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Literature summary for 3.2.2.4 extracted from

  • Schramm, V.L.; Hochstein, L.I.
    Stabilization of allosteric adenosine monophosphate nucleosidase by inorganic salts, substrate, and essential activator (1971), Biochemistry, 10, 3411-3417.
    View publication on PubMed
Search for more literature for 3.2.2.4

Activating Compound

Activating Compound Comment Organism Structure
ATP
-
 Azotobacter vinelandii
MgATP2-
-
 Azotobacter vinelandii

Inhibitors

Inhibitors Comment Organism Structure
phosphate
-
 Azotobacter vinelandii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.08
-
 AMP
-
 Azotobacter vinelandii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
180000
-
 gel filtration, oligomer, inactive enzyme Azotobacter vinelandii
360000
-
 gel filtration, polymer, active enzyme 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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2
-
-
 Azotobacter vinelandii

Storage Stability

Storage Stability Organism
-10°C, Tris-K2SO4-buffer, 2 months 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
polymer
-
 Azotobacter vinelandii