Information on EC 3.6.1.22 - NAD+ diphosphatase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.6.1.22
-
RECOMMENDED NAME
GeneOntology No.
NAD+ diphosphatase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NAD+ + H2O = AMP + NMN
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
NAD salvage pathway I
-
-
NAD salvage pathway II
-
-
pyridine nucleotide cycling (plants)
-
-
NAD metabolism
-
-
Nicotinate and nicotinamide metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
NAD+ phosphohydrolase
Also acts on NADP+, 3-acetylpyridine and the thionicotinamide analogues of NAD+ and NADP+.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
alkaline phosphodiesterase I
-
-
-
NAD diphosphatase
-
-
-
-
NAD pyrophosphatase
-
-
-
-
NAD+ diphosphatase
-
-
-
-
NAD+ pyrophosphatase
-
-
-
-
NADH pyrophosphatase
-
-
-
-
NADH pyrophosphatase
-
growth factor gene 1 (GFG1, At4g12720) encodes a nudix hydrolase, that is an NADH pyrophosphatase and ADP-ribose pyrophosphatase
NADH pyrophosphatase
-
NADH pyrophosphatase
-
NADH pyrophosphatase
-
-
NADP pyrophosphatase
-
-
-
-
nicotinamide adenine dinucleotide pyrophosphatase
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37289-33-1
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
deletion of the NADH pyrophosphatase gene nudC results in increased susceptibility to isoniazid and ethionamide
physiological function
NADH pyrophosphatase NudC plays an important role in the inactivation of isoniazid and ethionamide
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetylpyridine adenine dinucleotide + H2O
?
show the reaction diagram
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
?
ADP-glucose + H2O
?
show the reaction diagram
-
-
-
-
?
ADP-ribose + H2O
?
show the reaction diagram
-
-
-
?
ADPribose + H2O
?
show the reaction diagram
-
-
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
?
AppA + H2O
?
show the reaction diagram
-
-
-
-
?
ApppA + H2O
?
show the reaction diagram
-
-
-
-
?
AppppA + H2O
?
show the reaction diagram
-
-
-
-
?
dATP + H2O
?
show the reaction diagram
-
-
-
-
?
deamino-NAD+ + H2O
deamino-NMN + AMP
show the reaction diagram
-
-
-
?
deamino-NADH + H2O
deamino-NMNH + AMP
show the reaction diagram
-
-
-
?
diadenosine diphosphate + H2O
?
show the reaction diagram
-
-
-
?
ethionamide-NAD+ + H2O
ethionamide-NMNH + AMP
show the reaction diagram
-
-
?
FAD + H2O
?
show the reaction diagram
-
-
-
-
?
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
?
NAD+ + H2O
NMN + AMP
show the reaction diagram
weak substrate
-
?
NAD+ + H2O
NMN + AMP
show the reaction diagram
weak substrate
-
?
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
enzyme of the pyridine-nucleotide cycle, involved in nicotine production
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
enzyme of the pyridine-nucleotide cycle, involved in nicotine production
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
possible function in NAD transport
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
weak substrate
-
?
NAD+ + H2O
NMN + AMP
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium LT-2
-
-
-
ir
NAD+ + H2O
AMP + NMN
show the reaction diagram
-
GFG1 transcript levels are rapidly and transiently induced during both biotic stresses imposed by avirulent pathogens and abiotic stresses like ozone and osmoticum.T-DNA knock out plants of GFG1 gene, gfg1-1, exhibit pleiotropic phenotypes such as reduced size, increased levels of reactive oxygen species and NADH, microscopic cell death, constitutive expression of pathogenesis-related genes and enhanced resistance to bacterial pathogens
-
?
NAD+ + H2O
AMP + NMN
show the reaction diagram
-
the enzyme is involved in NAD+ homeostasis
-
?
NADH + H2O
NMNH + AMP
show the reaction diagram
-
-
?
