Information on EC 2.7.6.1 - ribose-phosphate diphosphokinase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
2.7.6.1
-
RECOMMENDED NAME
GeneOntology No.
ribose-phosphate diphosphokinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
mechanism
-
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
mechanism; ordered bi-bi reaction; ordered bi-bi reaction with ribose-5-phosphate binding first and 5-phosphoribose diphosphate being released last
-
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
mechanism
-
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
mechanism; ordered bi-bi reaction; ordered bi-bi reaction with ribose-5-phosphate binding first and 5-phosphoribose diphosphate being released last
-
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
ordered bi-bi reaction; ordered bi-bi reaction with ribose-5-phosphate binding first and 5-phosphoribose diphosphate being released last
-
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
sequential kinetic mechanism
-
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
sequential kinetic mechanism
-
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
steady state ordered mechanism in which Mg2+ binds first and D-ribose 5-phosphate binds last
-
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
ordered bi-bi reaction; sequential kinetic mechanism
-
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
diphosphate transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
PRPP biosynthesis I
-
Pentose phosphate pathway
-
Purine metabolism
-
Metabolic pathways
-
Biosynthesis of secondary metabolites
-
Microbial metabolism in diverse environments
-
SYSTEMATIC NAME
IUBMB Comments
ATP:D-ribose-5-phosphate diphosphotransferase
dATP can also act as donor.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5-phospho-alpha D-ribosyl 1-diphosphate synthase
-
-
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 diphosphate synthase
Q58761
-
phosphoribosyl pyrophosphate synthase 1 (PRS-1)
-
-
phosphoribosyl pyrophosphate synthase enzyme
-
-
phosphoribosyl pyrophosphate synthetase
E7EAU9
-
phosphoribosyl pyrophosphate synthetase
Bacillus amyloliquefaciens IAM 1523
E7EAU9
-
-
phosphoribosyl pyrophosphate synthetase
Emericella nidulans
-
-
phosphoribosyl pyrophosphate synthetase
Emericella nidulans WJA01
-
-
-
phosphoribosyl pyrophosphate synthetase
P60891
-
phosphoribosyl pyrophosphate synthetase
Q97CA5
-
phosphoribosyl-1-pyrophosphate synthetase
-
-
phosphoribosyl-diphosphate synthetase
-
-
-
-
phosphoribosylpyrophosphate synthase
-
-
-
-
phosphoribosylpyrophosphate synthase
-
-
phosphoribosylpyrophosphate synthase
Mycobacterium tuberculosis Rv1017c
-
-
-
phosphoribosylpyrophosphate synthase
-
-
phosphoribosylpyrophosphate synthetase
-
-
-
-
phosphoribosylpyrophosphate synthetase
P60891
-
phosphoribosylpyrophosphate synthetase
-
-
phosphoribosylpyrophosphate synthetase
Mycobacterium tuberculosis Rv1017
-
-
-
phosphoribosylpyrophosphate synthetase
-
-
phosphoribosylpyrophosphate synthetase
Salmonella enterica DM10373
-
-
-
phosphoribosylpyrophosphate synthetase 1
-
-
phosphoribosylpyrophosphate synthetase 1
P60891
-
phosphoribosylpyrophosphate synthetase subunit 1
-
-
PP-ribose P synthetase
-
-
-
-
PPRibP synthetase
-
-
-
-
PRibPP synthase
-
-
PRPP synthase
-
-
-
-
PRPP synthase
Q58761
-
PRPP synthetase
-
-
-
-
PRPP synthetase
-
-
PRPP synthetase
Emericella nidulans
-
-
PRPP synthetase
Emericella nidulans WJA01
-
-
-
PRPP synthetase
-
-
PRPP synthetase
-
-
PRPP synthetase
P60891
-
PRPP synthetase
-
-
PRPP synthetase
-
-
PRPP synthetase
Salmonella enterica DM10373
-
-
-
PRPP synthetase
Q97CA5
-
PRPPase
Mycobacterium tuberculosis Rv1017
-
-
-
PRPS1
H9D1K2
-
PRS
Bacillus amyloliquefaciens IAM 1523
E7EAU9
-
-
PRS
Emericella nidulans
-
-
PRS
Emericella nidulans WJA01
-
-
-
PRS
Mycobacterium tuberculosis Rv1017c
-
-
-
PRS-I
P60891
-
PRS1
-
-
PRS1
P60891
-
PrsA
Salmonella enterica DM10373
-
-
-
pyrophosphokinase, ribose phosphate
-
-
-
-
pyrophosphoribosylphosphate synthetase
-
-
-
-
ribophosphate pyrophosphokinase
-
-
-
-
ribose-5-phosphate pyrophosphokinase
-
-
-
-
ribose-phosphate pyrophosphokinase
-
-
-
-
ribose-phosphate pyrophosphokinase 1
H9D1K2
-
CAS REGISTRY NUMBER
COMMENTARY
9015-83-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Bacillus amyloliquefaciens IAM 1523
-
UniProt
Manually annotated by BRENDA team
Culex pipiens subsp. pallens
UniProt
Manually annotated by BRENDA team
Emericella nidulans
-
-
-
Manually annotated by BRENDA team
Emericella nidulans WJA01
-
-
-
Manually annotated by BRENDA team
strain ATCC 10895, two genes AGR371C and AGL080C encode isozymes AgPRS2,4 and AgPRS3, respectively
-
-
