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show all sequences of 3.2.2.14

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
Activating Compound
Commentary
Organism
Structure
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
General Stability
Organism
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
Inhibitors
Commentary
Organism
Structure
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]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
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]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
213000
-
gel filtration, Sephadex G-200
Azotobacter vinelandii
240000
-
gel filtration, Sepharose 6B
Azotobacter vinelandii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Azotobacter vinelandii
-
-
-
Azotobacter vinelandii O
-
-
-
Escherichia coli
-
-
-
Purification (Commentary)
Commentary
Organism
partially from sonic extract, purified enzyme loses over 90% of its activity after Sephadex G-200 treatment
Azotobacter vinelandii
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.0051
-
-
Escherichia coli
0.0069
-
-
Escherichia coli
0.0195
-
-
Azotobacter vinelandii
Storage Stability
Storage Stability
Organism
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)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
39
-
-
Azotobacter vinelandii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
9
-
Azotobacter vinelandii
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
3
-
p-chloromercuribenzoate
-
Azotobacter vinelandii
80
-
N-ethylmaleimide
-
Azotobacter vinelandii
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
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)
General Stability
Organism
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)
Inhibitors
Commentary
Organism
Structure
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)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
3
-
p-chloromercuribenzoate
-
Azotobacter vinelandii
80
-
N-ethylmaleimide
-
Azotobacter vinelandii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
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)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
213000
-
gel filtration, Sephadex G-200
Azotobacter vinelandii
240000
-
gel filtration, Sepharose 6B
Azotobacter vinelandii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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)
Commentary
Organism
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)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.0051
-
-
Escherichia coli
0.0069
-
-
Escherichia coli
0.0195
-
-
Azotobacter vinelandii
Storage Stability (protein specific)
Storage Stability
Organism
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)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
39
-
-
Azotobacter vinelandii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
9
-
Azotobacter vinelandii
Other publictions for EC 3.2.2.14
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
732384
Ashihara
Pyridine metabolism in tea pla ...
Camellia sinensis
J. Plant Res.
125
781-791
2012
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
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-
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1
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-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
171776
Denicola-Seoane
Studies of NAD kinase and NMN: ...
Haemophilus influenzae, Haemophilus influenzae RD
J. Gen. Microbiol.
136
425-430
1990
-
-
-
-
-
-
-
-
-
-
-
2
-
7
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
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-
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-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
171769
Imai
Properties of allosteric nicot ...
Azotobacter vinelandii
J. Biochem.
101
163-173
1987
3
-
-
-
-
-
4
1
-
-
3
1
-
2
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
4
-
1
-
-
3
1
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
171770
Imai
Isolation and characterization ...
Azotobacter vinelandii
J. Biochem.
101
153-161
1987
2
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
171771
Wagner
The pyridine-nucleotide cycle ...
Nicotiana tabacum
Planta
167
226-232
1986
-
-
-
-
-
-
-
1
-
-
-
1
-
1
-
-
1
-
-
1
-
-
1
-
-
-
-
-
-
-
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-
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-
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-
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1
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1
-
-
-
1
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
171772
Wagner
Regulation in tobacco callus o ...
Nicotiana tabacum
Planta
168
408-413
1986
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
-
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1
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-
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-
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-
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-
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-
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-
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-
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1
-
-
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-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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
-
43
-
-
-
-
-
-
17
-
2
-
-
-
-
-
1
-
-
-
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-
-
-
14
-
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-
-
1
2
-
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-
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17
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
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
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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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