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Literature summary extracted from

  • Parkin, D.W.; Mentch, F.; Banks, G.A.; Horenstein, B.A.; Schramm, V.L.
    Transition-state analysis of a Vmax mutant of AMP nucleosidase by the application of heavy-atom kinetic isotope effects (1991), Biochemistry, 30, 4586-4594.
    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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.2.4 8-bromo-AMP
-
 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 Vmax mutant AMP nucleosidase 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 0.6
-
 mutant enzyme 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 ?
-
 ?