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Literature summary for 3.2.2.4 extracted from

  • Giranda, V.L.; Berman, H.M.; Schramm, V.L.
    Crystallization and preliminary X-ray study of AMP nucleosidase (1986), J. Biol. Chem., 261, 15307-15309.
    View publication on PubMed

Activating Compound

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

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
tetramer Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Formycin monophosphate
-
Azotobacter vinelandii
Formycin monophosphate
-
Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52000
-
4 * 52000, gel electrophoresis Escherichia coli
208000
-
PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
-
-
-
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
47
-
-
Escherichia coli

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
tetramer 4 * 52000, gel electrophoresis Escherichia coli