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Information on EC 4.2.1.93 - ATP-dependent NAD(P)H-hydrate dehydratase
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EC Tree
4.2.1.93 ATP-dependent NAD(P)H-hydrate dehydrataseIUBMB Comments
Acts equally well on hydrated NADH and hydrated NADPH. NAD(P)H spontaneously hydrates to both the (6S)- and (6R)- isomers, and these are interconverted by EC 5.1.99.6, NAD(P)H-hydrate epimerase, to a 60:40 ratio . Hence EC 4.2.1.93 together with EC 5.1.99.6 can restore the mixture of hydrates into NAD(P)H [3,4]. The enzyme from eukaryotes has no activity with ADP, contrary to the enzyme from bacteria (cf. EC 4.2.1.136, ADP-dependent NAD(P)H-hydrate dehydratase) .
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Word Map
- 4.2.1.93
-
nadphx
-
epimerase
- dehydrogenases
-
salvage
- 5'-phosphate
-
apolipoprotein
-
epimer
- children
-
neurodegeneration
-
febrile
-
reconvert
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)-NAD(P)HX dehydratase
ADP/ATP-dependent NAD(P)H-hydrate dehydratase
At5g19150
ATP-dependent H4NAD(P)OH dehydratase
-
-
-
-
ATP-dependent NNRD
Carkd
NAD(P)HX dehydratase
NAD(P)X dehydratase
NAXD
NNRD
reduced nicotinamide adenine dinucleotide hydrate dehydratase
-
-
-
-
YKL151C
YxkO
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = ADP + phosphate + NADH
also acts on hydrated NADPH
-
-
-
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate = ADP + phosphate + NADPH
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C-O bond cleavage by elimination of water
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase (ATP-hydrolysing; NADH-forming)
Acts equally well on hydrated NADH and hydrated NADPH. NAD(P)H spontaneously hydrates to both the (6S)- and (6R)- isomers, and these are interconverted by EC 5.1.99.6, NAD(P)H-hydrate epimerase, to a 60:40 ratio [4]. Hence EC 4.2.1.93 together with EC 5.1.99.6 can restore the mixture of hydrates into NAD(P)H [3,4]. The enzyme from eukaryotes has no activity with ADP, contrary to the enzyme from bacteria (cf. EC 4.2.1.136, ADP-dependent NAD(P)H-hydrate dehydratase) [4].
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CAS REGISTRY NUMBER
COMMENTARY
116669-08-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
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
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
Saccharomyces cerevisiae ATCC 204508 / S288c
-
-
-
?
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
-
-
-
?
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
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
Saccharomyces cerevisiae ATCC 204508 / S288c
-
-
-
?
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
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
Saccharomyces cerevisiae ATCC 204508 / S288c
-
-
-
?
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
-
-
-
?
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
Saccharomyces cerevisiae ATCC 204508 / S288c
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
stereospecific for (S)-NAD(P)HX epimer
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
atp-dependent nad(p)h-hydrate dehydratase deficiency
NAD(P)HX repair deficiency causes central metabolic perturbations in yeast and human cells.
Dehydration
Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00069 - 0.00089
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
0.00086
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
pH 8.0, 22°C
0.00115
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
-
pH 8.0, 22°C
0.00069
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
-
pH 8.0, 22°C
0.00089
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
pH 8.0, 22°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.34 - 0.38
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
0.26
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
-
pH 8.0, 22°C
0.3
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
pH 8.0, 22°C
0.34
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
-
pH 8.0, 22°C
0.38
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
pH 8.0, 22°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
509 - 524
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
262
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
-
pH 8.0, 22°C
358
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
pH 8.0, 22°C
509
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
-
pH 8.0, 22°C
524
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
pH 8.0, 22°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
NNRD is restricted to seeds but appears to be dispensable during the normal Arabidopsis life cycle, NNRD accumulates in seeds
brenda
-
dry, main expression; NNRD is restricted to seeds but appears to be dispensable during the normal Arabidopsis life cycle, NNRD accumulates in seeds
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
import assays with purified pea (Pisum sativum) chloroplasts and mitochondria
brenda
-
; import assays with purified pea (Pisum sativum) chloroplasts and mitochondria
-
brenda
-
import assays with purified pea (Pisum sativum) chloroplasts and mitochondria
-
brenda
import assays with purified pea (Pisum sativum) chloroplasts and mitochondria
brenda
-
import assays with purified pea (Pisum sativum) chloroplasts and mitochondria
brenda
-
import assays with purified pea (Pisum sativum) chloroplasts and mitochondria
-
brenda
-
import assays with purified pea (Pisum sativum) chloroplasts and mitochondria
-
brenda
import assays with purified pea (Pisum sativum) chloroplasts and mitochondria
brenda
additional information
-
the enzyme is predominantly (if not exclusively) found in chloroplasts and mitochondria
-
brenda
additional information
