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Enzyme Nomenclature
Information on EC 4.2.1.93 - ATP-dependent NAD(P)H-hydrate dehydratase
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
4.2.1.93
-
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RECOMMENDED NAME
GeneOntology No.
ATP-dependent NAD(P)H-hydrate dehydratase
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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
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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
K7TRV3
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
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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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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
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
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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
K7TRV3
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 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
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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
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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
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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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
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
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
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
-
-
-
-
ir
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
K7TRV3
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
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
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Q94AF2
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
Q94AF2
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
K7TRV3
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
Q94AF2
stereospecific for (S)-NAD(P)HX epimer
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
Q94AF2
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
-
-
?
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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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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
K7TRV3
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
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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
K7TRV3
pH 8.0, 22°C
0.34
(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
K7TRV3
pH 8.0, 22°C
509
(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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
import assays with purified pea (Pisum sativum) chloroplasts and mitochondria
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; import assays with purified pea (Pisum sativum) chloroplasts and mitochondria
-
-
import assays with purified pea (Pisum sativum) chloroplasts and mitochondria
-
K7TRV3
import assays with purified pea (Pisum sativum) chloroplasts and mitochondria
-
import assays with purified pea (Pisum sativum) chloroplasts and mitochondria
-
; import assays with purified pea (Pisum sativum) chloroplasts and mitochondria
-
-
import assays with purified pea (Pisum sativum) chloroplasts and mitochondria
-
K7TRV3
import assays with purified pea (Pisum sativum) chloroplasts and mitochondria
additional information
-
the enzyme is predominantly (if not exclusively) found in chloroplasts and mitochondria
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additional information
-
the enzyme is predominantly (if not exclusively) found in chloroplasts and mitochondria
-
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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
35701
-
4 * 35701, His-tagged enzyme, mass spectrometry, and gel filtration coupled to static light scattering
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
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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LINKS TO OTHER DATABASES (specific for EC-Number 4.2.1.93)
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