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Literature summary for 2.7.6.1 extracted from
- Phosphoribosylpyrophosphate synthetase and the regulation of phosphoribosylpyrophosphate production in human cells (2001), Prog. Nucleic Acid Res. Mol. Biol., 69, 115-148.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| phosphate | - |
Bacillus subtilis |  |
| phosphate | specific and absolute requirement | Homo sapiens | |
| phosphate | its removal results in complete but reversible loss of activity | Homo sapiens | |
| sulfate | can partially replace phosphate in activation | Homo sapiens | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of isoenzymes PRSI and PRSII in Escherichia coli | Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| in the presence of Mg2+ | Bacillus subtilis |
General Stability
| General Stability | Organism |
|---|---|
| PRSII undergoes substantial immediate but reversible inactivation when diluted in phosphate buffer lacking Mg2+ and ATP | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 2,3-diphosphoglycerate | inhibition, even in the presence of stabilizing agents such as albumin, EDTA and dithiothreitol | Homo sapiens | |
| ADP | the most effective | Bacillus subtilis | |
| ADP | even in the presence of stabilizing agents such as albumin, EDTA and dithiothreitol; the most effective | Homo sapiens | |
| Ca2+ | - |
Homo sapiens | |
| GDP | - |
Bacillus subtilis | |
| GDP | even in the presence of stabilizing agents such as albumin, EDTA and dithiothreitol | Homo sapiens | |
| additional information | pyrimidine, pyridine and purine nucleotides and reaction products | Homo sapiens | |
| PRPP synthetase-associated proteins | inhibit catalytic and perhaps regulatory functions of the enzyme | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.021 | - |
ATP | pH and temperature conditions not mentioned, rPRSI isoenzyme | Homo sapiens | |
| 0.021 | - |
ATP | ATP in form of MgATP2- | Homo sapiens | |
| 0.052 | - |
D-ribose 5-phosphate | pH and temperature conditions not mentioned, rPRSI isoenzyme | Homo sapiens | |
| 0.083 | - |
D-ribose 5-phosphate | pH and temperature conditions not mentioned, rPRSII isoenzyme | Homo sapiens | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Cd2+ | can partially replace Mg2+ | Homo sapiens | |
| Mg2+ | requirement | Bacillus subtilis | |
| Mg2+ | requirement | Homo sapiens | |
| Mg2+ | required to form a complex with ATP and as a free cation | Bacillus subtilis | |
| Mg2+ | required to form a complex with ATP and as a free cation | Homo sapiens | |
| Mg2+ | the most effective | Bacillus subtilis | |
| Mg2+ | the most effective | Homo sapiens | |
| Mn2+ | can partially replace Mg2+ | Bacillus subtilis | |
| Mn2+ | can partially replace Mg2+ | Homo sapiens | |
| additional information | absolute requirement for a divalent cation for activity | Bacillus subtilis | |
| additional information | absolute requirement for a divalent cation for activity | Homo sapiens |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| additional information | - |
enzyme occurs in multiple states of aggregation | Homo sapiens |
| 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 |
| 34600 | - |
x * 34600, isoenzyme PRSII | Homo sapiens |
| 34700 | - |
x * 34700, isoenzyme PRSI | Homo sapiens |
| 1000000 | - |
HPLC, in the presence of Mg2+ and ATP | Homo sapiens |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | |
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
| Homo sapiens | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate | sequential kinetic mechanism | Bacillus subtilis | |
| ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate | sequential kinetic mechanism | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| erythrocyte | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + D-ribose 5-phosphate | - |
Bacillus subtilis | AMP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
r | |
| 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 | |
| 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 | |
| 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 | |
| ATP + ribulose-5-phosphate | - |
Homo sapiens | AMP + 5-phospho-ribulose-1-diphosphate | - |
r | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 34700, isoenzyme PRSI | Homo sapiens |
| ? | x * 34600, isoenzyme PRSII | Homo sapiens |
| More | three catalytic isoenzymes of identical length and two PRPP synthetase-associated proteins of 39000 and 41000 Da | Homo sapiens |
| More | the functional form of the enzyme is a homohexamer | Bacillus subtilis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
isoenzyme PRSII is more thermolabile than PRSI | Homo sapiens |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.01 | - |
ADP | pH conditions and temperature conditions not mentioned | Homo sapiens | |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Homo sapiens | isoenzyme PRSII | - |
6.6 |
| Homo sapiens | isoenzyme PRSI | - |
6.8 |
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