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Literature summary extracted from

  • Schramm, V.L.; Reed, G.H.
    Interaction of Mn2+ and MnATP2- with the allosteric sites of AMP nucleosidase (1980), J. Biol. Chem., 255, 5795-5801.
No PubMed abstract available

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.2.4 ATP
-
 Azotobacter vinelandii
3.2.2.4 MnATP2-
-
 Azotobacter vinelandii

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.2.4 Formycin monophosphate
-
 Azotobacter vinelandii
3.2.2.4 Mn2+
-
 Azotobacter vinelandii
3.2.2.4 phosphate
-
 Azotobacter vinelandii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.2.4 110
-
 AMP saturating concentration of MgATP2- Azotobacter vinelandii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.2.4 54000
-
-
 Azotobacter vinelandii
3.2.2.4 320000
-
 hexamer 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
-
 ?
-
 ?

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

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 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.2.4 hexamer
-
 Azotobacter vinelandii