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Information on EC 5.1.99.6 - NAD(P)H-hydrate epimerase and Organism(s) Mus musculus and UniProt Accession Q8K4Z3

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EC Tree
     5 Isomerases
         5.1 Racemases and epimerases
             5.1.99 Acting on other compounds
                5.1.99.6 NAD(P)H-hydrate epimerase
IUBMB Comments
The enzyme can use either (R)-NADH-hydrate or (R)-NADPH-hydrate as a substrate. Its physiological role is to convert the (R) forms to the (S) forms, which could then be restored to active dinucleotides by EC 4.2.1.93, ATP-dependent NAD(P)H-hydrate dehydratase.
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This record set is specific for:
Mus musculus
UNIPROT: Q8K4Z3
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
apoa1bp, nad(p)hx epimerase, ynl200c, nad(p)h-hydrate epimerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NAD(P)HX epimerase
-
AIBP
-
-
apolipoprotein A-1-binding protein
-
-
NAD(P)HX epimerase
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(6R)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide 6-epimerase
The enzyme can use either (R)-NADH-hydrate or (R)-NADPH-hydrate as a substrate. Its physiological role is to convert the (R) forms to the (S) forms, which could then be restored to active dinucleotides by EC 4.2.1.93, ATP-dependent NAD(P)H-hydrate dehydratase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(6R)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
show the reaction diagram
i.e. NADHX
-
-
r
(6R)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
show the reaction diagram
i.e. NADPHX
-
-
r
(R)-NADH-hydrate
(S)-NADH-hydrate
show the reaction diagram
-
-
-
-
?
(R)-NADPH-hydrate
(S)-NADPH-hydrate
show the reaction diagram
-
higher catalytic efficiency with (R)-NADPH-hydrate compared to(R)-NADH-hydrate
-
-
?
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
(6R)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide
show the reaction diagram
i.e. NADHX
-
-
r
(6R)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
(6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate
show the reaction diagram
i.e. NADPHX
-
-
r
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NH4Cl
-
stimulatory effect on enzyme activity
additional information
-
NaCl does not affect activity up to a concentration of 5 mM
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0016
(R)-NADH-hydrate
-
in the presence of 5 mM KCl, at 30°C in 25 mM Tris-HCl, pH 8.0, 2 mM MgCl2, 0.2 mM ATP
0.00033
(R)-NADPH-hydrate
-
in the presence of 5 mM KCl, at 30°C in 25 mM Tris-HCl, pH 8.0, 2 mM MgCl2, 0.2 mM ATP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
82
(R)-NADH-hydrate
-
in the presence of 5 mM KCl, at 30°C in 25 mM Tris-HCl, pH 8.0, 2 mM MgCl2, 0.2 mM ATP
1827
(R)-NADPH-hydrate
-
in the presence of 5 mM KCl, at 30°C in 25 mM Tris-HCl, pH 8.0, 2 mM MgCl2, 0.2 mM ATP
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene Aibp
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NNRE_MOUSE
282
0
30973
Swiss-Prot
Mitochondrion (Reliability: 2)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+- or Co2+-charged column chromatography and Q-Sepharose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Aibp, expression of GFP-fused or Myc-tagged mAIBP in CHO cells and in HEK-293 cells, in vitro transcription-translation assays, full-length coding sequences of the mouse mAIBP
expressed in Escherichia coli BL21(DE3) cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Marbaix, A.; Nol, G.; Detroux, A.; Vertommen, D.; Van Schaftingen, E.; Linster, C.
Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide
J. Biol. Chem.
286
41246-41252
2011
Mus musculus, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Marbaix, A.Y.; Tyteca, D.; Niehaus, T.D.; Hanson, A.D.; Linster, C.L.; Van Schaftingen, E.
Occurrence and subcellular distribution of the NAD(P)HX repair system in mammals
Biochem. J.
460
49-58
2014
Homo sapiens (Q8NCW5), Mus musculus (Q8K4Z3), Rattus norvegicus (B0BNM1)
Manually annotated by BRENDA team