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Information on EC 3.2.2.14 - NMN nucleosidase
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3.2.2.14 NMN nucleosidaseSpecify your search results
Word Map
- 3.2.2.14
- pyridine
-
nicotinic
- riboside
-
azotobacter
- typhimurium
-
salvage
-
pyrophosphatase
- vinelandii
- purine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
nmn glycohydrolase, nar nucleosidase, nicotinamide mononucleotide glycohydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
nicotinamide mononucleotidase
-
-
-
-
nicotinamide mononucleotide glycohydrolase
-
-
-
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nicotinamide mononucleotide nucleosidase
-
-
-
-
NMN glycohydrolase
-
-
-
-
NMNase
-
-
-
-
NMNGhase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
beta-nicotinamide D-ribonucleotide + H2O = D-ribose 5-phosphate + nicotinamide
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of N-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
nicotinamide-nucleotide phosphoribohydrolase
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CAS REGISTRY NUMBER
COMMENTARY
37237-49-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nicotinamide mononucleotide + H2O
?
-
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
-
-
-
nicotinamide mononucleotide + H2O
?
-
biological function reusing NMN resulting from degradation of pyridine cofactors by nucleotide pyrophosphatase, EC 3.6.1.9, in concert with NMN aminohydrolase, EC 3.5.1.42
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-
-
nicotinamide mononucleotide + H2O
?
-
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
-
-
-
nicotinamide mononucleotide + H2O
?
-
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
-
-
-
nicotinamide mononucleotide + H2O
?
-
NMN, product of DNA ligase activity
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-
-
nicotinamide mononucleotide + H2O
?
-
-
-
-
-
nicotinamide mononucleotide + H2O
?
-
-
-
-
-
nicotinamide mononucleotide + H2O
nicotinamide + ribose 5-phosphate
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irreversible hydrolysis of the N-ribosidic linkage of NMN
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ir
nicotinamide mononucleotide + H2O
nicotinamide + ribose 5-phosphate
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irreversible hydrolysis of the N-ribosidic linkage of NMN
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ir
nicotinamide mononucleotide + H2O
nicotinamide + ribose 5-phosphate
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-
-
-
nicotinamide mononucleotide + H2O
nicotinamide + ribose 5-phosphate
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-
-
?
nicotinic acid mononucleotide + H2O
nicotinic acid + ribose 5-phosphate
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NaNM reaction slowly, 8% hydrolysis of the rate of NMN
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?
nicotinic acid mononucleotide + H2O
nicotinic acid + ribose 5-phosphate
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NaNM reaction slowly, 8% hydrolysis of the rate of NMN
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nicotinamide mononucleotide + H2O
?
-
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
-
-
-
nicotinamide mononucleotide + H2O
?
-
biological function reusing NMN resulting from degradation of pyridine cofactors by nucleotide pyrophosphatase, EC 3.6.1.9, in concert with NMN aminohydrolase, EC 3.5.1.42
-
-
-
nicotinamide mononucleotide + H2O
?
-
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
-
-
-
nicotinamide mononucleotide + H2O
?
-
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
-
-
-
nicotinamide mononucleotide + H2O
?
-
NMN, product of DNA ligase activity
-
-
-
nicotinamide mononucleotide + H2O
?
-
-
-
-
-
nicotinamide mononucleotide + H2O
?
-
-
-
-
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-phosphoribose 1-diphosphate
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PRPP, inorganic polyphosphates, affinity of 5-phosphoribose 1-pyrophosphate for the enzyme is dependent on the activator concentration , inhibition mechanism with 5-phosphoribose 1-pyrophosphate is competitive with GTP
adenosine
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addition of 1.4 mM, inhibition 54.7%
ADP-ribose
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addition of 1-1.4 mM, inhibition 74.4%
AMP
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addition of 1.4 mM AMP, inhibition 92.5%
D-ribose-5-phosphate
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addition of 1.4 mM, inhibition 42.3%
dCMP
-
effective inhibition in presence of 1 mM GTP, noncompetitive inhibitor
desamido-NAD+
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addition of 1 mM, inhibition 66.6%
dGMP
-
effective inhibition in presence of 1 mM GTP, noncompetitive inhibitor
guanosine
-
addition of 1.4 mM, inhibition 44.6%
NAD+
-
greatly inhibited by intracellular levels of NAD+ and reduced NADH, addition of 1 mM NAD+, inhibition 73.2%
