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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
34288 | - |
- |
Escherichia coli |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A717 | - |
- |
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 | Comment | Organism |
---|---|---|
More | x * 34288, sequence calculation, three-dimensional structure analysis | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
phosphoribosyl pyrophosphate synthetase | - |
Escherichia coli |
PRPPS | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Escherichia coli |
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 |