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Literature summary extracted from

  • Schramm, V.L.; Hochstein, L.I.
    Purification, crystallization, and subunit structure of allosteric adenosine 5¦-monophosphate nucleosidase (1972), Biochemistry, 11, 2777-2783.
    View publication on PubMed

Activating Compound

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.2.4
-
Azotobacter vinelandii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.2.4 325000
-
Archibald approach to equilibrium method Azotobacter vinelandii
3.2.2.4 370000
-
gel filtration and sedimentation velocity experiments 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

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 34
-
-
Azotobacter vinelandii

Storage Stability

EC Number Storage Stability Organism
3.2.2.4 -70°C, dry ice mixture, 1 year 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