Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Li, S.; Lu, Y.; Peng, B.; Ding, J.
    Crystal structure of human phosphoribosylpyrophosphate synthetase 1 reveals a novel allosteric site (2007), Biochem. J., 401, 39-47.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.6.1 phosphate
-
 Homo sapiens
2.7.6.1 phosphate required for enzymatic activity by class 1 PRSs Bacillus subtilis
2.7.6.1 phosphate required for enzymatic activity by class 1 PRSs Homo sapiens
2.7.6.1 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)

EC Number Cloned (Comment) Organism
2.7.6.1 gene PRS1 from a cDNA library, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3) Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.6.1 hanging-drop vapour diffusion method Bacillus subtilis
2.7.6.1 hanging-drop vapour diffusion method Homo sapiens
2.7.6.1 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

EC Number Protein Variants Comment Organism
2.7.6.1 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
2.7.6.1 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

EC Number Inhibitors Comment Organism Structure
2.7.6.1 ADP allosterical inhibition Bacillus subtilis
2.7.6.1 ADP allosterical inhibition Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.6.1 Cd2+ can serve as substitutes for Mg2+ with relatively lower activity Homo sapiens
2.7.6.1 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
2.7.6.1 Co2+ can serve as substitutes for Mg2+ with relatively lower activity Homo sapiens
2.7.6.1 Mg2+
-
 Homo sapiens
2.7.6.1 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
2.7.6.1 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
2.7.6.1 Mn2+ can serve as substitutes for Mg2+ with relatively lower activity Homo sapiens
2.7.6.1 Ni2+ can serve as substitutes for Mg2+ with relatively lower activity Homo sapiens
2.7.6.1 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
2.7.6.1 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.6.1 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
-
 ?
2.7.6.1 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
-
 ?
2.7.6.1 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

EC Number Organism UniProt Comment Textmining
2.7.6.1 Bacillus subtilis
-
-
-
2.7.6.1 Homo sapiens
-
-
-
2.7.6.1 Homo sapiens P60891 gene PRS1
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.6.1 recombinant His-tagged PRS1 from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography 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 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
-
 ?
2.7.6.1 ATP + D-ribose 5-phosphate allosteric regulatory mechanism, overview Homo sapiens AMP + 5-phospho-alpha-D-ribose 1-diphosphate
-
 ?
2.7.6.1 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
-
 ?
2.7.6.1 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

EC Number Subunits Comment Organism
2.7.6.1 hexamer
-
 Bacillus subtilis
2.7.6.1 homodimer
-
 Homo sapiens
2.7.6.1 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

EC Number Synonyms Comment Organism
2.7.6.1 ATP: D-ribose-5-phosphate pyrophosphotransferase
-
 Bacillus subtilis
2.7.6.1 ATP: D-ribose-5-phosphate pyrophosphotransferase
-
 Homo sapiens
2.7.6.1 bsPRS
-
 Bacillus subtilis
2.7.6.1 phosphoribosylpyrophosphate synthetase 1
-
 Bacillus subtilis
2.7.6.1 phosphoribosylpyrophosphate synthetase 1
-
 Homo sapiens
2.7.6.1 PRPP synthetase
-
 Bacillus subtilis
2.7.6.1 PRPP synthetase
-
 Homo sapiens
2.7.6.1 PRS
-
 Bacillus subtilis
2.7.6.1 PRS
-
 Homo sapiens
2.7.6.1 PRS1
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.6.1 37
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.6.1 8
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.6.1 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