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Literature summary for 3.2.2.4 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

Activating Compound Comment Organism Structure
ATP
-
Azotobacter vinelandii
MnATP2-
-
Azotobacter vinelandii

Inhibitors

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

KM Value [mM]

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54000
-
-
Azotobacter vinelandii
320000
-
hexamer Azotobacter vinelandii

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Azotobacter vinelandii

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
hexamer
-
Azotobacter vinelandii