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Literature summary for 2.4.2.9 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)

Crystallization (Comment) Organism
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

Inhibitors Comment Organism Structure
5-fluorouracil competitive Escherichia coli

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
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
11.4
-
pH 7.3, 37°C Escherichia coli

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
UPRT
-
Escherichia coli

IC50 Value

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