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Literature summary for 2.4.2.10 extracted from

  • McClard, R.W.; Holets, E.A.; MacKinnon, A.L.; Witte, J.F.
    Half-of-sites binding of orotidine 5-phosphate and alpha-D-5-phosphorylribose 1-diphosphate to orotate phosphoribosyltransferase from Saccharomyces cerevisiae supports a novel variant of the Theorell-Chance mechanism with alternating site catalysis (2006), Biochemistry, 45, 5330-5342.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information detailed kinetic analysis, isothermal titration calorimetry, the double Theorell-Chance mechanism yields a steady-state rate equation indistinguishable in form from the observed classical ping-pong bi-bi kinetics, steady-state kinetics, overview Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for substrate binding Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
orotidine 5-phosphate + diphosphate Saccharomyces cerevisiae
-
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate reaction scheme, half-of-sites binding of orotidine 5-phosphate and alpha-D-5-phosphorylribose 1-diphosphate to the enzyme supports an alternative variant of the Theorell-Chance mechanism with alternating site catalysis, in addition to a ping-pong bi-bi kinetic mechanism, overview Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information half-of-sites binding of orotidine 5-phosphate and alpha-D-5-phosphorylribose 1-diphosphate to the enzyme supports an alternative variant of the Theorell-Chance mechanism with alternating site catalysis, overview Saccharomyces cerevisiae ?
-
?
orotidine 5-phosphate + diphosphate
-
Saccharomyces cerevisiae orotate + 5-phospho-alpha-D-ribose 1-diphosphate
-
?
orotidine 5-phosphate + diphosphate the compounds bind very tightly to the enzyme in a Mg2+-dependent manner, overview Saccharomyces cerevisiae orotate + 5-phospho-alpha-D-ribose 1-diphosphate the compounds bind very tightly to the enzyme in a Mg2+-dependent manner, overview ?

Subunits

Subunits Comment Organism
dimer homodimer Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
OPRTase
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Saccharomyces cerevisiae