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2.4.2.9: uracil phosphoribosyltransferase

This is an abbreviated version!
For detailed information about uracil phosphoribosyltransferase, go to the full flat file.

Word Map on EC 2.4.2.9

Reaction

UMP
+
diphosphate
=
Uracil
 +
5-phospho-alpha-D-ribose 1-diphosphate

Synonyms

AFR052C, AFR052Cp, AGOS_AFR052C, AgUPRT, CD-UPRT, cytosine deaminase-uracil phosphoribosyltransferase, cytosine deaminase/uracil phosphoribosyltransferase, More, MtUPRT, phosphoribosyltransferase, uracil, Rv3309c, TtUPRT, TtUPRT3, UK/UPRT1, UMP pyrophosphorylase, UMP:pyrophosphate phosphoribosyltransferase, UPP, UPRT, UPRTase, uracil phosphoribosyl transferase, uridine 5'-phosphate pyrophosphorylase, uridine kinase-like protein (uracil phosphoribosyltransferase), uridine kinase/uracil phosphoribosyltransferase 1, uridine monophosphate pyrophosphorylase, uridylate pyrophosphorylase, uridylic pyrophosphorylase

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.9 uracil phosphoribosyltransferase

Crystallization

Crystallization on EC 2.4.2.9 - uracil phosphoribosyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
sitting drop vapor diffusion method, using 0.1 M sodium acetate trihydrate pH 4.6, 1.5 M sodium formate with a 2:1 reservoir-to-protein solution ratio at 25°C
enzyme in complex with UMP, enzyme in complex with CTP, structure with UMP bound in half of the active sites. Hanging-drop vapour-diffusion method
two structures of the activated state enzyme in complex with GTP, X-ray diffraction structure determination and analysis at 2.8 A resolution, the first structure which contains PRPP in all active sites, and 2.9 A resolution, for the second structure with PRPP in two sites and the hydrolysis products ribose-5-phosphate and diphosphate in the other sites, respectively, and a third structure of the enzyme in complex with UMP and the allosteric inhibitor CTP
hanging drop-vapour diffusion method, enzyme complexed with uracil and 5-phosphoribose 1-diphosphate, 20 mg/ml, mixing of equal volumes, 15 mM sodium citrate/phosphate, 0.2 M NaCl, pH 4.7, 10% polyethylene glycol 3400, X-ray diffraction structure analysis, dynamic light scattering
hanging drop-vapour diffusion technique, 2.0 M ammonium phosphate as precipitant, pH 8.0, room temperature, X-ray diffraction structure analysis, crystals are enzymatically active, wild-type and mutant enzymes
vapour diffusion using hanging or sitting drops, room temperature, protein solution 20 mg/ml, pH 7.0, 5 mM phosphate, 0.003 ml + 0.003 ml reservoir solution, pH 7.5, 6-10% polyethylene glycol 4000, 0.1 M HEPES, crystals appeared after 3 weeks, structure determination and analysis