Manually annotated by BRENDA team
chicken
-
-
Manually annotated by BRENDA team
rubber tree
-
-
Manually annotated by BRENDA team
gene PRPS1
SwissProt
Manually annotated by BRENDA team
gene PRS1
SwissProt
Manually annotated by BRENDA team
mouse
-
-
Manually annotated by BRENDA team
Mycobacterium tuberculosis Rv1017
-
-
-
Manually annotated by BRENDA team
Mycobacterium tuberculosis Rv1017c
-
-
-
Manually annotated by BRENDA team
Salmonella enterica DM10373
-
-
-
Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimurium LT-2
LT-2
-
-
Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimurium Su 422
Su 422 strain
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
Emericella nidulans
-
the reduction of enzyme activity causes both premature and hyperseptation
malfunction
Emericella nidulans WJA01
-
the reduction of enzyme activity causes both premature and hyperseptation
-
physiological function
Emericella nidulans
-
normal cytokinesis is dependent on a normal level of enzyme activity. The enzyme is required for the proper timing of septation
physiological function
-, H9D1K2
the increased expression level of ribose-phosphate pyrophosphokinase 1 plays roles in the regulation of deltamethrin resistance
physiological function
-
the enzyme is crucial for mycobacterial cell wall biosynthesis
physiological function
Emericella nidulans WJA01
-
normal cytokinesis is dependent on a normal level of enzyme activity. The enzyme is required for the proper timing of septation
-
physiological function
Mycobacterium tuberculosis Rv1017
-
the enzyme is crucial for mycobacterial cell wall biosynthesis
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(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
5'-adenylyl-beta,gamma-imidodiphosphate + D-ribose 5-phosphate
?
show the reaction diagram
-
-
-
-
?
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
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 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-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 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-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 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-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Emericella nidulans
-
-
-
-
?
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 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-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
-
ir
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
-
?
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
-
ir
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-, H9D1K2
-
-
-
?
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-, E7EAU9
-
-
-
?
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Q97CA5, -
-
-
-
ir
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
ribose product also known as 5-phosphoryl-D-ribofuranose alpha-1-diphosphate
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
highly specific for ATP
ribose product also known as PRPP
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
highly specific for ATP
ribose product also known as PRPP
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
highly specific for ATP
ribose product also known as PRPP
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
highly specific for ATP
ribose product also known as 5-phosphoryl-D-ribofuranose alpha-1-diphosphate
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
highly specific for D-ribose 5-phosphate
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
highly specific for D-ribose 5-phosphate
ribose product also known as PRPP, ribose product also known as 5-phosphoryl-D-ribofuranose alpha-1-diphosphate
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
highly specific for D-ribose 5-phosphate
ribose product also known as 5-phosphoryl-D-ribofuranose alpha-1-diphosphate
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
maximal velocity of the reverse reaction is 9-10% of the forward reaction
ribose product also known as PRPP
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
maximal velocity of the reverse reaction is 9-10% of the forward reaction
ribose product also known as PRPP
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
maximal velocity of the reverse reaction is 9-10% of the forward reaction
ribose product also known as 5-phosphoryl-D-ribofuranose alpha-1-diphosphate
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
ATP is bound to the enzyme in the form of MgATP2- complex
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
P60891
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, allosteric regulatory mechanism, overview
-
-
?
