Data extracted from this reference:
Activating Compound
ATP
less effective activator than GTP
Azotobacter vinelandii
dGMP
Azotobacter vinelandii
dGTP
Azotobacter vinelandii
GDP
Azotobacter vinelandii
GMP
Azotobacter vinelandii
GTP
most potent activator
Azotobacter vinelandii
guanosine 2'-monophosphate
Azotobacter vinelandii
guanosine 3'-monophosphate
Azotobacter vinelandii
guanosine 5'-tetraphosphate
most potent activator
Azotobacter vinelandii
General Stability
remains active for 1 week at 4°C in 0.025 M Tris-HCl, pH 7.5, containing 1 mM reduced glutathione
Azotobacter vinelandii
Inhibitors
Cd2+
1 mM
Azotobacter vinelandii
Cu2+
1 mM
Azotobacter vinelandii
dCMP
effective inhibition in presence of 1 mM GTP, noncompetitive inhibitor
Azotobacter vinelandii
dGMP
effective inhibition in presence of 1 mM GTP, noncompetitive inhibitor
Azotobacter vinelandii
EDTA
1 mM inhibits NMN hydrolysis by 30%
Azotobacter vinelandii
GMP
effective inhibition in presence of 1 mM GTP
Azotobacter vinelandii
N-ethylmaleimide
50% inhibition at 80 mM
Azotobacter vinelandii
p-chloromercuribenzoate
50% inhibition at 3 mM
Azotobacter vinelandii
Zn2+
1 mM
Azotobacter vinelandii
KM Value [mM]
2
nicotinamide mononucleotide
in absence of GTP
Azotobacter vinelandii
4
nicotinamide mononucleotide
0.52 mM dGTP as effector
Azotobacter vinelandii
4.4
nicotinamide mononucleotide
0.5 mM guanosine 5'-tetraphosphate as effector
Azotobacter vinelandii
4.5
nicotinamide mononucleotide
0.5 mM/1 mM GTP
Azotobacter vinelandii
Molecular Weight [Da]
213000
gel filtration, Sephadex G-200
Azotobacter vinelandii
240000
gel filtration, Sepharose 6B
Azotobacter vinelandii
Natural Substrates/ Products (Substrates)
nicotinamide mononucleotide + H2O
Escherichia coli
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
?
nicotinamide mononucleotide + H2O
Azotobacter vinelandii
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
?
nicotinamide mononucleotide + H2O
Azotobacter vinelandii O
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
?
Organism
Purification (Commentary)
partially from sonic extract, purified enzyme loses over 90% of its activity after Sephadex G-200 treatment
Azotobacter vinelandii
Specific Activity [micromol/min/mg]
0.0195
Azotobacter vinelandii
Storage Stability
0 to -16°C stored for a month without significant loss of activity
Azotobacter vinelandii
0°C, 0.025 M Tris-HCl, pH 9, containing 1 mM reduced glutathione, one-half of enzyme activity lost in 5 days
Azotobacter vinelandii
Substrates and Products (Substrate)
nicotinamide mononucleotide + H2O
171774
Escherichia coli
nicotinamide + ribose 5-phosphate
171774
Escherichia coli
nicotinamide mononucleotide + H2O
irreversible hydrolysis of the N-ribosidic linkage of NMN
171774
Azotobacter vinelandii
nicotinamide + ribose 5-phosphate
171774
Azotobacter vinelandii
ir
nicotinamide mononucleotide + H2O
irreversible hydrolysis of the N-ribosidic linkage of NMN
171774
Azotobacter vinelandii O
nicotinamide + ribose 5-phosphate
171774
Azotobacter vinelandii O
ir
nicotinamide mononucleotide + H2O
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
171774
Escherichia coli
?
nicotinamide mononucleotide + H2O
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
171774
Azotobacter vinelandii
?
nicotinamide mononucleotide + H2O
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
171774
Azotobacter vinelandii O
?
nicotinic acid mononucleotide + H2O
NaNM reaction slowly, 8% hydrolysis of the rate of NMN
171774
Azotobacter vinelandii
nicotinic acid + ribose 5-phosphate
171774
Azotobacter vinelandii
?
nicotinic acid mononucleotide + H2O
NaNM reaction slowly, 8% hydrolysis of the rate of NMN
171774
Azotobacter vinelandii O
nicotinic acid + ribose 5-phosphate
171774
Azotobacter vinelandii O
?
