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Information on EC 3.6.1.22 - NAD+ diphosphatase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P53164

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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.22 NAD+ diphosphatase
IUBMB Comments
This enzyme, described from plants, animals, and bacteria, can act on both reduced and oxidized forms of its substrate, although enzymes from different organisms have different preferences. Also acts on other dinucleotides, including NADP(H), FAD(H2), and the thionicotinamide analogues of NAD+ and NADP+.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P53164
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
alkaline phosphodiesterase i, nadh pyrophosphatase, nad pyrophosphatase, atnudx19, nudx19, nad+ pyrophosphatase, nadph pyrophosphohydrolase, nudix hydrolase 19, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NAD diphosphatase
-
-
-
-
NAD pyrophosphatase
-
-
-
-
NAD+ diphosphatase
-
-
-
-
NAD+ pyrophosphatase
-
-
-
-
NADH pyrophosphatase
-
-
-
-
NADP pyrophosphatase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
NAD+ phosphohydrolase
This enzyme, described from plants, animals, and bacteria, can act on both reduced and oxidized forms of its substrate, although enzymes from different organisms have different preferences. Also acts on other dinucleotides, including NADP(H), FAD(H2), and the thionicotinamide analogues of NAD+ and NADP+.
CAS REGISTRY NUMBER
COMMENTARY hide
37289-33-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP-ribose + H2O
?
show the reaction diagram
-
-
-
?
diadenosine diphosphate + H2O
?
show the reaction diagram
-
-
-
?
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
-
?
NADH + H2O
NMNH + AMP
show the reaction diagram
-
-
-
?
NADP+ + H2O
? + AMP
show the reaction diagram
-
-
-
?
NADPH + H2O
NMNH + AMP
show the reaction diagram
-
-
-
?
ADPribose + H2O
?
show the reaction diagram
-
-
-
-
?
AppA + H2O
?
show the reaction diagram
-
-
-
-
?
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
-
-
ir
NADH + H2O
AMP + NMNH
show the reaction diagram
-
-
-
?
NADH + H2O
NMNH + AMP
show the reaction diagram
-
possible function in regulation of NAD+/NADH-ratio
-
ir
P1,P4-bis(5'-adenosyl) tetraphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
enzyme may work in the regulation of nicotinamide coenzyme concentration in the peroxisome
-
-
?
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
NADH + H2O
NMNH + AMP
show the reaction diagram
-
possible function in regulation of NAD+/NADH-ratio
-
ir
additional information
?
-
enzyme may work in the regulation of nicotinamide coenzyme concentration in the peroxisome
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
strong activation
Mn2+
-
strong activation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
in presence of Mg2+ complete inhibition
Zn2+
-
in presence of Mg2+ complete inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3
ADP-ribose
pH 7.7, 37°C
0.5
NAD+
pH 7.7, 37°C
0.17
NADH
pH 7.7, 37°C
6.6
NAD+
-
50 mM Tris-HCl, pH 7.5, 5 mM MgCl2
1.6
NADH
-
50 mM Tris-HCl, pH 7.5, 5 mM MgCl2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000167
NAD+
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43500
-
homodimer, 2 * 43500
87000
-
two subunits of 43500 Da found
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
homodimer, 2 * 43500
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
protein has a potential peroxisomal targeting signal
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of gene product from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Xu, W.; Dunn, C.A.; Bessman, M.J.
Cloning and characterization of the NADH pyrophospatases from Caenorhabditis elegans and Saccharomyces cerevisiae, members of a nudix hydrolase subfamily
Biochem. Biophys. Res. Commun.
273
753-758
2000
Caenorhabditis elegans, Escherichia coli, Saccharomyces cerevisiae
Manually annotated by BRENDA team
AbdelRaheim, S.R.; Cartwright, J.L.; Gasmi, L.; McLennan, A.G.
The NADH diphosphatase encoded by the Saccharomyces cerevisiae NPY1 nudix hydrolase gene is located in peroxisomes
Arch. Biochem. Biophys.
388
18-24
2001
Saccharomyces cerevisiae (P53164)
Manually annotated by BRENDA team