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Information on EC 4.2.1.93 - ATP-dependent NAD(P)H-hydrate dehydratase and Organism(s) Rattus norvegicus and UniProt Accession D4AAT7

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.93 ATP-dependent NAD(P)H-hydrate dehydratase
IUBMB 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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This record set is specific for:
Rattus norvegicus
UNIPROT: D4AAT7
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Word Map
  • 4.2.1.93
  • nadphx
  • epimerase
  • dehydrogenases
  • febrile
  • salvage
  • neurometabolic
  • epimer
  • neurodevelopmental
  • neurodegeneration
  • protein-truncating
  • reconvert
  • apolipoprotein
  • 5'-phosphate
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
nad(p)hx dehydratase, ykl151c, carkd, atp-dependent nnrd, atp-dependent nad(p)h-hydrate dehydratase, adp/atp-dependent nad(p)h-hydrate dehydratase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NAD(P)HX dehydratase
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ATP-dependent H4NAD(P)OH dehydratase
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-
-
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reduced nicotinamide adenine dinucleotide hydrate dehydratase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-O bond cleavage by elimination of water
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-
-
-
PATHWAY SOURCE
PATHWAYS
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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].
CAS REGISTRY NUMBER
COMMENTARY hide
116669-08-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
show the reaction diagram
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-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
show the reaction diagram
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-
-
?
additional information
?
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NAD(P)HX dehydratase is specific for the (S)-epimer of NAD(P)HX
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
ADP + phosphate + NADH
show the reaction diagram
-
-
-
?
ATP + (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
ADP + phosphate + NADPH
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
dependent on
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
lowest enzyme content
Manually annotated by BRENDA team
highest enzyme content
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NNRD_RAT
343
1
36518
Swiss-Prot
Secretory Pathway (Reliability: 1)
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team