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EC Tree
IUBMB Comments The enzyme is thought to participate in an NAD+-salvage pathway. In eukaryotic organisms this activity has been attributed to EC 3.2.2.6, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
nmn glycohydrolase, nar nucleosidase, nicotinamide mononucleotide glycohydrolase,
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nicotinamide mononucleotidase
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nicotinamide mononucleotide glycohydrolase
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nicotinamide mononucleotide nucleosidase
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beta-nicotinamide D-ribonucleotide + H2O = D-ribose 5-phosphate + nicotinamide
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hydrolysis of N-glycosyl bond
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nicotinamide-nucleotide phosphoribohydrolase
The enzyme is thought to participate in an NAD+-salvage pathway. In eukaryotic organisms this activity has been attributed to EC 3.2.2.6, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase.
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beta-nicotinamide D-riboside + H2O
D-ribose + nicotinamide
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guanosine 3'-diphosphate 5'-triphosphate + H2O
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nicotinamide mononucleotide + H2O
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nicotinamide mononucleotide + H2O
nicotinamide + ribose 5-phosphate
nicotinic acid mononucleotide + H2O
nicotinic acid + ribose 5-phosphate
nicotinamide mononucleotide + H2O
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conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
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nicotinamide mononucleotide + H2O
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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
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conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
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nicotinamide mononucleotide + H2O
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conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
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nicotinamide mononucleotide + H2O
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NMN, product of DNA ligase activity
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nicotinamide mononucleotide + H2O
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nicotinamide mononucleotide + H2O
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nicotinamide mononucleotide + H2O
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nicotinamide mononucleotide + H2O
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nicotinamide mononucleotide + H2O
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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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beta-nicotinamide D-riboside + H2O
D-ribose + nicotinamide
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nicotinamide mononucleotide + H2O
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nicotinamide mononucleotide + H2O
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conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
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nicotinamide mononucleotide + H2O
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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
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conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
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nicotinamide mononucleotide + H2O
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conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
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nicotinamide mononucleotide + H2O
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NMN, product of DNA ligase activity
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nicotinamide mononucleotide + H2O
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nicotinamide mononucleotide + H2O
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nicotinamide mononucleotide + H2O
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nicotinamide mononucleotide + H2O
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nicotinamide mononucleotide + H2O
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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
7-methylguanosine-5'-triphosphate
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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
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effective inhibition in presence of 1 mM GTP, noncompetitive inhibitor
desamido-NAD+
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addition of 1 mM, inhibition 66.6%
dGMP
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effective inhibition in presence of 1 mM GTP, noncompetitive inhibitor
EDTA
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1 mM inhibits NMN hydrolysis by 30%
guanosine
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addition of 1.4 mM, inhibition 44.6%
N-ethylmaleimide
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50% inhibition at 80 mM
NAD+
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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%
p-chloromercuribenzoate
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50% inhibition at 3 mM
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
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effective inhibition in presence of 1 mM GTP
GMP
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addition of 1.4 mM GMP, inhibition 89.4%
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ATP
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less effective activator than GTP
guanosine 2'-monophosphate
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guanosine 3'-diphosphate-5'-triphosphate
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guanine nucleotides, guanosinetriphosphate and polyphosphate derivatives, effective activation
guanosine 3'-monophosphate
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guanosine 5'-tetraphosphate
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most potent activator
SO42-
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10 mM relative activity 103%, 100% activity with nicotinamide as substrate
GTP
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GTP
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most potent activator
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0.0087
guanosine 3'-diphosphate 5'-triphosphate
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0.22 - 4.5
nicotinamide mononucleotide
0.22
nicotinamide mononucleotide
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2
nicotinamide mononucleotide
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in absence of GTP
4
nicotinamide mononucleotide
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0.52 mM dGTP as effector
4.4
nicotinamide mononucleotide
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0.5 mM guanosine 5'-tetraphosphate as effector
4.5
nicotinamide mononucleotide
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0.5 mM/1 mM GTP
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3
p-chloromercuribenzoate
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0.032
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addition of 1.4 mM GTP, inhibition 93.1%
0.034
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addition of 1.4 mM AMP, inhibition 92.5%
0.049
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addition of 1.4 mM GMP, inhibition 89.4%
0.117
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addition of 1.4 mM ADP-ribose, inhibition 74.4%
0.122
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addition of 1 mM ADP-ribose, inhibition 74.4%
0.128
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addition of 1 mM NAD+, inhibition 73.2%
0.15
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addition of 1 mM NADH, inhibition 68.6%
0.16
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addition of 1 mM desamido-NAD+, inhibition 66.6%
0.176
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addition of 1 mM thio-NAD+, inhibition 63.2%
0.186
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addition of 1 mM NHD, inhibition 61.4%
0.208
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addition of 1.4 mM adenosine, inhibition 54.7%
0.254
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addition of 1.4 mM guanosine, inhibition 44.6%
0.264
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addition of 1.4 mM D-ribose-5-phosphate, inhibition 42.3%
0.363
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addition of 1 mM NADP+, inhibition 24%
0.418
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addition of 1.4 mM pyridoxal 5'-phosphate, inhibition 8.8%
0.434
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addition of 1.4 mM pyridoxal HCl, inhibition 5.2%
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brenda
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brenda
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brenda
bacterial meningitis, type b
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brenda
bacterial meningitis, type b
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brenda
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brenda
LT-2
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brenda
LT-2
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brenda
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brenda
K-12
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brenda
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established from the roots of seedlings
brenda
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brenda
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A0A289ZYP3_9ACTN
241
1
25677
TrEMBL
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110000
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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
213000
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gel filtration, Sephadex G-200
240000
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240000
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gel filtration, Sepharose 6B
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dimer
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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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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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0 to -16°C stored for a month without significant loss of activity
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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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partially from sonic extract, purified enzyme loses over 90% of its activity after Sephadex G-200 treatment
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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
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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, Escherichia coli, Azotobacter vinelandii O
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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3.2.2.14 NMN nucleosidase
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