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Literature summary extracted from

  • Becker, M.A.
    Phosphoribosylpyrophosphate synthetase and the regulation of phosphoribosylpyrophosphate production in human cells (2001), Prog. Nucleic Acid Res. Mol. Biol., 69, 115-148.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.6.1 phosphate
-
 Bacillus subtilis
2.7.6.1 phosphate specific and absolute requirement Homo sapiens
2.7.6.1 phosphate its removal results in complete but reversible loss of activity Homo sapiens
2.7.6.1 sulfate can partially replace phosphate in activation Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.6.1 expression of isoenzymes PRSI and PRSII in Escherichia coli Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.6.1 in the presence of Mg2+ Bacillus subtilis

General Stability

EC Number General Stability Organism
2.7.6.1 PRSII undergoes substantial immediate but reversible inactivation when diluted in phosphate buffer lacking Mg2+ and ATP Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.6.1 2,3-diphosphoglycerate inhibition, even in the presence of stabilizing agents such as albumin, EDTA and dithiothreitol Homo sapiens
2.7.6.1 ADP the most effective Bacillus subtilis
2.7.6.1 ADP even in the presence of stabilizing agents such as albumin, EDTA and dithiothreitol; the most effective Homo sapiens
2.7.6.1 Ca2+
-
 Homo sapiens
2.7.6.1 GDP
-
 Bacillus subtilis
2.7.6.1 GDP even in the presence of stabilizing agents such as albumin, EDTA and dithiothreitol Homo sapiens
2.7.6.1 additional information pyrimidine, pyridine and purine nucleotides and reaction products Homo sapiens
2.7.6.1 PRPP synthetase-associated proteins inhibit catalytic and perhaps regulatory functions of the enzyme Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.6.1 0.021
-
 ATP pH and temperature conditions not mentioned, rPRSI isoenzyme Homo sapiens
2.7.6.1 0.021
-
 ATP ATP in form of MgATP2- Homo sapiens
2.7.6.1 0.052
-
 D-ribose 5-phosphate pH and temperature conditions not mentioned, rPRSI isoenzyme Homo sapiens
2.7.6.1 0.083
-
 D-ribose 5-phosphate pH and temperature conditions not mentioned, rPRSII isoenzyme Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.6.1 Cd2+ can partially replace Mg2+ Homo sapiens
2.7.6.1 Mg2+ requirement Bacillus subtilis
2.7.6.1 Mg2+ requirement Homo sapiens
2.7.6.1 Mg2+ required to form a complex with ATP and as a free cation Bacillus subtilis
2.7.6.1 Mg2+ required to form a complex with ATP and as a free cation Homo sapiens
2.7.6.1 Mg2+ the most effective Bacillus subtilis
2.7.6.1 Mg2+ the most effective Homo sapiens
2.7.6.1 Mn2+ can partially replace Mg2+ Bacillus subtilis
2.7.6.1 Mn2+ can partially replace Mg2+ Homo sapiens
2.7.6.1 additional information absolute requirement for a divalent cation for activity Bacillus subtilis
2.7.6.1 additional information absolute requirement for a divalent cation for activity Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.6.1 additional information
-
 enzyme occurs in multiple states of aggregation Homo sapiens
2.7.6.1 additional information
-
 reversible aggregation of the enzyme subunits in phosphate buffer depends on the concentration of Mg2+ and ATP and the enzyme activity resides in the largest aggregates Homo sapiens
2.7.6.1 34600
-
 x * 34600, isoenzyme PRSII Homo sapiens
2.7.6.1 34700
-
 x * 34700, isoenzyme PRSI Homo sapiens
2.7.6.1 1000000
-
 HPLC, in the presence of Mg2+ and ATP Homo sapiens

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 Bacillus subtilis the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 r
2.7.6.1 ATP + D-ribose 5-phosphate Homo sapiens the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.6.1 Bacillus subtilis
-
-
-
2.7.6.1 Homo sapiens
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.6.1 ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate sequential kinetic mechanism Bacillus subtilis
a
2.7.6.1 ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate sequential kinetic mechanism Homo sapiens
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.6.1 erythrocyte
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.6.1 ATP + D-ribose 5-phosphate
-
 Bacillus subtilis AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 r
2.7.6.1 ATP + D-ribose 5-phosphate ATP is bound to the enzyme in the form of MgATP2- complex Homo sapiens AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 r
2.7.6.1 ATP + D-ribose 5-phosphate the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan Bacillus subtilis AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 r
2.7.6.1 ATP + D-ribose 5-phosphate the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan Homo sapiens AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 r
2.7.6.1 ATP + ribulose-5-phosphate
-
 Homo sapiens AMP + 5-phospho-ribulose-1-diphosphate
-
 r

Subunits

EC Number Subunits Comment Organism
2.7.6.1 ? x * 34700, isoenzyme PRSI Homo sapiens
2.7.6.1 ? x * 34600, isoenzyme PRSII Homo sapiens
2.7.6.1 More three catalytic isoenzymes of identical length and two PRPP synthetase-associated proteins of 39000 and 41000 Da Homo sapiens
2.7.6.1 More the functional form of the enzyme is a homohexamer Bacillus subtilis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.6.1 additional information
-
 isoenzyme PRSII is more thermolabile than PRSI Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.6.1 0.01
-
 ADP pH conditions and temperature conditions not mentioned Homo sapiens

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.6.1 Homo sapiens isoenzyme PRSII
-
 6.6
2.7.6.1 Homo sapiens isoenzyme PRSI
-
 6.8