NADH + H2O
NMNH + AMP
show the reaction diagram
-
possible function in regulation of NAD+/NADH-ratio
-
ir
NADH + H2O
NMNH + AMP
show the reaction diagram
-
possible function in regulation of NAD+/NADH-ratio
-
ir
NADH + H2O
NMNH + AMP
show the reaction diagram
highest activity with NADH
-
?
NADH + H2O
NMNH + AMP
show the reaction diagram
highest activity with NADH
-
?
NADH + H2O
AMP + NMNH
show the reaction diagram
-
-
-
?
NADH + H2O
AMP + NMNH
show the reaction diagram
-
-
-
?
NADH + H2O
AMP + NMNH
show the reaction diagram
-
-
-
?
NADH + H2O
AMP + NMNH
show the reaction diagram
-
-
-
?
NADP+ + H2O
NMN + adenosine 3',5'-diphosphate
show the reaction diagram
-
-
-
?
NADP+ + H2O
NMN + adenosine 3',5'-diphosphate
show the reaction diagram
-
-
-
?
NADP+ + H2O
NMN + adenosine 3',5'-diphosphate
show the reaction diagram
-
-
-
?
NADP+ + H2O
NMN + adenosine 3',5'-diphosphate
show the reaction diagram
-
possible function in regulation of NADP-level
-
?
NADP+ + H2O
? + AMP
show the reaction diagram
-
-
?
NADPH + H2O
?
show the reaction diagram
-
-
-
-
?
NADPH + H2O
?
show the reaction diagram
-
-
-
-
?
NADPH + H2O
NMNH + AMP
show the reaction diagram
-
-
?
thio-NAD+ + H2O
?
show the reaction diagram
-
-
-
-
?
thio-NADP+ + H2O
?
show the reaction diagram
-
-
-
-
?
thymidine 5'-p-nitrophenylphosphate + H2O
thymidine + 4-nitrophenyl phosphate
show the reaction diagram
-
-
-
?
UDP + H2O
UMP + phosphate
show the reaction diagram
-
-
-
?
isoniazid-NAD+ + H2O
isoniazid-NMNH + AMP
show the reaction diagram
-
-
?
additional information
?
-
-
enzyme may serve a regulatory role in modifying the inhibitory effect of ecto-NAD on T-cell activation
-
-
-
additional information
?
-
enzyme may work in the regulation of nicotinamide coenzyme concentration in the peroxisome
-
-
-
additional information
?
-
-
involved in NAD uptake and processing to nicotinamide riboside
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
-
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
enzyme of the pyridine-nucleotide cycle, involved in nicotine production
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
enzyme of the pyridine-nucleotide cycle, involved in nicotine production
-
ir
NAD+ + H2O
NMN + AMP
show the reaction diagram
-
possible function in NAD transport
-
ir
NAD+ + H2O
AMP + NMN
show the reaction diagram
-
GFG1 transcript levels are rapidly and transiently induced during both biotic stresses imposed by avirulent pathogens and abiotic stresses like ozone and osmoticum.T-DNA knock out plants of GFG1 gene, gfg1-1, exhibit pleiotropic phenotypes such as reduced size, increased levels of reactive oxygen species and NADH, microscopic cell death, constitutive expression of pathogenesis-related genes and enhanced resistance to bacterial pathogens
-
?
NAD+ + H2O
AMP + NMN
show the reaction diagram
-
the enzyme is involved in NAD+ homeostasis
-
?
NADH + H2O
NMNH + AMP
show the reaction diagram
-
possible function in regulation of NAD+/NADH-ratio
-
ir
NADH + H2O
NMNH + AMP
show the reaction diagram
-
possible function in regulation of NAD+/NADH-ratio
-
ir
NADP+ + H2O
NMN + adenosine 3',5'-diphosphate
show the reaction diagram
-
possible function in regulation of NADP-level
-
?
additional information
?
-
-
enzyme may serve a regulatory role in modifying the inhibitory effect of ecto-NAD on T-cell activation
-
-
-
additional information
?
