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Information on EC 2.7.6.1 - ribose-phosphate diphosphokinase and Organism(s) Homo sapiens and UniProt Accession P60891

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IUBMB Comments
dATP can also act as donor.
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Homo sapiens
UNIPROT: P60891
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
prps1, prpp synthetase, phosphoribosylpyrophosphate synthetase, phosphoribosyl pyrophosphate synthetase, prpp synthase, prpps, prs-i, ribose-phosphate pyrophosphokinase, ppribp synthetase, 5-phosphoribosyl-1-pyrophosphate synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoribosyl pyrophosphate synthase 1 (PRS-1)
-
phosphoribosyl pyrophosphate synthetase
-
phosphoribosylpyrophosphate synthetase
-
phosphoribosylpyrophosphate synthetase 1
-
PRPP synthetase
-
5-phosphoribose pyrophosphorylase
-
-
-
-
5-phosphoribosyl-1-pyrophosphate synthetase
-
-
-
-
5-phosphoribosyl-alpha-1-pyrophosphate synthetase
-
-
-
-
ATP: D-ribose-5-phosphate pyrophosphotransferase
-
-
ATP:D-ribose-5-phosphate pyrophosphotransferase
-
-
-
-
phosphoribosyl pyrophosphate synthase enzyme
-
-
phosphoribosyl-diphosphate synthetase
-
-
-
-
phosphoribosylpyrophosphate synthase
-
-
-
-
phosphoribosylpyrophosphate synthetase
-
-
-
-
phosphoribosylpyrophosphate synthetase 1
-
-
phosphoribosylpyrophosphate synthetase subunit 1
-
-
PP-ribose P synthetase
-
-
-
-
PPRibP synthetase
-
-
-
-
PRPP synthase
-
-
-
-
PRPP synthetase
PRS1
-
-
pyrophosphokinase, ribose phosphate
-
-
-
-
pyrophosphoribosylphosphate synthetase
-
-
-
-
ribophosphate pyrophosphokinase
-
-
-
-
ribose-5-phosphate pyrophosphokinase
-
-
-
-
ribose-phosphate pyrophosphokinase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diphosphate transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:D-ribose-5-phosphate diphosphotransferase
dATP can also act as donor.
CAS REGISTRY NUMBER
COMMENTARY hide
9015-83-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
ribose-5-phosphate + ATP
phosphoribosyldiphosphate + AMP
show the reaction diagram
first step in purine metabolic pathway
-
-
?
(R)9-(2-phosphonylmethoxypropyl)adenine + 5-phospho-alpha-D-ribose 1-diphosphate
(R)9-(2-phosphonylmethoxypropyl)adenine-diphosphate + D-ribose 5-phosphate
show the reaction diagram
-
-
-
r
(R)9-(3-fluoro-2-phosphonylmethoxypropyl)adenine + 5-phospho-alpha-D-ribose 1-diphosphate
(R)9-(3-fluoro-2-phosphonylmethoxypropyl)adenine-diphosphate + D-ribose 5-phosphate
show the reaction diagram
-
-
-
r
(S)9-(2-phosphonylmethoxypropyl)adenine + 5-phospho-alpha-D-ribose 1-diphosphate
(S)9-(2-phosphonylmethoxypropyl)adenine-diphosphate + D-ribose 5-phosphate
show the reaction diagram
-
-
-
r
(S)9-(3-fluoro-2-phosphonylmethoxypropyl)adenine + 5-phospho-alpha-D-ribose 1-diphosphate
(S)9-(3-fluoro-2-phosphonylmethoxypropyl)adenine-diphosphate + D-ribose 5-phosphate
show the reaction diagram
-
-
-
r
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate + 5-phospho-alpha-D-ribose 1-diphosphate
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-triphosphate + D-ribose 5-phosphate
show the reaction diagram
-
-
-
r
9-(2-phosphonylmethoxyethoxy)adenine + 5-phospho-alpha-D-ribose 1-diphosphate
9-(2-phosphonylmethoxyethoxy)adenine-diphosphate + D-ribose 5-phosphate
show the reaction diagram
-
-
-
r
9-(2-phosphonylmethoxyethyl)adenine + 5-phospho-alpha-D-ribose 1-diphosphate
9-(2-phosphonylmethoxyethyl)adenine-diphosphate + D-ribose 5-phosphate
show the reaction diagram
-
-
-
r
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
ATP + D-ribose 5-phosphate
show the reaction diagram
-
-
-
r
ATP + 1,2,3-trihydroxy-4-cyclopentanemethanol-6-phosphate
?
