Data extracted from this reference:
Activating Compound
3.2.2.14
ATP
less effective activator than GTP
Azotobacter vinelandii
3.2.2.14
dGMP
Azotobacter vinelandii
3.2.2.14
dGTP
Azotobacter vinelandii
3.2.2.14
GDP
Azotobacter vinelandii
3.2.2.14
GMP
Azotobacter vinelandii
3.2.2.14
GTP
most potent activator
Azotobacter vinelandii
3.2.2.14
guanosine 2'-monophosphate
Azotobacter vinelandii
3.2.2.14
guanosine 3'-monophosphate
Azotobacter vinelandii
3.2.2.14
guanosine 5'-tetraphosphate
most potent activator
Azotobacter vinelandii
General Stability
3.2.2.14
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
3.2.2.14
Cd2+
1 mM
Azotobacter vinelandii
3.2.2.14
Cu2+
1 mM
Azotobacter vinelandii
3.2.2.14
dCMP
effective inhibition in presence of 1 mM GTP, noncompetitive inhibitor
Azotobacter vinelandii
3.2.2.14
dGMP
effective inhibition in presence of 1 mM GTP, noncompetitive inhibitor
Azotobacter vinelandii
3.2.2.14
EDTA
1 mM inhibits NMN hydrolysis by 30%
Azotobacter vinelandii
3.2.2.14
GMP
effective inhibition in presence of 1 mM GTP
Azotobacter vinelandii
3.2.2.14
N-ethylmaleimide
50% inhibition at 80 mM
Azotobacter vinelandii
3.2.2.14
p-chloromercuribenzoate
50% inhibition at 3 mM
Azotobacter vinelandii
3.2.2.14
Zn2+
1 mM
Azotobacter vinelandii
KM Value [mM]
3.2.2.14
2
nicotinamide mononucleotide
in absence of GTP
Azotobacter vinelandii
3.2.2.14
4
nicotinamide mononucleotide
0.52 mM dGTP as effector
Azotobacter vinelandii
3.2.2.14
4.4
nicotinamide mononucleotide
0.5 mM guanosine 5'-tetraphosphate as effector
Azotobacter vinelandii
3.2.2.14
4.5
nicotinamide mononucleotide
0.5 mM/1 mM GTP
Azotobacter vinelandii
Molecular Weight [Da]
3.2.2.14
213000
gel filtration, Sephadex G-200
Azotobacter vinelandii
3.2.2.14
240000
gel filtration, Sepharose 6B
Azotobacter vinelandii
Natural Substrates/ Products (Substrates)
3.2.2.14
nicotinamide mononucleotide + H2O
Escherichia coli
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
?
3.2.2.14
nicotinamide mononucleotide + H2O
Azotobacter vinelandii
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
?
3.2.2.14
nicotinamide mononucleotide + H2O
Azotobacter vinelandii O
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
?
Organism
3.2.2.14
Azotobacter vinelandii
3.2.2.14
Azotobacter vinelandii O
3.2.2.14
Escherichia coli
Purification (Commentary)
3.2.2.14
partially from sonic extract, purified enzyme loses over 90% of its activity after Sephadex G-200 treatment
Azotobacter vinelandii
Specific Activity [micromol/min/mg]
3.2.2.14
0.0051
Escherichia coli
3.2.2.14
0.0069
Escherichia coli
3.2.2.14
0.0195
Azotobacter vinelandii
Storage Stability
3.2.2.14
0 to -16°C stored for a month without significant loss of activity
Azotobacter vinelandii
3.2.2.14
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)
3.2.2.14
nicotinamide mononucleotide + H2O
171774
Escherichia coli
nicotinamide + ribose 5-phosphate
171774
Escherichia coli
3.2.2.14
nicotinamide mononucleotide + H2O
irreversible hydrolysis of the N-ribosidic linkage of NMN
171774
Azotobacter vinelandii
nicotinamide + ribose 5-phosphate
171774
Azotobacter vinelandii
ir
3.2.2.14
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
3.2.2.14
nicotinamide mononucleotide + H2O
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
171774
Escherichia coli
?
3.2.2.14
nicotinamide mononucleotide + H2O
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
171774
Azotobacter vinelandii
?
3.2.2.14
nicotinamide mononucleotide + H2O
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
171774
Azotobacter vinelandii O
?
3.2.2.14
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
?