Temperature Optimum [°C]
39
Azotobacter vinelandii
pH Optimum
8.5
9
Azotobacter vinelandii
Ki Value [mM]
3
p-chloromercuribenzoate
Azotobacter vinelandii
80
N-ethylmaleimide
Azotobacter vinelandii
Activating Compound (protein specific)
ATP
less effective activator than GTP
Azotobacter vinelandii
dGMP
Azotobacter vinelandii
dGTP
Azotobacter vinelandii
GDP
Azotobacter vinelandii
GMP
Azotobacter vinelandii
GTP
most potent activator
Azotobacter vinelandii
guanosine 2'-monophosphate
Azotobacter vinelandii
guanosine 3'-monophosphate
Azotobacter vinelandii
guanosine 5'-tetraphosphate
most potent activator
Azotobacter vinelandii
General Stability (protein specific)
remains active for 1 week at 4°C in 0.025 M Tris-HCl, pH 7.5, containing 1 mM reduced glutathione
Azotobacter vinelandii
Inhibitors (protein specific)
Cd2+
1 mM
Azotobacter vinelandii
Cu2+
1 mM
Azotobacter vinelandii
dCMP
effective inhibition in presence of 1 mM GTP, noncompetitive inhibitor
Azotobacter vinelandii
dGMP
effective inhibition in presence of 1 mM GTP, noncompetitive inhibitor
Azotobacter vinelandii
EDTA
1 mM inhibits NMN hydrolysis by 30%
Azotobacter vinelandii
GMP
effective inhibition in presence of 1 mM GTP
Azotobacter vinelandii
N-ethylmaleimide
50% inhibition at 80 mM
Azotobacter vinelandii
p-chloromercuribenzoate
50% inhibition at 3 mM
Azotobacter vinelandii
Zn2+
1 mM
Azotobacter vinelandii
Ki Value [mM] (protein specific)
3
p-chloromercuribenzoate
Azotobacter vinelandii
80
N-ethylmaleimide
Azotobacter vinelandii
KM Value [mM] (protein specific)
2
nicotinamide mononucleotide
in absence of GTP
Azotobacter vinelandii
4
nicotinamide mononucleotide
0.52 mM dGTP as effector
Azotobacter vinelandii
4.4
nicotinamide mononucleotide
0.5 mM guanosine 5'-tetraphosphate as effector
Azotobacter vinelandii
4.5
nicotinamide mononucleotide
0.5 mM/1 mM GTP
Azotobacter vinelandii
Molecular Weight [Da] (protein specific)
213000
gel filtration, Sephadex G-200
Azotobacter vinelandii
240000
gel filtration, Sepharose 6B
Azotobacter vinelandii
Natural Substrates/ Products (Substrates) (protein specific)
nicotinamide mononucleotide + H2O
Escherichia coli
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
?
nicotinamide mononucleotide + H2O
Azotobacter vinelandii
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
?
nicotinamide mononucleotide + H2O
Azotobacter vinelandii O
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
?
Purification (Commentary) (protein specific)
partially from sonic extract, purified enzyme loses over 90% of its activity after Sephadex G-200 treatment
Azotobacter vinelandii
Specific Activity [micromol/min/mg] (protein specific)
0.0195
Azotobacter vinelandii
Storage Stability (protein specific)
0 to -16°C stored for a month without significant loss of activity
Azotobacter vinelandii
0°C, 0.025 M Tris-HCl, pH 9, containing 1 mM reduced glutathione, one-half of enzyme activity lost in 5 days
Azotobacter vinelandii
Substrates and Products (Substrate) (protein specific)
nicotinamide mononucleotide + H2O
171774
Escherichia coli
nicotinamide + ribose 5-phosphate
171774
Escherichia coli
nicotinamide mononucleotide + H2O
irreversible hydrolysis of the N-ribosidic linkage of NMN
171774
Azotobacter vinelandii
nicotinamide + ribose 5-phosphate
171774
Azotobacter vinelandii
ir
nicotinamide mononucleotide + H2O
irreversible hydrolysis of the N-ribosidic linkage of NMN
171774
Azotobacter vinelandii O
nicotinamide + ribose 5-phosphate
171774
Azotobacter vinelandii O
ir
nicotinamide mononucleotide + H2O
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
171774
Escherichia coli
?
