Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Imai, T.
    Isolation and properties of a glycohydrolase specific for nicotinamide mononucleotide from Azotobacter vinelandii (1979), J. Biochem., 85, 887-899.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment 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 Comment 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 Comment 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] Comment 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 Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment Textmining
3.2.2.14 Azotobacter vinelandii
-
-
-
3.2.2.14 Azotobacter vinelandii O
-
-
-
3.2.2.14 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) 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] Comment 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.14 nicotinamide mononucleotide + H2O
-
Escherichia coli nicotinamide + ribose 5-phosphate
-
?
3.2.2.14 nicotinamide mononucleotide + H2O irreversible hydrolysis of the N-ribosidic linkage of NMN Azotobacter vinelandii nicotinamide + ribose 5-phosphate
-
ir
3.2.2.14 nicotinamide mononucleotide + H2O irreversible hydrolysis of the N-ribosidic linkage of NMN Azotobacter vinelandii O nicotinamide + ribose 5-phosphate
-
ir
3.2.2.14 nicotinamide mononucleotide + H2O conversion to nicotinamide as a precursor of NAD+ via nicotinic acid Escherichia coli ?
-
?
3.2.2.14 nicotinamide mononucleotide + H2O conversion to nicotinamide as a precursor of NAD+ via nicotinic acid Azotobacter vinelandii ?
-
?
3.2.2.14 nicotinamide mononucleotide + H2O conversion to nicotinamide as a precursor of NAD+ via nicotinic acid Azotobacter vinelandii O ?
-
?
3.2.2.14 nicotinic acid mononucleotide + H2O NaNM reaction slowly, 8% hydrolysis of the rate of NMN Azotobacter vinelandii nicotinic acid + ribose 5-phosphate
-
?
3.2.2.14 nicotinic acid mononucleotide + H2O NaNM reaction slowly, 8% hydrolysis of the rate of NMN Azotobacter vinelandii O nicotinic acid + ribose 5-phosphate
-
?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.2.14 39
-
-
Azotobacter vinelandii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.2.14 8.5 9
-
Azotobacter vinelandii

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.2.14 3
-
p-chloromercuribenzoate
-
Azotobacter vinelandii
3.2.2.14 80
-
N-ethylmaleimide
-
Azotobacter vinelandii