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
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2.4.2.9
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5-fluorouracil
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pyrimidine
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salvage
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5-fluorocytosine
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suicide
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prodrug
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orotate
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bystander
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5-fluorouridine
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oncolytic
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markerless
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phosphoribosyltransferases
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counterselectable
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flucytosine
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4-thiouracil
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medicine
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virotherapy
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cd/5-fc
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gene-directed
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synthesis
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analysis
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molecular biology
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pharmacology
- 2.4.2.9
- 5-fluorouracil
- pyrimidine
-
salvage
- 5-fluorocytosine
-
suicide
-
prodrug
- orotate
-
bystander
- 5-fluorouridine
-
oncolytic
-
markerless
-
phosphoribosyltransferases
-
counterselectable
-
flucytosine
- 4-thiouracil
- medicine
-
virotherapy
-
cd/5-fc
-
gene-directed
- synthesis
- analysis
- molecular biology
- pharmacology
Reaction
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
2.4.2.9 uracil phosphoribosyltransferaseAdvanced search results
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results (Activating Compound
Activating Compound on EC 2.4.2.9 - uracil phosphoribosyltransferase
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ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
alendronate
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1 mM, increases the initial rate of synthesis of 5-fluoro-UMP 2.5fold, increases the initial rate of synthesis of UMP 2.3fold
clodronate
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1 mM, increases the initial rate of synthesis of 5-fluoro-UMP 2fold, increases the initial rate of synthesis of UMP 1.9fold
etidronate
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1 mM, increases the initial rate of synthesis of 5-fluoro-UMP 2.8fold, increases the initial rate of synthesis of UMP 2.1fold
glutathione
Lactobacillus bifidus
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omission of glutathione reduces the reaction rate about 25%
pamidronate
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1 mM, increases the initial rate of synthesis of 5-fluoro-UMP 2.6fold, increases the initial rate of synthesis of UMP 2.1fold
GTP
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highly activating at low 5-phosphoribose 1-diphosphate concentration, e.g. 0.2 mM, by modification of the structure from dimer/trimer to pentamer/hexamer
GTP
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about 5-7fold increase of Km for 5-phosphoribose 1-diphosphate, unaltered Vmax
GTP
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effect is pH-dependent, pH 7.5: lowers Km value for 5-phospho-alpha-D-ribose 1-diphosphate and increases Vmax 2fold, no effect on Km for uracil, pH 8.0: no effect
GTP
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strong activation at pH 6 and at pH 8. The concentration of GTP required for half-maximal activation is about 0.080 mM
GTP
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strong stimulation, binds cooperatively with 5-phosphoribosyl 1-diphosphate
GTP
activating allosteric regulation by GTP. The regulatory triphosphate binds at a site in the center of the tetramer changing the quaternary arrangement. The effector contacts Pro94 at the beginning of a long beta-strand in the dimer interface, which extends into a flexible loop over the active site. In the GTP-bound state, two flexible loop residues, Tyr123 and Lys125, bind the diphosphate moiety of PRPP in the neighboring subunit and contribute to catalysis. The C-terminal Gly216 participates in a hydrogen-bond network in the dimer interface that stabilizes the inhibited, but not the activated, state
GTP
activation, stabilization of the tetrameric structure at 2 mM, without GTP enzyme forms dimers
GTP
about 5-7fold increase of Km for 5-phosphoribose 1-diphosphate, unaltered Vmax
additional information
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the enzyme undergoes a transition from a weakly active or inactive T-state, favored by binding of UMP and CTP, to an active R-state, favored by binding of GTP and 5-phosphoribosyl 1-diphosphate
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additional information
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no activating effect with methylene biphosphonate
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