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ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
additional information
?
-
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
-
ir
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
stereospecific for (S)-NAD(P)HX epimer
-
-
?
additional information
?
-
the dehydratase is stereospecific and only uses (S)-NADHX. Coupled enzyme assay with the NADHX epimerase from Arabidopsis thaliana
-
-
?
additional information
?
-
the dehydratase is stereospecific and only uses (S)-NADHX. Coupled enzyme assay with the NADHX epimerase from Arabidopsis thaliana
-
-
?
additional information
?
-
NAD(P)HX dehydratase is specific for the (S)-epimer of NAD(P)HX
-
-
?
additional information
?
-
NAD(P)HX dehydratase is specific for the (S)-epimer of NAD(P)HX
-
-
?
additional information
?
-
-
no reaction occurs in absence of ATP, AMP is completely inactive, with ADP an initial lag period is observed, but the reaction then proceeds to completion, ADP appears to be active as source of ATP
-
-
?
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ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
stereospecific for (S)-NAD(P)HX epimer
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
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
the enzyme belongs to the ribokinase superfamily
evolution
-
the enzyme belongs to the ribokinase superfamily
-
evolution
-
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
-
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
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
-
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
-
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
-
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
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
-
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 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
-
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
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
-
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
-
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
-
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 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
-
additional information
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
-
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
-
homology models of the three-dimensional structures of NAD(P)X dehydratase and NAD(P)X epimerase
-
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additional information
the nnrd-1 mutant line GK-104E02, phenotype, overview. NNRD is dispensable for growth and development under standard conditions
additional information
-
the nnrd-1 mutant line GK-104E02, phenotype, overview. NNRD is dispensable for growth and development under standard conditions
-
additional information
construction of a Bacillus subtilis168 yxkO gene knockout mutant encoding a metabolite repair enzyme, transfer of the insertional mutation of the mini-Tn10 transposon to the yxkO gene from an asporogenic genetic background from a previously prepared mutant, for inactivation of the yxkO gene, an integrative vector pMUTIN4 is used. Analysis of gene yxkO knockout phenotype, overview
additional information
-
construction of a Bacillus subtilis168 yxkO gene knockout mutant encoding a metabolite repair enzyme, transfer of the insertional mutation of the mini-Tn10 transposon to the yxkO gene from an asporogenic genetic background from a previously prepared mutant, for inactivation of the yxkO gene, an integrative vector pMUTIN4 is used. Analysis of gene yxkO knockout phenotype, overview
additional information
-
construction of a Bacillus subtilis168 yxkO gene knockout mutant encoding a metabolite repair enzyme, transfer of the insertional mutation of the mini-Tn10 transposon to the yxkO gene from an asporogenic genetic background from a previously prepared mutant, for inactivation of the yxkO gene, an integrative vector pMUTIN4 is used. Analysis of gene yxkO knockout phenotype, overview
-
additional information
generation of an enzyme-deficient ykl151cDELTA mutant strain. In strains deleted for the YKL151C gene, concentrations of (S)-, (R)-, and cyclic NADHX are significantly increased. NAD(P)HX dehydratase deficiency leads to NAD(P)HX accumulation and NAD+ depletion in yeast, which is increased at higher gorwth temepratrure of 37°C compared to 25°C, no increase of the NADHX levels is observed in the wild-type cells at 37°C, phenotype, detailed overview. Analysis of significantly changed genes with most different expression levels between wild-type and ykl151cD strains
additional information
-