show the reaction diagram
-
very poor substrate
-
-
?
ATP + 1,4,5-trihydroxy-3-cyclopent-2-enemethanol-6-phosphate
?
show the reaction diagram
-
very poor substrate, better than 1,2,3-trihydroxy-4-cyclopentanemethanol-6-phosphate
-
-
?
ATP + 6-deoxyhomoribose 6-phosphonate
AMP + 6-deoxyhomoribose 6-phosphonate 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
ATP + D-ribose 5-phosphothionate
AMP + 5-phosphotionate-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + ribulose-5-phosphate
AMP + 5-phospho-ribulose-1-diphosphate
show the reaction diagram
-
-
-
r
CTP + D-ribose 5-phosphate
CMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
does not serve as substrate
-
-
?
D-ribose 5-phosphate + ATP
5-phospho-alpha-D-ribose 1-diphosphate + AMP
show the reaction diagram
biosynthesis of purines and pyrimidines
-
-
?
D-ribose 5-phosphate + ATP
phosphoribosyldiphosphate + AMP
show the reaction diagram
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.
-
-
?
dATP + D-ribose 5-phosphate
dAMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
in erythrocyte enzyme and tumor cell enzyme
-
r
UTP + D-ribose 5-phosphate
UMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
does not serve as substrate
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
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
-
-
?
ribose-5-phosphate + ATP
phosphoribosyldiphosphate + AMP
show the reaction diagram
first step in purine metabolic pathway
-
-
?
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
D-ribose 5-phosphate + ATP
5-phospho-alpha-D-ribose 1-diphosphate + AMP
show the reaction diagram
biosynthesis of purines and pyrimidines
-
-
?
D-ribose 5-phosphate + ATP
phosphoribosyldiphosphate + AMP
show the reaction diagram
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.
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
a Cd2+ ion binds at the active site and in a position to interact with the beta- and gamma-phosphates of ATP
Co2+
can serve as substitutes for Mg2+ with relatively lower activity
Ni2+
can serve as substitutes for Mg2+ with relatively lower activity
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.
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diadenosine pentaphosphate
Inhibits the dephosphorylation of ATP and ADP by nonspecific phosphatases.
1,2,3-trihydroxy-4-cyclopentanemethanol-6-phosphate
-
at pH 7.5, competitive inhibition with respect to D-ribose 5-phosphate and noncompetitive inhibition with respect to ATP
1,4,5-trihydroxy-3-cyclopent-2-enemethanol-6-phosphate
-
partial noncompetitive inhibition with respect to D-ribose 5-phosphate and no inhibition with respect to ATP
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate
-
-
2,3-diphosphoglycerate
2-deoxy-D-ribose 5-phosphate
-
92% inhibition at 1 mM
5-phospho-alpha-D-ribose 1-diphosphate
9-(2-phosphonylmethoxyethoxy)adenine
-
IC50 of more than 2.5 mM
9-(2-phosphonylmethoxyethyl)adenine
-
IC50 of 2.1 mM
adenosine
-
27% inhibition at 1 mM
allopurinol ribonucleotides
-
23% inhibition at 1 mM
alpha,beta-methyleneATP
-
competitive inhibition to ATP
D-fructose 1,6-diphosphate
-
20% inhibition at 1 mM
D-Fructose 1-phosphate
-
19% inhibition at 1 mM
D-ribose 1-phosphate
-
13% inhibition at 1 mM
FAD
-
51% inhibition at 1 mM
glyceraldehyde 3-phosphate
-
14% inhibition at 1 mM
guanosine
-
20% inhibition at 1 mM
IDP
-
47% inhibition at 1 mM
IMP
-
21% inhibition at 1 mM
ITP
-
36% inhibition at 1 mM
NAD+
-
100% inhibition at 1 mM
NADH
-
72% inhibition at 1 mM
NADPH
-
100% inhibition at 1 mM
PRPP synthetase-associated proteins
-
inhibit catalytic and perhaps regulatory functions of the enzyme
-
TDP
-
100% inhibition at 1 mM
