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Literature summary for 2.7.6.1 extracted from

  • Timofeev, V.; Abramchik, Y.; Zhukhlistova, N.; Kuranova, I.
    Crystallization and preliminary X-ray diffraction study of phosphoribosyl pyrophosphate synthetase from E. coli (2015), Crystallogr. Rep., 60, 685-688.
No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment) Organism
purified enzyme, hanging drop vapor diffusion technique by mixing of 0.001 ml of 10 mg/mL protein in 0.02 M Tris-HCl buffer, pH 7.5, containing 0.04% NaN3, with 0.001 ml of reservoir solution containing from 18% (NH4)2SO4, 0.02 M Tris-HCl buffer, pH 7.5, 0.02 mM MgCl2 and 0.02 mM ATP, screening and optimization to capillary counter-diffusion technique, largest crystals are obtained using a protein solution with a protein concentration of 14 mg/mL in 0.02 M Tris-HCl buffer, pH 7.5, containing 2 mM MgCl2, 2 mM ATP, and 0.04% NaN3, and a reservoir solution composed of 14% ammonium sulfate in 0.1 M Tris buffer, pH 8.5, containing 0.3 M NaCl, 2 mM MgCl2, and 0.04% NaN3, X-ray diffraction structure determination and analysis at 3.1 A resolution Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34288
-
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + D-ribose 5-phosphate Escherichia coli
-
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A717
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-ribose 5-phosphate
-
Escherichia coli AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
?

Subunits

Subunits Comment Organism
More x * 34288, sequence calculation, three-dimensional structure analysis Escherichia coli

Synonyms

Synonyms Comment Organism
phosphoribosyl pyrophosphate synthetase
-
Escherichia coli
PRPPS
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli

General Information

General Information Comment Organism
evolution the enzyme belongs to the phosphoribosyl diphosphate synthetase family, enzymes of this family are widespread in different eukaryotic and prokaryotic organisms and are involved in a number of important biochemical processes associated with purine and pyrimidine metabolism Escherichia coli
physiological function the enzyme produces 5-phosphoribosyl diphosphate which is an essential metabolite and an allosteric regulator in the de novo and salvage pathways of the biosynthesis of purine and pyrimidine nucleotides, pyrimidine-containing enzyme cofactors, and the amino acids histidine and tryptophan. Due to the key role of the enzyme in cell metabolism, the activity of these enzymes is tightly regulated by an excess of the substrate via feedback inhibition, as well as by allosteric interactions through the binding of ADP or GDP molecules in a special site between the subunits of the enzyme Escherichia coli