-
P53164
enzyme may work in the regulation of nicotinamide coenzyme concentration in the peroxisome
-
-
-
additional information
?
-
-
involved in NAD uptake and processing to nicotinamide riboside
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
reactivation of EDTA-treated enzyme
Co2+
-
necessary for maximum activity
Co2+
-
slight activation
Fe2+
-
slight activation
Fe2+
the enzyme shows some activity on NADH in the presence of Fe2+
Mg2+
-
slight activation at concentration of 1.0 mM
Mg2+
-
strong activation at concentration of 0.4 mM
Mg2+
-
strong activation
Mg2+
-
strong activation
Mg2+
-
strong activation
Mg2+
Mg2+ has highest stimulating effect
Mn2+
-
slight activation at concentration of 1.0 mM, reactivation of EDTA-treated enzyme
Mn2+
-
strong activation at concentration of 0.4 mM
Mn2+
-
strong activation
Mn2+
-
strong activation
Mn2+
-
strong activation
Mn2+
Mn2+ has highest stimulating effect
Ni2+
-
strong activation at concentration of 0.4 mM
Zn2+
-
slight activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2',5'-ADP
-
44% inhibition at concentration of 0.133 mM
3-acetylpyridine
-
20% inhibition at conentration of 0.1 M
ADP
-
21% inhibition at concentration of 0.133 mM
ATP
-
22% inhibition at concentration of 0.066 mM
Ca2+
-
20% inhibition at concentration of 0.33 mM
Ca2+
-
in presence of Mg2+ complete inhibition
Ca2+
no activity in the presence of Ca2+
Ca2+
no activity in the presence of Ca2+
Co2+
-
40% inhibition of the purified enzyme at concentration of 0.33 mM, activity in crude extract not affected
CoA
-
85% inhibition at concentration of 0.133 mM
CTP
-
55% inhibition at concentration of 0.066 mM
Cu2+
no activity in the presence of Cu2+
Cu2+
no activity in the presence of Cu2+
DNA
-
strong inhibition by denaturated DNA, slight inhibition by native DNA
EDTA
-
87% inhibition, reactivation by Mn2+ or Co2+
FAD
-
35% inhibition at concentration of 0.133 mM
Fe2+
no activity in the presence of Fe2+
Fe3+
no activity in the presence of Fe3+
Fe3+
no activity in the presence of Fe3+
GTP
-
53% inhibition at concentration of 0.066 mM
Mg2+
no activity in the presence of Mg2+
NMNH
-
competitive inhibitor with Ki: 4.2 mM, no inhibition with NMN+
RNA
-
strong inhibition
UDP
-
32% inhibition at concentration of 0.133 mM
UTP
-
36% inhibition at concentration of 0.066 mM
Zn2+
-
70% inhibition at concentration of 0.33 mM
Zn2+
-
in presence of Mg2+ complete inhibition
Zn2+
no activity in the presence of Zn2+
Zn2+
no activity in the presence of Zn2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Urea
-
8 M urea, 30 mM Phosphate buffer, pH 7.4, 100% activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.3
ADP-ribose
pH 7.7, 37C
1.8
ADP-ribose
-
in presence of 20 mM MgCl2, 50 mM Tris-HCl, pH 8.5
0.67
AppA
-
in presence of 20 mM MgCl2, 50 mM Tris-HCl, pH 8.5
2.6
dNAD+
-
in presence of 20 mM MgCl2, 50 mM Tris-HCl, pH 8.5
0.29
dNADH
-
in presence of 20 mM MgCl2, 50 mM Tris-HCl, pH 8.5
0.01
NAD+
-
100 mM MOPS-NaOH, pH 7.4, 5 mM MgCl2, 10 mM dithioerythritol, 0.1 mM EDTA
0.5
NAD+
pH 7.7, 37C
5.1
NAD+
-
in presence of 20 mM MgCl2, 50 mM Tris-HCl, pH 8.5
6.6
NAD+
-
50 mM Tris-HCl, pH 8.5, 5 mM MgCl2
6.6
NAD+
-
50 mM Tris-HCl, pH 7.5, 5 mM MgCl2
0.11
NADH
-
in presence of 20 mM MgCl2, 50 mM Tris-HCl, pH 8.5
0.17
NADH
pH 7.7, 37C
1.4
NADH
-
50 mM Tris-HCl, pH 8.5, 5 mM MgCl2
1.6
NADH
-
50 mM Tris-HCl, pH 7.5, 5 mM MgCl2
0.025
NADP+
-
Tris-HCl, pH 7.0
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000167
NAD+
Caenorhabditis elegans, Saccharomyces cerevisiae
-
-
0.001
NADH
Escherichia coli