nicotinamide mononucleotide + H2O
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
171774
Azotobacter vinelandii
?
nicotinamide mononucleotide + H2O
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
171774
Azotobacter vinelandii O
?
nicotinic acid mononucleotide + H2O
NaNM reaction slowly, 8% hydrolysis of the rate of NMN
171774
Azotobacter vinelandii
nicotinic acid + ribose 5-phosphate
171774
Azotobacter vinelandii
?
nicotinic acid mononucleotide + H2O
NaNM reaction slowly, 8% hydrolysis of the rate of NMN
171774
Azotobacter vinelandii O
nicotinic acid + ribose 5-phosphate
171774
Azotobacter vinelandii O
?
Temperature Optimum [°C] (protein specific)
39
Azotobacter vinelandii
pH Optimum (protein specific)
8.5
9
Azotobacter vinelandii
Other publictions for EC 3.2.2.14
732384
Ashihara
Pyridine metabolism in tea pla ...
Camellia sinensis
J. Plant Res.
125
781-791
2012
-
-
-
-
-
-
-
-
-
-
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1
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
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1
-
-
-
-
-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
171776
Denicola-Seoane
Studies of NAD kinase and NMN: ...
Haemophilus influenzae, Haemophilus influenzae RD
J. Gen. Microbiol.
136
425-430
1990
-
-
-
-
-
-
-
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2
-
7
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2
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2
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2
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-
171769
Imai
Properties of allosteric nicot ...
Azotobacter vinelandii
J. Biochem.
101
163-173
1987
3
-
-
-
-
-
4
1
-
-
3
1
-
2
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
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3
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-
-
-
-
-
4
-
1
-
-
3
1
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
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-
-
-
171770
Imai
Isolation and characterization ...
Azotobacter vinelandii
J. Biochem.
101
153-161
1987
2
-
-
-
-
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-
-
-
-
-
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4
-
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2
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-
-
-
171771
Wagner
The pyridine-nucleotide cycle ...
Nicotiana tabacum
Planta
167
226-232
1986
-
-
-
-
-
-
-
1
-
-
-
1
-
1
-
-
1
-
-
1
-
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1
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-
-
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-
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-
1
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1
-
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1
-
1
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1
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-
-
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-
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-
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-
171772
Wagner
Regulation in tobacco callus o ...
Nicotiana tabacum
Planta
168
408-413
1986
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-
-
-
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-
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1
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1
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1
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1
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1
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1
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1
-
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-
-
-
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-
-
-
-
-
-
171773
Foster
Pyridine nucleotide cycle of S ...
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium LT2
J. Bacteriol.
145
1002-1009
1981
-
-
-
-
-
-
14
-
-
-
1
2
-
44
-
-
-
-
-
-
17
-
2
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
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14
-
-
-
-
1
2
-
-
-
-
-
-
17
-
2
-
-
-
-
-
1
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-
-
-
-
-
-
-
-
171774
Imai
Isolation and properties of a ...
Azotobacter vinelandii, Azotobacter vinelandii O, Escherichia coli
J. Biochem.
85
887-899
1979
9
-
-
-
-
1
9
4
-
-
2
3
-
4
-
-
1
-
-
-
3
2
8
-
-
1
-
-
-
1
-
-
-
2
-
-
9
-
-
-
-
-
1
-
9
2
4
-
-
2
3
-
-
-
1
-
-
3
2
8
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
171775
Andreoli
The pyridine nucleotide cycle: ...
Escherichia coli
Biochem. Biophys. Res. Commun.
49
264-269
1972
-
-
-
-
-
-
-
-
1
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1
-
1
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1
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1
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2
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1
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1
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1
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1
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2
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