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Literature summary 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)

EC Number Crystallization (Comment) Organism
2.7.6.1 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

EC Number Metals/Ions Comment Organism Structure
2.7.6.1 Mg2+ required Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.6.1 34288
-
-
Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.7.6.1 Escherichia coli P0A717
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
2.7.6.1 phosphoribosyl pyrophosphate synthetase
-
Escherichia coli
2.7.6.1 PRPPS
-
Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.6.1 ATP
-
Escherichia coli

General Information

EC Number General Information Comment Organism
2.7.6.1 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
2.7.6.1 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