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
-
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
- 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
results (
results (Inhibitors
Inhibitors on EC 2.4.2.9 - uracil phosphoribosyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
CTP
-
powerful inhibitor in combination with UMP. CTP and UMP can be bound simultaneously
CTP
inhibitory allosteric regulation by CTP. 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, two flexible loops. In the inhibited state, residues, Tyr123 and Lys125 contribute to the configuration of the active site for UMP rather than PRPP binding. The C-terminal Gly216 participates in a hydrogen-bond network in the dimer interface that stabilizes the inhibited, but not the activated, state
diphosphate
-
noncompetitive against uracil, competitive against 5-phosphoribose 1-diphosphate
UMP
-
powerful inhibitor in combination with CTP. CTP and UMP can be bound simultaneously
additional information
-
not significantly activated or inhibited by ATP, UTP, and CTP
-
additional information
MtUPRT is unlikely to be a good target for drugs against Mycobacterium tuberculosis
-
additional information
-
MtUPRT is unlikely to be a good target for drugs against Mycobacterium tuberculosis
-
additional information
-
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
-
additional information
-
no inhibition by cytosine, orotic acid, 6-azauracil
-
additional information
-
no inhibition by thymine, cytosine, orotic acid, and hypoxanthine
-
