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 hide
3.6.1.22
-
RECOMMENDED NAME
GeneOntology No.
NAD+ diphosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NAD+ + H2O = AMP + NMN
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
NAD metabolism
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NAD salvage pathway I
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NAD salvage pathway II
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NAD salvage pathway III
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Nicotinate and nicotinamide metabolism
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pyridine nucleotide cycling (plants)
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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
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
deletion of the NADH pyrophosphatase gene nudC results in increased susceptibility to isoniazid and ethionamide
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetylpyridine adenine dinucleotide + H2O
?
show the reaction diagram
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-
-
-
?
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
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-
-
-
?
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
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-
-
?
ethionamide-NAD+ + H2O
ethionamide-NMNH + AMP
show the reaction diagram
-
-
-
?
FAD + H2O
?
show the reaction diagram
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-
-
-
?
isoniazid-NAD+ + H2O
isoniazid-NMNH + AMP
show the reaction diagram
-
-
-
?
NAD+ + H2O
AMP + NMN
show the reaction diagram
NAD+ + H2O
NMN + AMP
show the reaction diagram
NADH + H2O
AMP + NMNH
show the reaction diagram
NADH + H2O
NMNH + AMP
show the reaction diagram
NADP+ + H2O
? + AMP
show the reaction diagram
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-
-
?
NADP+ + H2O
NMN + adenosine 3',5'-diphosphate
show the reaction diagram
NADPH + H2O
?
show the reaction diagram
NADPH + H2O
NMNH + AMP
show the reaction diagram
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-
-
?
NMN + H2O
nicotinamide riboside + phosphate
show the reaction diagram
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-
-
?
thio-NAD+ + H2O
?
show the reaction diagram
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-
-
-
?
thio-NADP+ + H2O
?
show the reaction diagram
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-
-
-
?
thymidine 5'-p-nitrophenylphosphate + H2O
thymidine + 4-nitrophenyl phosphate
show the reaction diagram
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-
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?
UDP + H2O
UMP + phosphate
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NAD+ + H2O
AMP + NMN
show the reaction diagram
NAD+ + H2O
NMN + AMP
show the reaction diagram
NADH + H2O
NMNH + AMP
show the reaction diagram
NADP+ + H2O
NMN + adenosine 3',5'-diphosphate
show the reaction diagram
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possible function in regulation of NADP-level
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ni2+
-
strong activation at concentration of 0.4 mM
Zn2+
-
slight activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2',5'-ADP
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44% inhibition at concentration of 0.133 mM
3-acetylpyridine
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20% inhibition at conentration of 0.1 M
ADP
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21% inhibition at concentration of 0.133 mM
ATP
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22% inhibition at concentration of 0.066 mM
Co2+
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40% inhibition of the purified enzyme at concentration of 0.33 mM, activity in crude extract not affected
CoA
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85% inhibition at concentration of 0.133 mM
CTP
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55% inhibition at concentration of 0.066 mM
DNA
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strong inhibition by denaturated DNA, slight inhibition by native DNA
EDTA
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87% inhibition, reactivation by Mn2+ or Co2+
FAD
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35% inhibition at concentration of 0.133 mM
GTP
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53% inhibition at concentration of 0.066 mM
Mg2+
no activity in the presence of Mg2+
NMNH
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competitive inhibitor with Ki: 4.2 mM, no inhibition with NMN+
RNA
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strong inhibition
UDP
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32% inhibition at concentration of 0.133 mM
UTP
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36% inhibition at concentration of 0.066 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Urea
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8 M urea, 30 mM Phosphate buffer, pH 7.4, 100% activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3 - 1.8
ADP-ribose
0.67
AppA
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in presence of 20 mM MgCl2, 50 mM Tris-HCl, pH 8.5
2.6
dNAD+
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in presence of 20 mM MgCl2, 50 mM Tris-HCl, pH 8.5
0.29
dNADH
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in presence of 20 mM MgCl2, 50 mM Tris-HCl, pH 8.5
0.0053 - 6.6
NAD+
0.007 - 1.6
NADH
0.025
NADP+
-
Tris-HCl, pH 7.0
0.0111
NMN
pH 7.5, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000167 - 19.3
NAD+
0.001 - 10
NADH
1492
NMN
Escherichia coli
P07024
pH 7.5, 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3700
NAD+
Escherichia coli
P07024
pH 7.5, 30C
7
1400
NADH
Escherichia coli
P07024
pH 7.5, 30C
8
135000
NMN
Escherichia coli
P07024
pH 7.5, 30C
775
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.1
NMNH
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competitive inhibitor, no inhibiton with NMN+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0008
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crude extract
0.17
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partially purified enzyme
0.29
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activity of inner membrane fraction
0.78
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purified enzyme with 1 mM MnCl2
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
enzyme activity rapidly decreases below pH 7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9.5
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40% of maximum activity at pH 7.5, 60% of maximum activity at pH 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
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range 20-65C in 5C steps
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 45
enzyme activity rapidly decreases below 35C or above 45C
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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of infected rats and humans
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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more than 95% of membrane bound activity located at inner membrane
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Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
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gel filtration, Sephadex G-100
78200
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two subunits of 39100 Da found
80000
gel filtration
87000
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two subunits of 43500 Da found
105000
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SDS-PAGE
120000
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gel filtration, Sephadex G-150
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 40000, SDS-PAGE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
protein has a potential peroxisomal targeting signal
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
73
-
2 min causes activation
98
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few min at 98C causes loss of activity, 30 s causes activation
100
-
2 min at 100C causes complete loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, storage of homogenates for several weeks, no loss of activity
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18C, 50 mM phosphate buffer, pH 7.0, 1 h, 70% loss of activity
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37C, 0.1 M Tris, pH 8.75, 150 min, no loss of activity
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4C, 100 mM MOPS-NaOH, pH 7.4, 5 mM MgCl2, 10 mM dithioerythritol, 0.1 mM EDTA, 5h, no loss of activity
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4C, 50 mM phosphate buffer, pH 7.0, overnight, 70% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
more than 98% purity
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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
expressed in Escherichia coli BL21 (DE3) cells and in Mycobacterium smegmatis strain mc2155
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
0.5% lauryldimethylamine oxide or 1% Triton X-100, 30 min after SDS-PAGE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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enzyme may serve a regulatory role in modifying the inhibitory effect of ecto-NAD on T-cell activation
synthesis
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preparation of NMN
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