generation of an enzyme-deficient ykl151cDELTA mutant strain. In strains deleted for the YKL151C gene, concentrations of (S)-, (R)-, and cyclic NADHX are significantly increased. NAD(P)HX dehydratase deficiency leads to NAD(P)HX accumulation and NAD+ depletion in yeast, which is increased at higher gorwth temepratrure of 37°C compared to 25°C, no increase of the NADHX levels is observed in the wild-type cells at 37°C, phenotype, detailed overview. Analysis of significantly changed genes with most different expression levels between wild-type and ykl151cD strains
additional information
-
generation of an enzyme-deficient ykl151cDELTA mutant strain. In strains deleted for the YKL151C gene, concentrations of (S)-, (R)-, and cyclic NADHX are significantly increased. NAD(P)HX dehydratase deficiency leads to NAD(P)HX accumulation and NAD+ depletion in yeast, which is increased at higher gorwth temepratrure of 37°C compared to 25°C, no increase of the NADHX levels is observed in the wild-type cells at 37°C, phenotype, detailed overview. Analysis of significantly changed genes with most different expression levels between wild-type and ykl151cD strains
-
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gene At5g19150, sequence comparisons, functional recombinant expression of YFP-tagged enzyme in wild-type Arabidopsis thaliana leaf mesophyll via Agrobacterium tumefaciens strain C58 transformation, enzyme expression analyses, functional recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli, coexpression with NNRE or PDX3
gene At5g19150, sequence comparisons, recombinant expression of C-terminally His6-tagged in Escherichia coli strain BL21(DE3), expression of YFP-tagged enzyme in Arabidopsis thaliana cells
gene Carkd, recombinant expression of Myc-His-tagged mitochondrial isozyme mCarkd, the enzyme contains a mitochondrial propeptide, in HEK-293T cells, the recombinant enzyme is not secreted (not due to dysfunction of the HEK-293T cells)
gene NAXD, expression analysis
gene YKL151C, located on chromosome 11, expression analysis
recombinant expression as GFP-tagged enzyme in Nicotiana tabacum suspension cells, subcellular localization comprises cytosol, mitochondria, and chloroplasts
recombinant expression as GFP-tagged enzyme in Nicotiana tabacum suspension cells, subcellular localization comprises cytosol, mitochondria, and chloroplasts
recombinant expression as GFP-tagged enzyme in Nicotiana tabacum suspension cells, subcellular localization comprises cytosol, mitochondria, and chloroplasts
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Meinhart, J.O.; Chaykin, S.; Krebs, E.G.
Enzymatic conversion of a reduced diphosphopyridine nucleotide derivative to reduced diphosphopyridine nucleotide
J. Biol. Chem.
220
821-829
1956
Saccharomyces cerevisiae
brenda
Acheson, S.A.; Kirkman, H.N.; Wolfenden, R.
Equilibrium of 5,6-hydration of NADH and mechanism of ATP-dependent dehydration
Biochemistry
27
7371-7375
1988
Saccharomyces cerevisiae
brenda
Niehaus, T.D.; Richardson, L.G.; Gidda, S.K.; Elbadawi-Sidhu, M.; Meissen, J.K.; Mullen, R.T.; Fiehn, O.; Hanson, A.D.
Plants utilize a highly conserved system for repair of NADH and NADPH hydrates
Plant Physiol.
165
52-61
2014
Zea mays (A0A3L6F337), Zea mays, Arabidopsis thaliana (Q94AF2), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q94AF2)
brenda
Colinas, M.; Shaw, H.; Loubery, S.; Kaufmann, M.; Moulin, M.; Fitzpatrick, T.
A pathway for repair of NAD(P)H in plants
J. Biol. Chem.
289
14692-14706
2014
Arabidopsis thaliana (Q94AF2), Arabidopsis thaliana Col-0 (Q94AF2)
brenda
Marbaix, A.Y.; Tyteca, D.; Niehaus, T.D.; Hanson, A.D.; Linster, C.L.; Van Schaftingen, E.
Occurrence and subcellular distribution of the NADPHX repair system in mammals
Biochem. J.
460
49-58
2014
Rattus norvegicus (D4AAT7), Mus musculus (Q9CZ42)
brenda
Becker-Kettern, J.; Paczia, N.; Conrotte, J.F.; Zhu, C.; Fiehn, O.; Jung, P.P.; Steinmetz, L.M.; Linster, C.L.
NAD(P)HX repair deficiency causes central metabolic perturbations in yeast and human cells
FEBS J.
285
3376-3401
2018
Saccharomyces cerevisiae (P36059), Saccharomyces cerevisiae, Homo sapiens (Q8IW45), Homo sapiens, Saccharomyces cerevisiae ATCC 204508 / S288c (P36059)
brenda
Colinas, M.; Shaw, H.; Loubery, S.; Kaufmann, M.; Moulin, M.; Fitzpatrick, T.
A pathway for repair of NAD(P)H in plants
J. Biol. Chem.
289
14692-14706
2014
Arabidopsis thaliana (Q94AF2), Arabidopsis thaliana Col-0 (Q94AF2)
brenda
Petrovova, M.; Tkadlec, J.; Dvoracek, L.; Streitova, E.; Licha, I.
NAD(P)H-hydrate dehydratase - a metabolic repair enzyme and its role in Bacillus subtilis stress adaptation
PLoS ONE
9
e112590
2014
Bacillus subtilis (P94368), Bacillus subtilis, Bacillus subtilis 168 (P94368)
brenda