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Literature summary extracted from

  • Sauve, A.A.; Cahill, S.M.; Zech, S.G.; Basso, L.A.; Lewandowicz, A.; Santos, D.S.; Grubmeyer, C.; Evans, G.B.; Furneaux, R.H.; Tyler, P.C.; McDermott, A.; Girvin, M.E.; Schramm, V.L.
    Ionic States of Substrates and Transition State Analogues at the Catalytic Sites of N-Ribosyltransferases (2003), Biochemistry, 42, 5694-5705.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.2.8 functional expression in Escherichia coli Tritrichomonas suis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.8 immucillin-H transition state analogue, binds tightly to the active site, inhibition mechanism and kinetics Tritrichomonas suis
2.4.2.8 immucillin-H 5'-phosphate transition state analogue, binds tightly to the active site, inhibition mechanism and kinetics Tritrichomonas suis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.8 Mg2+ required Tritrichomonas suis

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.8 Tritrichomonas suis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.2.8 recombinant from Escherichia coli Tritrichomonas suis

Reaction

EC Number Reaction Comment Organism Reaction ID
2.4.2.8 IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate catalytic mechanism Tritrichomonas suis
2.4.2.8 IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate active site structure Tritrichomonas suis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.8 guanine + 5-phospho-alpha-D-ribose 1-diphosphate
-
Tritrichomonas suis GMP + diphosphate
-
r
2.4.2.8 hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
-
Tritrichomonas suis IMP + diphosphate
-
r