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Q58761
the enzyme accepts ATP and dATP equally well as diphosphoryl donor
-
-
?
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium Su 422
-
highly specific for ATP, maximal velocity of the reverse reaction is 9-10% of the forward reaction
ribose product also known as PRPP
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium Su 422
-
-, the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Salmonella enterica DM10373
-
-
-
-
ir
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Bacillus amyloliquefaciens IAM 1523
E7EAU9
-
-
-
?
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Mycobacterium tuberculosis Rv1017c
-
-
-
-
?
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium LT-2
-
-, the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium LT-2
-
highly specific for ATP, maximal velocity of the reverse reaction is 9-10% of the forward reaction
ribose product also known as PRPP
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Emericella nidulans WJA01
-
-
-
-
?
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
-
-
-
r
CTP + D-ribose 5-phosphate
CMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
CTP + D-ribose 5-phosphate
CMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
-
?
CTP + D-ribose 5-phosphate
CMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
less effective than ATP
-
r
CTP + D-ribose 5-phosphate
CMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
does not serve as substrate
-
-
-
CTP + D-ribose 5-phosphate
CMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
does not serve as substrate
-
-
-
CTP + D-ribose 5-phosphate
CMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
does not serve as substrate
-
-
-
CTP + D-ribose 5-phosphate
CMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium Su 422
-
less than 3% of the activity with ATP
-
r
CTP + D-ribose 5-phosphate
CMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Mycobacterium tuberculosis Rv1017c
-
-
-
-
?
CTP + D-ribose 5-phosphate
CMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium LT-2
-
less than 3% of the activity with ATP
-
r
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.
-
-
?
D-ribose 5-phosphate + ATP
phosphoribosyldiphosphate + AMP
show the reaction diagram
P60891
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.
-
-
?
D-ribose 5-phosphate + ATP
5-phospho-alpha-D-ribose 1-diphosphate + AMP
show the reaction diagram
P60891
biosynthesis of purines and pyrimidines
-
-
?
dATP + D-ribose 5-phosphate
dAMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
dATP + D-ribose 5-phosphate
dAMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
dATP + D-ribose 5-phosphate
dAMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
dATP + D-ribose 5-phosphate
dAMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
equally effective as ATP
-
r
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
dATP + D-ribose 5-phosphate
dAMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
slightly more effective than ATP
-
r
dATP + D-ribose 5-phosphate
dAMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Q58761
the enzyme accepts ATP and dATP equally well as diphosphoryl donor
-
-
?
GTP + D-ribose 5-phosphate
GMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
GTP + D-ribose 5-phosphate
GMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
-
?
GTP + D-ribose 5-phosphate
GMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
less effective than ATP
-
r
GTP + D-ribose 5-phosphate
GMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
does not serve as substrate
-
-
-
GTP + D-ribose 5-phosphate
GMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium Su 422
-
less than 3% of the activity with ATP
-
r
GTP + D-ribose 5-phosphate
GMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Mycobacterium tuberculosis Rv1017c
-
-
-
-
?
GTP + D-ribose 5-phosphate
GMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium LT-2
-
less than 3% of the activity with ATP
-
r
ITP + D-ribose 5-phosphate
IMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
does not serve as substrate
-
-
-
ITP + D-ribose 5-phosphate
IMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
less than 3% of the activity with ATP
-
r
Mg-ATP2- + D-ribose 5-phosphate
Mg-AMP2- + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Mycobacterium tuberculosis, Mycobacterium tuberculosis Rv1017
-
-
-
-
?
ribose-5-phosphate + ATP
phosphoribosyldiphosphate + AMP
show the reaction diagram
P60891
first step in purine metabolic pathway
-
-
?
UTP + D-ribose 5-phosphate
UMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
UTP + D-ribose 5-phosphate
UMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
UTP + D-ribose 5-phosphate
UMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
-
?
UTP + D-ribose 5-phosphate
UMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
less effective than ATP
-
r
UTP + D-ribose 5-phosphate
UMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
does not serve as substrate
-
-
-
UTP + D-ribose 5-phosphate
UMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
does not serve as substrate
-
-
-
UTP + D-ribose 5-phosphate
UMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
does not serve as substrate
-
-
-
UTP + D-ribose 5-phosphate
UMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium Su 422
-
less than 3% of the activity with ATP
-
r
UTP + D-ribose 5-phosphate
UMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Mycobacterium tuberculosis Rv1017c
-
-
-
-
?
