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Literature summary extracted from

  • Yata, V.; Sen, K.; Kumar, M.; Ghosh, S.
    Interaction studies of E. coli uracil phosphoribosyltransferase with 5-fluorouracil for potent anti cancer activity (2012), Med. Chem. Res., 21, 1149-1155.
No PubMed abstract available

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.2.9 computational docking of inhibitor 5-fluorouracil to the active site of the enzyme. 5-fluorouracil forms hydrogen bonds with residues Tyr192, Gly196, and Leu197 in the complex. 5-fluorouracil shows low average free energy binding with the enzyme which indicates stronger binding than the natural substrate uracil Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.9 5-fluorouracil competitive Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.2.9 23000
-
 x * 23000, SDS-PAGE Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.9 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.2.9
-
 Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.2.9 11.4
-
 pH 7.3, 37°C Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.9 uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
 Escherichia coli UMP + diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.2.9 ? x * 23000, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.4.2.9 UPRT
-
 Escherichia coli

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.4.2.9 0.013
-
 pH 7.3, 37°C Escherichia coli 5-fluorouracil