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Literature summary extracted from

  • Skoog, M.T.
    Mechanism and activation for allosteric adenosine 5¦-monophosphate nucleosidase (1986), J. Biol. Chem., 261, 4451-4459.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.2.4 MgATP2-
-
 Azotobacter vinelandii

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.2.4 HPO42-
-
 Azotobacter vinelandii
3.2.2.4 phosphate dissociation to inactive dimers Azotobacter vinelandii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.2.4 AMP + H2O Azotobacter vinelandii
-
 ?
-
 ?
3.2.2.4 NMN + H2O Azotobacter vinelandii
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.2.4 Azotobacter vinelandii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.2.4
-
 Azotobacter vinelandii

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.2.4 120
-
 AMP Azotobacter vinelandii
3.2.2.4 8000
-
 NMN Azotobacter vinelandii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.2.4 AMP + H2O
-
 Azotobacter vinelandii adenine + ribose 5-phosphate
-
 ?
3.2.2.4 AMP + H2O
-
 Azotobacter vinelandii ?
-
 ?
3.2.2.4 NMN + H2O
-
 Azotobacter vinelandii ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.2.4 hexamer
-
 Azotobacter vinelandii

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.2.4 2
-
 NMN
-
 Azotobacter vinelandii
3.2.2.4 60
-
 AMP
-
 Azotobacter vinelandii