UTP + D-ribose 5-phosphate
UMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium LT-2
-
less than 3% of the activity with ATP
-
r
Mn-ATP2- + D-ribose 5-phosphate
Mn-AMP2- + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Mycobacterium tuberculosis, Mycobacterium tuberculosis Rv1017
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
2-deoxyribose-5-phosphate is not substrate
-
-
-
additional information
?
-
-
2-deoxyribose-5-phosphate is not substrate
-
-
-
additional information
?
-
-
D-ribitol-5-phosphate, alpha-methyl-D-ribofuranoside-5-phosphate, beta-methyl-D-ribofuranoside-5-phosphate are no substrates, other nucleosides di and triphosphates than ATP do not serve as substrates
-
-
-
additional information
?
-
-
other nucleosides di and triphosphates than ATP do not serve as substrates
-
-
-
additional information
?
-
-
ribose, ribose-1-phosphate, deoxyribose-5-phosphate, glucose-6-phosphate are not effective as substrates
-
-
-
additional information
?
-
P60891
the phosphoribosyl pyrophosphate synthetase enzyme critical for nucleotide biosynthesis
-
-
-
additional information
?
-
Q58761
the enzyme is essentially unable to use GTP (0.4% of the activity obtained with ATP), UTP (0.5%) or CTP (3%) as phosphoryl donor
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
P60891
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
-
-
?
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium Su 422
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium LT-2
-
the product phosphoribosyldiphosphate is required for the biosynthesis of purine, pyrimidine and pyridine nucleotides, L-histidine and L-tryptophan
-
r
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.
-
-
?
D-ribose 5-phosphate + ATP
phosphoribosyldiphosphate + AMP
show the reaction diagram
P60891
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.
-
-
?
ribose-5-phosphate + ATP
phosphoribosyldiphosphate + AMP
show the reaction diagram
P60891
first step in purine metabolic pathway
-
-
?
D-ribose 5-phosphate + ATP
5-phospho-alpha-D-ribose 1-diphosphate + AMP
show the reaction diagram
P60891
biosynthesis of purines and pyrimidines
-
-
?
additional information
?
-
P60891
the phosphoribosyl pyrophosphate synthetase enzyme critical for nucleotide biosynthesis
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
P60891
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 ACCESSION NO.
COMMENTARY
LITERATURE
Cd2+
-
can partially replace Mg2+
Cd2+
-
no activity observed
Cd2+
-
activity is 5-10% of the activity with Mg2+
Cd2+
P60891
a Cd2+ ion binds at the active site and in a position to interact with the beta- and gamma-phosphates of ATP; can serve as substitutes for Mg2+ with relatively lower activity
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
no activity observed
Co2+
-
no activity observed
Co2+
P60891
can serve as substitutes for Mg2+ with relatively lower activity
Cu2+
-
activity is 5-10% of the activity with Mg2+
Mg2+
-
required to form a complex with ATP and as a free cation; requirement
Mg2+
-
requirement
Mg2+
-
required to form a complex with ATP and as a free cation; the most effective
Mg2+
-
required to form a complex with ATP and as a free cation; the most effective
Mg2+
-
required to form a complex with ATP and as a free cation
Mg2+
-
required to form a complex with ATP and as a free cation
Mg2+
-
required to form a complex with ATP and as a free cation; requirement; the most effective
Mg2+
-
requirement; the most effective
Mg2+
-
activation of liver enzyme is almost maximal at 0.05 mM; required to form a complex with ATP and as a free cation; requirement
Mg2+
-
required to form a complex with ATP and as a free cation; requirement; the most effective
Mg2+
-
required to form a complex with ATP and as a free cation; requirement; the most effective
Mg2+
-
prepares the active site of the enzyme for the binding of the highly phosphorylated ligands
Mg2+
-
requirement
Mg2+
-
saturation with free Mg2+ results in hyperbolic activation by phosphate. At unsaturating free Mg2+ concentration, cooperative activation by phosphate is observed
Mg2+
-
required to form a complex with ATP and as a free cation; requirement
Mg2+
-
free Mg2+ required for maximal activity
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.
Mg2+
P60891
; 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.
