show Isolation and properties of a glycohydrolase specific for nicotinamide mononucleotide from Azotobacter vinelandii
Imai, T.; J. Biochem. 85, 887-899 (1979)
Data extracted from this reference:
Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
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
EC Number
General Stability
Organism
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
EC Number
Inhibitors
Commentary
Organism
Structure
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]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
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]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
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)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
3.2.2.14
Azotobacter vinelandii
-
-
-
3.2.2.14
Azotobacter vinelandii O
-
-
-
3.2.2.14
Escherichia coli
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
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]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
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
EC Number
Storage Stability
Organism
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)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.2.2.14
39
-
-
Azotobacter vinelandii
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.2.2.14
8.5
9
-
Azotobacter vinelandii
Ki Value [mM]
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
3.2.2.14
3
-
p-chloromercuribenzoate
-
Azotobacter vinelandii
3.2.2.14
80
-
N-ethylmaleimide
-
Azotobacter vinelandii
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
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)
EC Number
General Stability
Organism
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)
EC Number
Inhibitors
Commentary
Organism
Structure
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)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
3.2.2.14
3
-
p-chloromercuribenzoate
-
Azotobacter vinelandii
3.2.2.14
80
-
N-ethylmaleimide
-
Azotobacter vinelandii
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
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)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
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)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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)
EC Number
Commentary
Organism
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)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
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)
EC Number
Storage Stability
Organism
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)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
3.2.2.14
39
-
-
Azotobacter vinelandii
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
3.2.2.14
8.5
9
-
Azotobacter vinelandii