3.2.2.14
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]
3.2.2.14
39
Azotobacter vinelandii
pH Optimum
3.2.2.14
8.5
9
Azotobacter vinelandii
Ki Value [mM]
3.2.2.14
3
p-chloromercuribenzoate
Azotobacter vinelandii
3.2.2.14
80
N-ethylmaleimide
Azotobacter vinelandii
Activating Compound (protein specific)
3.2.2.14
ATP
less effective activator than GTP
Azotobacter vinelandii
3.2.2.14
dGMP
Azotobacter vinelandii
3.2.2.14
dGTP
Azotobacter vinelandii
3.2.2.14
GDP
Azotobacter vinelandii
3.2.2.14
GMP
Azotobacter vinelandii
3.2.2.14
GTP
most potent activator
Azotobacter vinelandii
3.2.2.14
guanosine 2'-monophosphate
Azotobacter vinelandii
3.2.2.14
guanosine 3'-monophosphate
Azotobacter vinelandii
3.2.2.14
guanosine 5'-tetraphosphate
most potent activator
Azotobacter vinelandii
General Stability (protein specific)
3.2.2.14
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)
3.2.2.14
Cd2+
1 mM
Azotobacter vinelandii
3.2.2.14
Cu2+
1 mM
Azotobacter vinelandii
3.2.2.14
dCMP
effective inhibition in presence of 1 mM GTP, noncompetitive inhibitor
Azotobacter vinelandii
3.2.2.14
dGMP
effective inhibition in presence of 1 mM GTP, noncompetitive inhibitor
Azotobacter vinelandii
3.2.2.14
EDTA
1 mM inhibits NMN hydrolysis by 30%
Azotobacter vinelandii
3.2.2.14
GMP
effective inhibition in presence of 1 mM GTP
Azotobacter vinelandii
3.2.2.14
N-ethylmaleimide
50% inhibition at 80 mM
Azotobacter vinelandii
3.2.2.14
p-chloromercuribenzoate
50% inhibition at 3 mM
Azotobacter vinelandii
3.2.2.14
Zn2+
1 mM
Azotobacter vinelandii
Ki Value [mM] (protein specific)
3.2.2.14
3
p-chloromercuribenzoate
Azotobacter vinelandii
3.2.2.14
80
N-ethylmaleimide
Azotobacter vinelandii
KM Value [mM] (protein specific)
3.2.2.14
2
nicotinamide mononucleotide
in absence of GTP
Azotobacter vinelandii
3.2.2.14
4
nicotinamide mononucleotide
0.52 mM dGTP as effector
Azotobacter vinelandii
3.2.2.14
4.4
nicotinamide mononucleotide
0.5 mM guanosine 5'-tetraphosphate as effector
Azotobacter vinelandii
3.2.2.14
4.5
nicotinamide mononucleotide
0.5 mM/1 mM GTP
Azotobacter vinelandii
Molecular Weight [Da] (protein specific)
3.2.2.14
213000
gel filtration, Sephadex G-200
Azotobacter vinelandii
3.2.2.14
240000
gel filtration, Sepharose 6B
Azotobacter vinelandii
Natural Substrates/ Products (Substrates) (protein specific)
3.2.2.14
nicotinamide mononucleotide + H2O
Escherichia coli
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
?
3.2.2.14
nicotinamide mononucleotide + H2O
Azotobacter vinelandii
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
?
3.2.2.14
nicotinamide mononucleotide + H2O
Azotobacter vinelandii O
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
?
Purification (Commentary) (protein specific)
3.2.2.14
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)
3.2.2.14
0.0051
Escherichia coli
3.2.2.14
0.0069
Escherichia coli
3.2.2.14
0.0195
Azotobacter vinelandii
Storage Stability (protein specific)
3.2.2.14
0 to -16°C stored for a month without significant loss of activity
Azotobacter vinelandii
3.2.2.14
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)
3.2.2.14
nicotinamide mononucleotide + H2O
171774
Escherichia coli
nicotinamide + ribose 5-phosphate
171774
Escherichia coli
3.2.2.14
nicotinamide mononucleotide + H2O
irreversible hydrolysis of the N-ribosidic linkage of NMN
171774
Azotobacter vinelandii
nicotinamide + ribose 5-phosphate
171774
Azotobacter vinelandii
ir
3.2.2.14
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
3.2.2.14
nicotinamide mononucleotide + H2O
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
171774
Escherichia coli
?
3.2.2.14
nicotinamide mononucleotide + H2O
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
171774
Azotobacter vinelandii
?
3.2.2.14
nicotinamide mononucleotide + H2O
conversion to nicotinamide as a precursor of NAD+ via nicotinic acid
171774
Azotobacter vinelandii O
?
3.2.2.14
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
?
3.2.2.14
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)
3.2.2.14
39
Azotobacter vinelandii
pH Optimum (protein specific)
3.2.2.14
8.5
9
Azotobacter vinelandii