Mg2+
Q97CA5, -
required
Mg2+
-
allosterically activated by Mg2+
Mg2+
Q58761
the activity of the enzyme depends on the presence of divalent cations, of which Mg2+ is the most effective. Mn2+ is also accepted, but the activity is less than 15% of that obtained with Mg2+, when assayed at pH 9.5
Mn2+
-
25-30% of the activity with Mg2+; can partially replace Mg2+
Mn2+
-
can partially replace Mg2+
Mn2+
-
25-30% of the activity with Mg2+
Mn2+
-
can partially replace Mg2+
Mn2+
-
no activity observed
Mn2+
-
can partially replace Mg2+
Mn2+
-
substitutes for Mg2+ at 30% of the activity obtained with Mg2+
Mn2+
P60891
can serve as substitutes for Mg2+ with relatively lower activity
Mn2+
-
allosterically activated by Mn2+
Ni2+
P60891
can serve as substitutes for Mg2+ with relatively lower activity
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.
SO42-
P60891
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.
Zn2+
-
no activity observed
Zn2+
-
no activity observed
Zn2+
-
activity is 5-10% of the activity with Mg2+
Mn2+
Q58761
the activity of the enzyme depends on the presence of divalent cations, of which Mg2+ is the most effective. Mn2+ is also accepted, but the activity is less than 15% of that obtained with Mg2+, when assayed at pH 9.5
additional information
-
absolute requirement for a divalent cation for activity; no activity observed with Ca2+
additional information
-
absolute requirement for a divalent cation for activity
additional information
-
absolute requirement for a divalent cation for activity; no activity observed with Ca2+
additional information
-
the enzyme binds two cations per subunit, the binding of a free cation can initiate the catalysis
additional information
-
no activity observed with Ca2+; no activity observed with Cd2+, Cu2+, Fe2+ and Ni2+
additional information
-
absolute requirement for a divalent cation for activity
additional information
-
absolute requirement for a divalent cation for activity
additional information
-
K+, Na+, Fe2+ Cu2+ and Ca2+ have no notable effects on the enzyme activity
additional information
-
no activity observed with Ca2+
additional information
-
Mn2+ and Mg2+ cannot be replaced by Ca2+
additional information
Q58761
the enzyme is essentially inactive in the presence of Cu2+, Ca2+, Co2+, Ni2+ or Fe2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,2,3-trihydroxy-4-cyclopentanemethanol-6-phosphate
-
mixed-type inhibition with respect to D-ribose 5-phosphate and no inhibition against ATP
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
-
1,4,5-trihydroxy-3-cyclopent-2-enemethanol-6-phosphate
-
partial mixed-type inhibition with respect to D-ribose 5-phosphate and ATP
-
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate
-
-
2,3-diphosphoglycerate
-
competitive to D-ribose 5-phosphate; inhibition of the erythrocyte enzyme
2,3-diphosphoglycerate
-
30% inhibition at 1 mM; competitive to D-ribose 5-phosphate
2,3-diphosphoglycerate
-
at 1 mM, inhibition of isoenzyme PRSI and PRSII, at 1-10 mM, stimulation of isoenzyme PRSI
2,3-diphosphoglycerate
-
-
2,3-diphosphoglycerate
-
inhibition, even in the presence of stabilizing agents such as albumin, EDTA and dithiothreitol
2-deoxy-D-ribose 5-phosphate
-
92% inhibition at 1 mM
5-phospho-alpha-D-ribose 1-diphosphate
-
competitive to ribose 5-phosphate
5-phospho-alpha-D-ribose 1-diphosphate
-
-
5-phospho-alpha-D-ribose 1-diphosphate
-
-
5-phospho-alpha-D-ribose 1-diphosphate
-
competitive with respect to ATP and noncompetitive with respect to D-ribose 5-phosphate
5-phospho-alpha-D-ribose 1-diphosphate
-
competitive with respect to ATP and noncompetitive with respect to D-ribose 5-phosphate
