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Literature summary for 3.2.2.8 extracted from

  • Minici, C.; Cacciapuoti, G.; De Leo, E.; Porcelli, M.; Degano, M.
    New determinants in the catalytic mechanism of nucleoside hydrolases from the structures of two isozymes from Sulfolobus solfataricus (2012), Biochemistry, 51, 4590-4599.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpressed in Escherichia coli Saccharolobus solfataricus

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure is determined at 1.6 A resolution. The enzyme is crystallized using the hanging drop vapor diffusion method by mixing an equal amount of protein and a precipitant solution, composed of 100 mM bicine (pH 9) and 1.5 M ammonium sulfate Saccharolobus solfataricus

Metals/Ions

Metals/Ions Comment Organism Structure
Na+ likely bound to the enzyme under physiological conditions Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q97ZS5
-
-
Saccharolobus solfataricus P2 Q97ZS5
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
inosine + H2O
-
Saccharolobus solfataricus hypoxanthine + D-ribose
-
?
inosine + H2O
-
Saccharolobus solfataricus P2 hypoxanthine + D-ribose
-
?

Synonyms

Synonyms Comment Organism
pyrimidine-specific nucleoside hydrolase
-
Saccharolobus solfataricus
SsCU-NH
-
Saccharolobus solfataricus
SSO0505
-
Saccharolobus solfataricus