NNRD has multiple locations, prediction of an N-terminal transit peptides for NNRD with a probability of mitochondrial and plastid localization for NNRD, the recombinant YFP-tagged enzyme from leaf mesophyll shows localization in cytosol, chloroplast stroma, and mitochondria, overview. NNRD is predominantly (if not exclusively) found in chloroplasts and mitochondria
-
brenda
additional information
-
NNRD has multiple locations, prediction of an N-terminal transit peptides for NNRD with a probability of mitochondrial and plastid localization for NNRD, the recombinant YFP-tagged enzyme from leaf mesophyll shows localization in cytosol, chloroplast stroma, and mitochondria, overview. NNRD is predominantly (if not exclusively) found in chloroplasts and mitochondria; the enzyme is predominantly (if not exclusively) found in chloroplasts and mitochondria
-
-
brenda
additional information
subcellular localization study of Myc-tagged enzyme, the Carkd gene encodes proteins with a predicted mitochondrial propeptide (mCARKD), a signal peptide (spCARKD) or neither of them (cCARKD)
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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
-
domain architectures of the NAD(P)HX dehydratase enzymes of prokaryotes, yeast, andmammals, and of dehydratase homologue in plants; 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
-
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
Saccharomyces cerevisiae ATCC 204508 / S288c
-
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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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 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
Saccharomyces cerevisiae ATCC 204508 / S288c
-
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
-
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
-
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 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
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 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
-
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; the enzyme is involved in the NAD(P)H repair pathway but is dispensable for growth and development under standard conditions; 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
-
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
Saccharomyces cerevisiae ATCC 204508 / S288c
-
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
-
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; homology models of the three-dimensional structures of NAD(P)X dehydratase and NAD(P)X epimerase
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Show AA Sequence and Transmembrane Helices (2071 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
132700
35701
-
4 * 35701, His-tagged enzyme, mass spectrometry, and gel filtration coupled to static light scattering
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 42000, glycosylated spCARKD, SDS-PAGE, x * 38000, deglycosylated spCARKD, SDS-PAGE
tetramer
tetramer
-
4 * 35701, His-tagged enzyme, mass spectrometry, and gel filtration coupled to static light scattering
tetramer
-
; 4 * 35701, His-tagged enzyme, mass spectrometry, and gel filtration coupled to static light scattering
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
spCARKD comprises two putative N-glycosylation sites at positions 236-238 (236NIT238) and 293-295 (293NGS295) in the mouse protein, deglycosylation by PNGase F
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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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
Saccharomyces cerevisiae ATCC 204508 / S288c
-
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from rat liver mitochondria by anion exchange chromatography, solubilization with 0.1% Triton X-100, desalting gel filtration, and Blue Trisacryl affinity chromatography
preparation of mesophyll protoplasts from stable Arabidopsis thaliana transfection lines recombinantly expressing the enzyme, isolation of mitochondria from transgenic seedlings or protoplasts, recombinant C-terminally His6-tagged enzyme from Escherichia coli by ncikel affinity chromatography. No copurification with coexpressed NNRE or PDX3
recombinant C-terminally His6-tagged from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
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recombinant Myc-His-tagged mCarkd from HEK-293T cells by affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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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)
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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recombinant expression as GFP-tagged enzyme in Nicotiana tabacum suspension cells, subcellular localization comprises cytosol, mitochondria, and chloroplasts
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
construction of cells deficient in the NAD(P)HX repair enzymes using HAP1 haploid cell lines and genetical modification by the CRISPR/Cas9 technology to disrupt the human homologue of the Saccharomyces cerevisiae YKL151C gene, NAXD. In the NAXD KO cell line, the mutated NAXD gene encodes a truncated protein containing the first 126 amino acids (out of the 329 amino acids of the native mitochondrial isoform) followed by nine non-native amino acids. Phenotype, detailed overview
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Arabidopsis thaliana, Arabidopsis thaliana (Q94AF2), Arabidopsis thaliana Col-0 (Q94AF2), Zea mays (A0A3L6F337), Zea mays
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
Mus musculus (Q9CZ42), Rattus norvegicus (D4AAT7)
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
Homo sapiens, Homo sapiens (Q8IW45), Saccharomyces cerevisiae (P36059), Saccharomyces cerevisiae, 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 168 (P94368), Bacillus subtilis, Bacillus subtilis (P94368)
brenda
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