prokaryotes, yeast, andmammals, and of dehydratase homologue in plants
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evolution
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domain architectures of the NAD(P)HX dehydratase enzymes of prokaryotes, yeast, andmammals, and of dehydratase homologue in plants
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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
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
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
malfunction
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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
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malfunction
Saccharomyces cerevisiae ATCC 204508 / S288c
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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
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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
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
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
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
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
metabolism
Saccharomyces cerevisiae ATCC 204508 / S288c
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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
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metabolism
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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
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the enzyme is involved in the NAD(P)H repair pathway but is dispensable for growth and development under standard conditions
physiological function
the enzyme is part of a canonical two-enzyme NAD(P)HX repair system that is directed to three subcellular compartments via the use of alternative translation start sites
physiological function
the enzyme is part of a canonical two-enzyme NAD(P)HX repair system that is directed to three subcellular compartments via the use of alternative translation start sites
physiological function
a stereospecific dehydratase (NNRD) and an epimerase (NNRE) constitute the NAD(P)H repair pathway and demonstrate their activity as NAD(P)HX repair enzymes. the ATP-dependent NNRD and NNRE act concomitantly to restore NAD(P)HX to NAD(P)H, but the proteins do not physically interact. The epimerase acts in conjunction with the dehydratase converting (R)-NAD(P)HX into (S)-NAD(P)HX. Whereas NNRE is present ubiquitously, NNRD is restricted to seeds but appears to be dispensable during the normal Arabidopsis life cycle
physiological function
the enzyme is part of the NADPHX repair system catalyzing hydration of inhibitory NAD(P)HX to the enzyme cofactor NAD(P)H
physiological function
the enzyme is part of the NADPHX repair system catalyzing hydration of inhibitory NAD(P)HX to the enzyme cofactor NAD(P)H
physiological function
the NAD(P)HX repair system has a role in preserving active forms of the central cofactors NAD and NADP and/or preventing accumulation of toxic derivatives thereof. NADHX and NADPHX are hydrated and redox inactive forms of the NADH and NADPH cofactors, known to inhibit several dehydrogenases in vitro
physiological function
the NAD(P)HX repair system has a role in preserving active forms of the central cofactors NAD and NADP and/or preventing accumulation of toxic derivatives thereof. NADHX and NADPHX are hydrated and redox inactive forms of the NADH and NADPH cofactors, known to inhibit several dehydrogenases in vitro. NADHX potently inhibits the first step of the serine synthesis pathway in yeast. A metabolite repair system that is conserved in all domains of life and that comprises 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
physiological function
the regulatory adaptive system called general stress response (GSR) is dependent on the SigB transcription factor in Bacillus sp.. The GSR is one of the largest regulon in Bacillus sp., including about 100 genes. The yxkO gene (encoding a putative ribokinase) is recently assigned in vitro as an ADP/ATP-dependent NAD(P)H-hydrate dehydratase and belongs to the SigB operon. YxkO has an impact on the activity of SigB-dependent Pctc promoter and adaptation to osmotic and ethanol stress and potassium limitation respectively. The enzyme might play a significant role in the survival of stressed cells
physiological function
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the regulatory adaptive system called general stress response (GSR) is dependent on the SigB transcription factor in Bacillus sp.. The GSR is one of the largest regulon in Bacillus sp., including about 100 genes. The yxkO gene (encoding a putative ribokinase) is recently assigned in vitro as an ADP/ATP-dependent NAD(P)H-hydrate dehydratase and belongs to the SigB operon. YxkO has an impact on the activity of SigB-dependent Pctc promoter and adaptation to osmotic and ethanol stress and potassium limitation respectively. The enzyme might play a significant role in the survival of stressed cells
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physiological function
Saccharomyces cerevisiae ATCC 204508 / S288c
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the NAD(P)HX repair system has a role in preserving active forms of the central cofactors NAD and NADP and/or preventing accumulation of toxic derivatives thereof. NADHX and NADPHX are hydrated and redox inactive forms of the NADH and NADPH cofactors, known to inhibit several dehydrogenases in vitro. NADHX potently inhibits the first step of the serine synthesis pathway in yeast. A metabolite repair system that is conserved in all domains of life and that comprises 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
-
physiological function
-
a stereospecific dehydratase (NNRD) and an epimerase (NNRE) constitute the NAD(P)H repair pathway and demonstrate their activity as NAD(P)HX repair enzymes. the ATP-dependent NNRD and NNRE act concomitantly to restore NAD(P)HX to NAD(P)H, but the proteins do not physically interact. The epimerase acts in conjunction with the dehydratase converting (R)-NAD(P)HX into (S)-NAD(P)HX. Whereas NNRE is present ubiquitously, NNRD is restricted to seeds but appears to be dispensable during the normal Arabidopsis life cycle
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physiological function
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the enzyme is part of a canonical two-enzyme NAD(P)HX repair system that is directed to three subcellular compartments via the use of alternative translation start sites
-
physiological function
-
the enzyme is involved in the NAD(P)H repair pathway but is dispensable for growth and development under standard conditions
-
physiological function
-
the enzyme is part of a canonical two-enzyme NAD(P)HX repair system that is directed to three subcellular compartments via the use of alternative translation start sites
-
homology models of the three-dimensional structures of NAD(P)X dehydratase and NAD(P)X epimerase
additional information
Arabidopsis thaliana NNRD and NNRE function in non-stoichiometric oligomeric states. Homology models of the three-dimensional structure of NNRD from Arabidopsis thaliana
additional information
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Arabidopsis thaliana NNRD and NNRE function in non-stoichiometric oligomeric states. Homology models of the three-dimensional structure of NNRD from Arabidopsis thaliana
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additional information
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homology models of the three-dimensional structures of NAD(P)X dehydratase and NAD(P)X epimerase
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