-
based on two active sites/dimer
0.00117
NADH
Caenorhabditis elegans
-
-
0.0025
NADH
Saccharomyces cerevisiae
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.1
NMNH
-
competitive inhibitor, no inhibiton with NMN+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0008
-
crude extract
0.17
-
partially purified enzyme
0.29
-
activity of inner membrane fraction
0.78
-
purified enzyme with 1 mM MnCl2
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
enzyme activity rapidly decreases below pH 7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 9.5
-
40% of maximum activity at pH 7.5, 60% of maximum activity at pH 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
range 20-65C in 5C steps
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 45
enzyme activity rapidly decreases below 35C or above 45C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
of infected rats and humans
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
more than 95% of membrane bound activity located at inner membrane
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50000
gel filtration
720498
60000
-
gel filtration, Sephadex G-100
209957
78200
-
two subunits of 39100 Da found
209959
80000
gel filtration
720498
87000
-
two subunits of 43500 Da found
209959
105000
-
SDS-PAGE
209958
120000
-
gel filtration, Sephadex G-150
171773
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
homodimer, 2 * 29774 in SDS-PAGE, gel filtration
dimer
-
homodimer, 2 * 39100
dimer
-
homodimer, 2 * 43500
homodimer
2 * 40000, SDS-PAGE
monomer
1 * 50000, SDS-PAGE; 1 * 51000, purified recombinant NudC (fused with Trx tag), calculated from amino acid sequence
monomer
-
1 * 50000, SDS-PAGE; 1 * 51000, purified recombinant NudC (fused with Trx tag), calculated from amino acid sequence
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
protein has a potential peroxisomal targeting signal
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
73
-
2 min causes activation
209951
98
-
few min at 98C causes loss of activity, 30 s causes activation
209951
100
-
2 min at 100C causes complete loss of activity
209948
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, storage of homogenates for several weeks, no loss of activity
-
37C, 0.1 M Tris, pH 8.75, 150 min, no loss of activity
-
4C, 100 mM MOPS-NaOH, pH 7.4, 5 mM MgCl2, 10 mM dithioerythritol, 0.1 mM EDTA, 5h, no loss of activity
-
18C, 50 mM phosphate buffer, pH 7.0, 1 h, 70% loss of activity
-
4C, 50 mM phosphate buffer, pH 7.0, overnight, 70% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification of gene product from Escherichia coli
-
more than 98% purity
-
nickel affinity column chromatography and Superdex 200 gel filtration
nickel affinity column chromatography and Superdex 200 gel filtration
purification of gene product from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3) cells and in Mycobacterium smegmatis strain mc2155
expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P237Q
the mutation prevents dimer formation, and results in a loss of enzymatic activity
P237Q
the mutation prevents dimer formation, and results in a loss of enzymatic activity
P237Q
-
the mutation prevents dimer formation, and results in a loss of enzymatic activity
-
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
0.5% lauryldimethylamine oxide or 1% Triton X-100, 30 min after SDS-PAGE
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
enzyme may serve a regulatory role in modifying the inhibitory effect of ecto-NAD on T-cell activation
synthesis
-
preparation of NMN