TTP
-
47% inhibition at 1 mM
UMP
-
10%-18% inhibition at 1 mM
XDP
-
36% inhibition at 1 mM
XTP
-
22% inhibition at 1 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphate
-
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
phosphate
sulfate
-
can partially replace phosphate in activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.571
(R)9-(2-phosphonylmethoxypropyl)adenine
-
pH 8.0, 37ºC
2.174
(S)9-(2-phosphonylmethoxypropyl)adenine
-
pH 8.0, 37ºC
0.422
9-(2-phosphonylmethoxyethoxy)adenine
-
pH 8.0, 37ºC
0.661
9-(2-phosphonylmethoxyethyl)adenine
-
pH 8.0, 37ºC
0.122
AMP
-
pH 8.0, 37ºC
0.007 - 0.14
ATP
0.052 - 0.57
D-ribose 5-phosphate
0.0002 - 0.2
Mg2+
0.7 - 2.1
phosphate
0.033
ribose 5-phosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.41
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate
-
pH 8.0, 37ºC
0.1
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 37ºC
0.37
9-(2-phosphonylmethoxyethyl)adenine
-
pH 8.0,37ºC
0.01
ADP
-
pH conditions and temperature conditions not mentioned
0.3 - 0.4
AMP
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5
9-(2-phosphonylmethoxyethoxy)adenine
Homo sapiens
-
IC50 of more than 2.5 mM
2.1
9-(2-phosphonylmethoxyethyl)adenine
Homo sapiens
-
IC50 of 2.1 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20.5 - 21.2
-
values from lymphoblasts extracts from normal and PRS catalytic superactivity affected patients
22.2 - 29.9
-
values from fibroblast extracts from normal and PRS catalytic superactivity affected patients
25
-
isoenzyme PRSI
3.65
-
wild type enzyme
35.7
-
isoenzyme PRSII
8.17
-
mutant enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 7.4
-
erythrocyte enzyme
7.4
-
isoenzyme PRSII
7.5
-
at 40-50 mM phosphate, isoenzymes PRSI and PRSII
8.8
-
isoenzyme PRSI
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.3
-
At pH 6.5, about 25% and 50% of maximum activity for isoenzymes PRSI and PRSII, respectively. At pH 9.3, about 40% and 60% of maximum activity for isoenzymes PRSII and PRSI, respectively
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
-
isoelectric focusing, mutant enzyme
5.1
-
isoelectric focusing, normal enzyme
5.5
-
two-dimensional protein electrophoresis, isoenzyme PRSI
5.7
-
two-dimensional protein electrophoresis, isoenzyme PRSII
6.6
-
isoenzyme PRSII
6.8
-
isoenzyme PRSI
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PRPS1_HUMAN
318
0
34834
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1000000
32000
-
x * 32000, SDS-PAGE
34500
-
x * 34500, SDS-PAGE
34600
-
x * 34600, isoenzyme PRSII
34700
-
x * 34700, isoenzyme PRSI
43000
-
x * 43000, sucrose density gradient sedimentation in the presence of urea 2 M combined with values of gel filtration
53000
-
x * 53000, sucrose density gradient sedimentation in the presence of NaCl, 1 M, combined with values of gel filtration
60000
-
x * 60000, sucrose density gradient sedimentation in phosphate buffer combined with values of gel filtration
700000 - 1200000
-
sucrose density gradient sedimentation and gel filtration
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
-
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
hanging-drop vapour diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E43D
naturally occuring mutation causes the Rosenberg-Chutorian syndrome, the disease locus CMTX5 is situated on the chromosome band Xq21.32-q24
S132A
the mutants show altered ligand binding and regulation at the allosteric site compared to the wild-type enzyme, comparison of crystal structures, overview
V142L
the mutation is associated with uric acid overproduction without gout but with developmental delay, hypotonia, hearing loss, and recurrent respiratory infections in human. The mutation affects both allosteric sites that are involved in inhibition of the enzyme and the ATP-binding site