NADH
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addition of 1 mM, inhibition 68.6%
NADP+
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addition of 1 mM, inhibition 24%
nicotinamide hypoxanthine dinucleotide
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addition of 1 mM nicotinamide hypoxanthine dinucleotide, inhibition 61.4%
pyridoxal 5'-phosphate
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addition of 1.4 mM, inhibition 8.8%
pyridoxal HCl
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addition of 1.4 mM, inhibition 5.2%
thio-NAD+
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addition of 1 mM, inhibition 63.2%
GMP
-
addition of 1.4 mM GMP, inhibition 89.4%
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
guanosine 3'-diphosphate-5'-triphosphate
-
guanine nucleotides, guanosinetriphosphate and polyphosphate derivatives, effective activation
SO42-
-
10 mM relative activity 103%, 100% activity with nicotinamide as substrate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.4
nicotinamide mononucleotide
-
0.5 mM guanosine 5'-tetraphosphate as effector
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.032
-
addition of 1.4 mM GTP, inhibition 93.1%
0.034
-
addition of 1.4 mM AMP, inhibition 92.5%
0.049
-
addition of 1.4 mM GMP, inhibition 89.4%
0.117
-
addition of 1.4 mM ADP-ribose, inhibition 74.4%
0.122
-
addition of 1 mM ADP-ribose, inhibition 74.4%
0.128
-
addition of 1 mM NAD+, inhibition 73.2%
0.15
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addition of 1 mM NADH, inhibition 68.6%
0.16
-
addition of 1 mM desamido-NAD+, inhibition 66.6%
0.176
-
addition of 1 mM thio-NAD+, inhibition 63.2%
0.186
-
addition of 1 mM NHD, inhibition 61.4%
0.208
-
addition of 1.4 mM adenosine, inhibition 54.7%
0.254
-
addition of 1.4 mM guanosine, inhibition 44.6%
0.264
-
addition of 1.4 mM D-ribose-5-phosphate, inhibition 42.3%
0.363
-
addition of 1 mM NADP+, inhibition 24%
0.418
-
addition of 1.4 mM pyridoxal 5'-phosphate, inhibition 8.8%
0.434
-
addition of 1.4 mM pyridoxal HCl, inhibition 5.2%
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
-
1 * 110000 + 1 * 110000, enzyme easily dissociates in presence of 1 mM ATP, consisting of 4 identical protomers, MW 55000, no dissociation in presence of GTP
240000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
1 * 110000 + 1 * 110000, enzyme easily dissociates in presence of 1 mM ATP, consisting of 4 identical protomers, MW 55000, no dissociation in presence of GTP
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
remains active for 1 week at 4°C in 0.025 M Tris-HCl, pH 7.5, containing 1 mM reduced glutathione
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, 0.025 M Tris-HCl, pH 9, containing 1 mM reduced glutathione, one-half of enzyme activity lost in 5 days
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
partially from sonic extract, purified enzyme loses over 90% of its activity after Sephadex G-200 treatment
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Imai, T.
Properties of allosteric nicotinamide mononucleotide glycohydrolase from Azotobacter vinelandii: Activation and inhibition
J. Biochem.
101
163-173
1987
Azotobacter vinelandii
brenda
Imai, T.
Isolation and characterization of an activator for Azotobacter vinelandii nicotinamide mononucleotide glycohydrolase
J. Biochem.
101
153-161
1987
Azotobacter vinelandii
brenda
Wagner, R.; Feth, F.; Wagner, K.G.
The pyridine-nucleotide cycle in tobacco. Enzyme activities for the recycling of NAD
Planta
167
226-232
1986
Nicotiana tabacum
brenda
Wagner, R.; Feth, F.; Wagner, K.G.
Regulation in tobacco callus of enzyme activities of the nicotine pathway II. The pyridine-nucleotide cycle
Planta
168
408-413
1986
Nicotiana tabacum
brenda
Foster, J.W.
Pyridine nucleotide cycle of Salmonella typhimurium: in vitro demonstration of nicotinamide adenine dinucleotide glycohydrolase, nicotinamide mononucleotide glycohydrolase, and nicotinamide adenine dinucleotide pyrophosphatase activities
J. Bacteriol.
145
1002-1009
1981
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium LT2
brenda
Imai, T.
Isolation and properties of a glycohydrolase specific for nicotinamide mononucleotide from Azotobacter vinelandii
J. Biochem.
85
887-899
1979
Azotobacter vinelandii, Azotobacter vinelandii O, Escherichia coli
brenda
Andreoli, A.J.; Okita, T.W.; Bloom, R.; Grover, T.A.
The pyridine nucleotide cycle: Presence of a nicotinamide mononucleotide-specific glycohydrolase in Escherichia coli
Biochem. Biophys. Res. Commun.
49
264-269
1972
Escherichia coli
brenda
Denicola-Seoane, A.; Anderson, B.M.
Studies of NAD kinase and NMN:ATP adenylyltransferase in Haemophilus influenzae
J. Gen. Microbiol.
136
425-430
1990
Haemophilus influenzae, Haemophilus influenzae RD
brenda
Ashihara, H.; Deng, W.
Pyridine metabolism in tea plants: Salvage, conjugate formation and catabolism
J. Plant Res.
125
781-791
2012
Camellia sinensis
brenda
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