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Literature summary for 2.4.2.9 extracted from

  • Schumacher, M.A.; Bashor, C.J.; Song, M.H.; Otsu, K.; Zhu, S.; Parry, R.J.; Ullman, B.; Brennan, R.G.
    The structural mechanism of GTP stabilized oligomerization and catalytic activation of the Toxoplasma gondii uracil phosphoribosyltransferase (2002), Proc. Natl. Acad. Sci. USA, 99, 78-83.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.2.9

Activating Compound

Activating Compound Comment Organism Structure
GTP activation, stabilization of the tetrameric structure at 2 mM, without GTP enzyme forms dimers Toxoplasma gondii
GTP about 5-7fold increase of Km for 5-phosphoribose 1-diphosphate, unaltered Vmax Toxoplasma gondii

Cloned(Commentary)

Cloned (Comment) Organism
functional overexpression in Escherichia coli JM109 Toxoplasma gondii
wild-type and mutant C128V Toxoplasma gondii

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop-vapour diffusion method, enzyme complexed with uracil and 5-phosphoribose 1-diphosphate, 20 mg/ml, mixing of equal volumes, 15 mM sodium citrate/phosphate, 0.2 M NaCl, pH 4.7, 10% polyethylene glycol 3400, X-ray diffraction structure analysis, dynamic light scattering Toxoplasma gondii

Protein Variants

Protein Variants Comment Organism
C128V site-directed mutagenesis, required for structural sudy Toxoplasma gondii
K150A site-directed mutagenesis, slightly reduced kcat, increased Km for 5-phosphoribose 1-diphosphate in presence of GTP, structural sudy Toxoplasma gondii
K59A site-directed mutagenesis, slightly enhanced kcat, increased Km for 5-phosphoribose 1-diphosphate in presence of GTP, structural sudy Toxoplasma gondii
R68A site-directed mutagenesis, slightly reduced kcat, increased Km for 5-phosphoribose 1-diphosphate in presence of GTP, structural sudy Toxoplasma gondii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km-values, recombinant mutant enzymes Toxoplasma gondii
0.037
-
 5-phospho-alpha-D-ribose 1-diphosphate recombinant wild-type, with GTP Toxoplasma gondii
0.216
-
 5-phospho-alpha-D-ribose 1-diphosphate recombinant wild-type, without GTP Toxoplasma gondii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
uracil + 5-phospho-alpha-D-ribose 1-diphosphate Toxoplasma gondii pyrimidine salvage enzyme, no de novo synthesis of pyrmidines UMP + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Toxoplasma gondii Q26998
-
-

Reaction

Reaction Comment Organism Reaction ID
UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate sequential reaction mechanism Toxoplasma gondii
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
uracil + 5-phospho-alpha-D-ribose 1-diphosphate transfer to N1 of uracil Toxoplasma gondii UMP + diphosphate
-
 ?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate 5-phospho-alpha-D-ribose 1-diphosphate binding site Toxoplasma gondii UMP + diphosphate
-
 ?
uracil + 5-phospho-alpha-D-ribose 1-diphosphate pyrimidine salvage enzyme, no de novo synthesis of pyrmidines Toxoplasma gondii UMP + diphosphate
-
 ?

Subunits

Subunits Comment Organism
More three-dimensional structure Toxoplasma gondii
More a tetramer of 2 dimers, equilibrium between dimeric and tetrameric form Toxoplasma gondii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information recombinant wild-type and mutant enzymes Toxoplasma gondii