Y146M
the mutants show altered ligand binding and regulation at the allosteric site compared to the wild-type enzyme, comparison of crystal structures, overview
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
85% of maximal activity, isoenzyme PRSI
642719
8.8
-
41% of maximal activity, isoenzyme PRSII
642719
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
isoenzyme PRSII is more thermolabile than PRSI
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dilution of highly purified isoenzyme PRSII to 0.1 mg/ml lacking Mg2+ and ATP results in immediate loss of 65% activity and 88% activity after 3 h at 4ºC. Dilution of isoenzyme PRSI to 0.1 mg/ml lacking Mg2+ and ATP results in loss of 10% activity after 3h at 4ºC
-
PRSII undergoes substantial immediate but reversible inactivation when diluted in phosphate buffer lacking Mg2+ and ATP
-
sulfhydryl compounds inactivate highly purified PRPP synthetase from erythrocytes, essential for stability and assay of partially purified enzyme
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged PRS1 from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
4500fold purification
-
partial, 400fold purification
-
streptomycin precipitation and ammonium sulfate fractionation for isoenzyme PRSI and polyethylene glycol, acid and ammonium sulfate precipitation for isoenzyme PRSII
-
to near homogeneity. Use of Mg2+, ATP and sulfhydryl compounds to stabilize the enzyme permit its isolation from erythrocytes
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene PRPS1, genomic structure, genotyping in European and Asian individuals
gene PRS1 from a cDNA library, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
expression in Escherichia coli
-
expression of isoenzymes PRSI and PRSII in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Switzer, R.L.
Phosphoribosylpyrophosphate synthetase and related pyrophosphokinases
The Enzymes,3rd Ed. (Boyer,P. D. ,ed. )
10
607-629
1974
Gallus gallus, Columba sp., Escherichia coli, Homo sapiens, Mus musculus, Ophiodon elongatus, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium
-
Manually annotated by BRENDA team
Fox, I.H.; Kelley, W.N.
Human phosphoribosylpyrophosphate synthetase. Kinetic mechanism and end product inhibition
J. Biol. Chem.
247
2126-2131
1972
Homo sapiens
Manually annotated by BRENDA team
Nosal, J.M.; Switzer, R.L.; Becker, M.A.
Overexpression, purification, and characterization of recombinant human 5-phosphoribosyl-1-pyrophosphate synthetase isozymes I and II
J. Biol. Chem.
268
10168-10175
1993
Homo sapiens
Manually annotated by BRENDA team
Becker, M.A.; Kostel, P.J.; Meyer, L.J.
Human phosphoribosylpyrophosphate synthetase. Comparison of purified normal and mutant enzymes
J. Biol. Chem.
250
6822-6830
1975
Homo sapiens
Manually annotated by BRENDA team
Parry, R.J.; Burns, M.R.; Skae, P.N.; Hoyt, J.C.; Pal, B.
Carbocyclic analogues of D-ribose-5-phosphate: synthesis and behavior with 5-phosphoribosyl alpha-1-pyrophosphate synthetases
Bioorg. Med. Chem.
4
1077-1088
1996
Bacillus subtilis, Homo sapiens, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Balzarini, J.; Nave, J.F.; Becker, M.A.; Tatibana, M.; De Clercq, E.
Kinetic properties of adenine nucleotide analogs against purified 5-phosphoribosyl-1-pyrophosphate synthetase from E. coli, rat liver and human erythrocytes
Nucleosides Nucleotides
14
1861-1871
1995
Escherichia coli, Homo sapiens, Rattus norvegicus
-
Manually annotated by BRENDA team
Okada, N.N.; Ishizuka, T.; Isogai, E.; Suzuki, N.; Tatibana, M.
