EC Number   |
General Information |
Reference |
|---|
    2.4.2.9 | evolution |
UPRT is an enzyme that is highly conserved across species and has been characterized in several organisms, from prokaryotes to human |
-, 759853 |
| 2.4.2.9 | malfunction |
gene upp disruption does not affect Mycobacterium tuberculosis growth in Middlebrook 7H9 medium, and it is not required for Mycobacterium tuberculosis virulence in a mouse model of infection |
-, 759202 |
| 2.4.2.9 | malfunction |
the pyrimidine auxotroph Ashbya gossypii mutant Agura3 shows hypersensitivity to uracil. The mutant's growth can be restored by uridine. In silico analysis of the AgUPRT does not highlight any particular feature that can account for limitations in its enzymatic activity |
-, 759853 |
| 2.4.2.9 | metabolism |
the enzyme is involved in the metabolism of uracil and related compounds in plants catalyzing the uracil salvage, which is of major importance for plant development, overview |
706237 |
| 2.4.2.9 | physiological function |
UPRTs, on-essential, energy-saving enzymes, are involved in the salvage of pyrimidines by catalyzing the formation of uridine monophosphate from uracil and phosphoribosylpyrophosphate. Uracil salvage is of major importance for plant development, especially early development |
706237 |
| 2.4.2.9 | physiological function |
uracil phosphoribosyltransferase (UPRT) catalyzes the reversible transfer of the 5-phosphoribosyl group from 5-phospho-alpha-D-ribosyl1-diphosphate (PRPP) to uracil N1 to form uridine-5'-monophosphate, UMP, in the presence of Mg2+. Nucleosides are essential metabolites in numerous biochemical processes in all living organisms |
758849 |
| 2.4.2.9 | physiological function |
uracil phosphoribosyltransferase (UPRT) is the pyrimidine salvage pathway enzyme responsible for converting uracil to uridine monophosphate in the presence of phosphoribosyl pyrophosphate (PRPP). Uracil-mediated regulation mechanism of the UPRT activity |
-, 759853 |
| 2.4.2.9 | physiological function |
uracil phosphoribosyltransferase from Mycobacterium tuberculosis (MtUPRT) converts uracil and 5-phosphoribosyl-alpha-1-diphosphate into diphosphate and uridine 5'-monophosphate, the precursor of all pyrimidine nucleotides. Although MtUPRT is a key enzyme of the pyrimidine salvage pathway, as it directly synthetizes UMP from uracil, its levels remain constant under hypoxic conditions. Accordingly, MtUPRT does not appear to play a significant role in the non-replicating latent stage of Mycobacterium tuberculosis in vitro. In addition, the upp gene is not required for the full virulence of Mycobacterium tuberculosis in mice in the model tested. In conclusion, MtUPRT is unlikely to be a good target for anti-tuberculosis drug development |
-, 759202 |
