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Literature summary for 2.7.6.1 extracted from
- Crystal structure of human phosphoribosylpyrophosphate synthetase 1 reveals a novel allosteric site (2007), Biochem. J., 401, 39-47.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| phosphate | - |
Homo sapiens |  |
| phosphate | required for enzymatic activity by class 1 PRSs | Bacillus subtilis | |
| phosphate | required for enzymatic activity by class 1 PRSs | Homo sapiens | |
| sulfate | the SO42- ion, an analogue of the activator phosphate, binds at both the R5P-binding site and the allosteric site defined previously. In addition, an extra SO42- binds at a site at the dimer interface between the ATP-binding site and the allosteric site. Binding of this SO42- stabilizes the conformation of the flexible loop at the active site, leading to the formation of the active, open conformation, which is essential for binding of ATP and initiation of the catalytic reaction, binding structure including residues Asp224, Thr225, Cys226, Gly227 and Thr228, overview | Homo sapiens | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene PRS1 from a cDNA library, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3) | Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging-drop vapour diffusion method | Bacillus subtilis |
| hanging-drop vapour diffusion method | Homo sapiens |
| purified recombinant enzyme in complex with Cd2+, ATP or sulfate, hanging drop vapour diffusion method, 20°C, X-ray diffraction structure determination and analysis at 2.20 A resolution | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| S132A | the mutants show altered ligand binding and regulation at the allosteric site compared to the wild-type enzyme, comparison of crystal structures, overview | Homo sapiens |
| Y146M | the mutants show altered ligand binding and regulation at the allosteric site compared to the wild-type enzyme, comparison of crystal structures, overview | Homo sapiens |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| ADP | allosterical inhibition | Bacillus subtilis | |
| ADP | allosterical inhibition | Homo sapiens | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Cd2+ | can serve as substitutes for Mg2+ with relatively lower activity | Homo sapiens | |
| Cd2+ | a Cd2+ ion binds at the active site and in a position to interact with the beta- and gamma-phosphates of ATP | Homo sapiens | |
| Co2+ | can serve as substitutes for Mg2+ with relatively lower activity | Homo sapiens | |
| Mg2+ | - |
Homo sapiens | |
| Mg2+ | Mg2+ is required for enzymatic activity by class 1 PRSs. Mg2+ forms a complex with ATP (MgATP2-) to act as the actual substrate of the enzyme. | Bacillus subtilis | |
| Mg2+ | Mg2+ is required for enzymatic activity by class 1 PRSs. Mg2+ forms a complex with ATP (MgATP2-) to act as the actual substrate of the enzyme. | Homo sapiens | |
| Mn2+ | can serve as substitutes for Mg2+ with relatively lower activity | Homo sapiens | |
| Ni2+ | can serve as substitutes for Mg2+ with relatively lower activity | Homo sapiens | |
| SO42- | A SO42- ion, an analogue of the activator phosphate, is found to bind at both the R5P-binding site and the allosteric site defined previously. In addition, an extra SO42- binds at a site at the dimer interface between the ATP-binding site and the allosteric site. Binding of this SO42- stabilizes the conformation of the flexible loop at the active site, leading to the formation of the active, open conformation which is essential for binding of ATP and initiation of the catalytic reaction. | Bacillus subtilis | |
| SO42- | A SO42- ion, an analogue of the activator phosphate, was found to bind at both the R5P-binding site and the allosteric site defined previously. In addition, an extra SO42- binds at a site at the dimer interface between the ATP-binding site and the allosteric site. Binding of this SO42- stabilizes the conformation of the flexible loop at the active site, leading to the formation of the active, open conformation which is essential for binding of ATP and initiation of the catalytic reaction. | Homo sapiens | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + D-ribose 5-phosphate | Homo sapiens | the enzymatic activity of PRS is regulated by both the activator phosphate and the inhibitor ADP competing for binding at a common allosteric regulatory site | AMP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| D-ribose 5-phosphate + ATP | Bacillus subtilis | PRPP (phosphoribosylpyrophosphate) synthetases are a family of enzymes that catalyse the synthesis of PRPP from ATP and R5P (ribose 5-phosphate) by transferring the beta, gamma-diphosphoryl moiety of ATP to the C1-hydroxy group of R5P. | phosphoribosyldiphosphate + AMP | - |
? | |
| D-ribose 5-phosphate + ATP | Homo sapiens | PRPP (phosphoribosylpyrophosphate) synthetases are a family of enzymes that catalyse the synthesis of PRPP from ATP and R5P (ribose 5-phosphate) by transferring the beta, gamma-diphosphoryl moiety of ATP to the C1-hydroxy group of R5P. | phosphoribosyldiphosphate + AMP | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
| Homo sapiens | - |
- |
- |
| Homo sapiens | P60891 | gene PRS1 | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged PRS1 from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + D-ribose 5-phosphate | the enzymatic activity of PRS is regulated by both the activator phosphate and the inhibitor ADP competing for binding at a common allosteric regulatory site | Homo sapiens | AMP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| ATP + D-ribose 5-phosphate | allosteric regulatory mechanism, overview | Homo sapiens | AMP + 5-phospho-alpha-D-ribose 1-diphosphate | - |
? | |
| D-ribose 5-phosphate + ATP | PRPP (phosphoribosylpyrophosphate) synthetases are a family of enzymes that catalyse the synthesis of PRPP from ATP and R5P (ribose 5-phosphate) by transferring the beta, gamma-diphosphoryl moiety of ATP to the C1-hydroxy group of R5P. | Bacillus subtilis | phosphoribosyldiphosphate + AMP | - |
? | |
| D-ribose 5-phosphate + ATP | PRPP (phosphoribosylpyrophosphate) synthetases are a family of enzymes that catalyse the synthesis of PRPP from ATP and R5P (ribose 5-phosphate) by transferring the beta, gamma-diphosphoryl moiety of ATP to the C1-hydroxy group of R5P. | Homo sapiens | phosphoribosyldiphosphate + AMP | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | - |
Bacillus subtilis |
| homodimer | - |
Homo sapiens |
| More | the allosteric regulatory site is composed of conserved residues Gln135, Asp143, Asn144 and Ser308-Phe313 of one subunit, residues Lys100-Arg104 of the flexible loop of the second subunit, and residues Ser47, Arg49, Ala80 and Ser81 of the third subunit, quarternary enzyme structure, modelling, overview | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ATP: D-ribose-5-phosphate pyrophosphotransferase | - |
Bacillus subtilis |
| ATP: D-ribose-5-phosphate pyrophosphotransferase | - |
Homo sapiens |
| bsPRS | - |
Bacillus subtilis |
| phosphoribosylpyrophosphate synthetase 1 | - |
Bacillus subtilis |
| phosphoribosylpyrophosphate synthetase 1 | - |
Homo sapiens |
| PRPP synthetase | - |
Bacillus subtilis |
| PRPP synthetase | - |
Homo sapiens |
| PRS | - |
Bacillus subtilis |
| PRS | - |
Homo sapiens |
| PRS1 | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | the AMP moiety of ATP binds at the ATP-binding site, structure, overview. A Cd2+ ion binds at the active site and in a position to interact with the beta- and gamma -phosphates of ATP | Homo sapiens | |
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