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Literature summary extracted from

  • Villela, A.D.; Pham, H.; Jones, V.; Grzegorzewicz, A.E.; Rodrigues-Junior, V.D.; Campos, M.M.; Basso, L.A.; Jackson, M.; Santos, D.S.
    Analysis of uracil phosphoribosyltransferase expression in Mycobacterium tuberculosis and evaluation of upp knockout strain in infected mice (2017), FEMS Microbiol. Lett., 364, gnx023 .
    View publication on PubMed

Application

EC Number Application Comment Organism
2.4.2.9 additional information MtUPRT is unlikely to be a good target for drugs against Mycobacterium tuberculosis Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.2.9 gene upp, recombinant expression, the basal level of MtUPRT expression is independent of either growth medium used, addition of bases, or oxygen presence/absence Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
2.4.2.9 additional information generation of an upp knockout strain by allelic replacement (using the pPR27xylE plasmid, which contains a thermosensitive origin of replication, the xylE reporter gene and the sacB counterselectable marker), evaluation of it in infected mice. Knockout and complemented strains are validated by a functional assay of uracil incorporation. Recombinant expression of Mycobacterium smegmatis gene upp in Mycobacterium tuberculosis wild-type strain H37Rv, resulting in strain CP, and in the upp knockout (KO) variant of H37Rv. Swiss male mice are infected intravenously with 5 × 105 colony forming units (CFU) of Mycobacterium tuberculosis H37Rv wild-type, knockout, or CP strains Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.9 additional information MtUPRT is unlikely to be a good target for drugs against Mycobacterium tuberculosis Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.2.9 UMP + diphosphate Mycobacterium tuberculosis
-
 uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
2.4.2.9 UMP + diphosphate Mycobacterium tuberculosis H37Rv
-
 uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
2.4.2.9 UMP + diphosphate Mycobacterium tuberculosis ATCC 25618
-
 uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.9 Mycobacterium tuberculosis P9WFF3
-
-
2.4.2.9 Mycobacterium tuberculosis ATCC 25618 P9WFF3
-
-
2.4.2.9 Mycobacterium tuberculosis H37Rv P9WFF3
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.9 UMP + diphosphate
-
 Mycobacterium tuberculosis uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
2.4.2.9 UMP + diphosphate
-
 Mycobacterium tuberculosis H37Rv uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
2.4.2.9 UMP + diphosphate
-
 Mycobacterium tuberculosis ATCC 25618 uracil + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.2.9 MtUPRT
-
 Mycobacterium tuberculosis
2.4.2.9 Rv3309c
-
 Mycobacterium tuberculosis
2.4.2.9 UPP
-
 Mycobacterium tuberculosis

General Information

EC Number General Information Comment Organism
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 Mycobacterium tuberculosis
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 Mycobacterium tuberculosis