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Literature summary extracted from

  • Grabner, G.K.; Switzer, R.L.
    Kinetic studies of the uracil phosphoribosyltransferase reaction catalyzed by the Bacillus subtilis pyrimidine attenuation regulatory protein PyrR (2003), J. Biol. Chem., 278, 6921-6927.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.9 diphosphate product inhibition forward reaction Bacillus subtilis
2.4.2.9 UMP product inhibition, forward reaction Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.9 0.068
-
 5-phospho-alpha-D-ribose 1-diphosphate
-
 Bacillus subtilis
2.4.2.9 0.13
-
 UMP
-
 Bacillus subtilis
2.4.2.9 0.159
-
 Uracil
-
 Bacillus subtilis
2.4.2.9 1
-
 diphosphate
-
 Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.2.9 Mg2+
-
 Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.9 Bacillus subtilis
-
 PyrR protein
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.4.2.9 UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate ping pong steady state kinetic pattern, ordered bi-bi mechanism, model, no formation of the phosphoribosyl-enzyme intermediate predicted by classic ping pong kinetics Bacillus subtilis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.9 additional information no catalysis of exchange reaction between uracil-UMP and diphosphate-5-phospho-alpha-D-ribose 1-diphosphate Bacillus subtilis ?
-
 ?
2.4.2.9 uracil + 5-phospho-alpha-D-ribose 1-diphosphate equilibrium lies far in the direction of UMP formation Bacillus subtilis UMP + diphosphate
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.4.2.9 More PyrR protein is a bifunctional protein, that primarily regulates the expression of pyrimidine biosynthetic pyr genes, but also catalyses the uracil phosphoribosyltransferase reaction, little amino acid sequence similarities to other bacterial UPRTases Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.2.9 37
-
 assay at Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.2.9 0.0015
-
 UMP reverse reaction Bacillus subtilis
2.4.2.9 5.1
-
 Uracil forward reaction Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.2.9 8.7
-
 assay at Bacillus subtilis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.4.2.9 additional information
-
 additional information product inhibition pattern Bacillus subtilis