Variation of phosphoribosylpyrophosphate synthetase activity in human cells
Biochem. Mol. Biol. Int.
44
1059-1067
1998
Homo sapiens
-
Manually annotated by BRENDA team
Becker, M.A.
Phosphoribosylpyrophosphate synthetase and the regulation of phosphoribosylpyrophosphate production in human cells
Prog. Nucleic Acid Res. Mol. Biol.
69
115-148
2001
Bacillus subtilis, Homo sapiens
Manually annotated by BRENDA team
Tatibana, M.; Kita, K.; Taira, M.; Ishijima, S.; Sonoda, T.; Ishizuka, T.; Iizasa, T.; Ahmad, I.
Mammalian phosphoribosyl-pyrophosphate synthetase
Adv. Enzyme Regul.
35
229-249
1995
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Becker, M.A.; Taylor, W.; Smith, P.R.; Ahmed, M.
Overexpression of the normal phosphoribosylpyrophosphate synthetase 1 isoform underlies catalytic superactivity of human phosphoribosylpyrophosphate synthetase
J. Biol. Chem.
271
19894-19899
1996
Homo sapiens
Manually annotated by BRENDA team
Kaida, A.; Ariumi, Y.; Baba, K.; Matsubae, M.; Takao, T.; Shimotohno, K.
Identification of a novel p300-specific-associating protein, PRS1 (phosphoribosylpyrophosphate synthetase subunit 1)
Biochem. J.
391
239-247
2005
Homo sapiens
Manually annotated by BRENDA team
de Brouwer, A.P.; Williams, K.L.; Duley, J.A.; van Kuilenburg, A.B.; Nabuurs, S.B.; Egmont-Petersen, M.; Lugtenberg, D.; Zoetekouw, L.; Banning, M.J.; Roeffen, M.; Hamel, B.C.; Weaving, L.; Ouvrier, R.A.; Donald, J.A.; Wevers, R.A.; Christodoulou, J.; van Bokhoven, H.
Arts syndrome is caused by loss-of-function mutations in PRPS1
Am. J. Hum. Genet.
81
507-518
2007
Homo sapiens (P60891), Homo sapiens
Manually annotated by BRENDA team
Kim, H.J.; Sohn, K.M.; Shy, M.E.; Krajewski, K.M.; Hwang, M.; Park, J.H.; Jang, S.Y.; Won, H.H.; Choi, B.O.; Hong, S.H.; Kim, B.J.; Suh, Y.L.; Ki, C.S.; Lee, S.Y.; Kim, S.H.; Kim, J.W.
Mutations in PRPS1, which encodes the phosphoribosyl pyrophosphate synthetase enzyme critical for nucleotide biosynthesis, cause hereditary peripheral neuropathy with hearing loss and optic neuropathy (cmtx5)
Am. J. Hum. Genet.
81
552-558
2007
Homo sapiens, Homo sapiens (P60891)
Manually annotated by BRENDA team
Li, S.; Lu, Y.; Peng, B.; Ding, J.
Crystal structure of human phosphoribosylpyrophosphate synthetase 1 reveals a novel allosteric site
Biochem. J.
401
39-47
2007
Bacillus subtilis, Homo sapiens, Homo sapiens (P60891)
Manually annotated by BRENDA team
Moran, R.; Kuilenburg, A.B.; Duley, J.; Nabuurs, S.B.; Retno-Fitri, A.; Christodoulou, J.; Roelofsen, J.; Yntema, H.G.; Friedman, N.R.; van Bokhoven, H.; de Brouwer, A.P.
Phosphoribosylpyrophosphate synthetase superactivity and recurrent infections is caused by a p.Val142Leu mutation in PRS-I
Am. J. Med. Genet. A
158A
455-460
2012
Homo sapiens (P60891), Homo sapiens
Manually annotated by BRENDA team