9-(2-phosphonylmethoxyethoxy)adenine
-
IC50 of 0.86 mM
9-(2-phosphonylmethoxyethoxy)adenine
-
IC50 of more than 2.5 mM
9-(2-phosphonylmethoxyethyl)adenine
-
IC50 of 1.9 mM
9-(2-phosphonylmethoxyethyl)adenine
-
IC50 of 2.1 mM
adenosine
-
27% inhibition at 1 mM
adenosine
-
no inhibition
adenosine 5'-(beta,gamma-imido)-triphosphate
-
inhibition at 1 mM
ADP
-
competitive inhibition to ATP
ADP
-
competitive inhibition to ATP
ADP
-
99% inhibition at 1 mM; competitive inhibition to ATP; end product inhibition; the most effective
ADP
-
non competitive with respect to ATP at 0.2 mM D-ribose-5-phosphate; the most effective
ADP
-
the most effective
ADP
-
the enzyme in MAU V cells is less sensitive than the enzyme in extracts of wild-type cells
ADP
-
when PAP39 complexes with PRSI or PRSII, the sensitivity to ADP inhibition is lowered
ADP
-
competitive inhibition to ATP
ADP
-
the most effective
ADP
-
even in the presence of stabilizing agents such as albumin, EDTA and dithiothreitol; the most effective
ADP
-
one of the most effective
ADP
-
no inhibition
ADP
-
inhibits isoenzymes PRS1 and PRS2 efficiently, but not isoenzymes PRS3 and PRS4
ADP
-
nonlinear competitive inhibition
ADP
-
at low concentrations ADP inhibition is linearly competitive with respect to ATP. Less than 1% residual activity in presence of 5 mM ADP
ADP
-
allosterical inhibition
ADP
P60891
; allosterical inhibition
ADP
-
strong inhibitor
ADP
-
strong inhibition
ADP
Q58761
a single ADP binding site, the active site, is present per subunit
allopurinol ribonucleotides
-
23% inhibition at 1 mM
alpha,beta-methylene ATP
Q58761
-
alpha,beta-methyleneATP
-
competitive inhibition to ATP
alpha,beta-methyleneATP
-
competitive inhibition to ATP
AMP
-
noncompetitive to both substrates
AMP
-
68% inhibition at 5 mM
AMP
-
69% inhibition at 1 mM
AMP
-
the enzyme in MAU V cells is less sensitive than the enzyme in extracts of wild-type cells, competitive with respect to ATP
AMP
-
non competitive with respect to D-ribose 5-phosphate and ATP
AMP
-
one of the most effective
AMP
-
no inhibition
AMP
-
noncompetitive to both substrates
AMP
-
noncompetitive with respect to D-ribose 5-phosphate and competitive with respect to ATP
ATP
-
free form, slight inhibition at 1 mM
ATP
-
free form, slight inhibition at 1 mM
ATP
-
moderate inhibition above 3 mM
ATP
-
no inhibition
Ca2+
-
inhibition even in presence of excess Mg2+
Ca2+
-
IC50 of 0.05 mM; inhibition even in presence of excess Mg2+
Ca2+
-
low concentrations of CaCl2 in the presence of an excess of MgCl2 result in a reduction in catalytic activity. At CaCl2 1 mM, the enzyme is less sensitive to ADP inhibition
Ca2+
-
inhibition even in presence of excess Mg2+
CDP
-
44% inhibition at 1 mM
CDP
-
no effect at 1 mM
CTP
-
no inhibition
CTP
-
40% inhibition at 1 mM
CTP
-
the most effective pyrimidine nucleotide inhibitor
CTP
-
no effect at 1 mM
CTP
-
weak inhibition at 1 mM
D-fructose 1,6-diphosphate
-
20% inhibition at 1 mM
D-fructose 1,6-diphosphate
-
no inhibition
D-fructose 1,6-diphosphate
-
no inhibition
D-Fructose 1-phosphate
-
19% inhibition at 1 mM
D-ribose 1-phosphate
-
13% inhibition at 1 mM
D-ribose 5-phosphate
-
substrate inhibition in presence of ADP, not in its absence
D-ribose 5-phosphate
-
substrate inhibition above 1.5 mM
D-ribose 5-phosphate
-
inhibition in presence of Ca2+, without ADP; substrate inhibition in presence of ADP, not in its absence
D-ribose 5-phosphate
-
at unsaturating phosphate concentrations
D-ribose 5-phosphate
-
-
dADP
-
competitive to ATP
dADP
-
induces substrate inhibition by D-ribose-5-phosphate
dATP
-
inhibition at 1 mM
diadenosine pentaphosphate
-
Inhibits the dephosphorylation of ATP and ADP by nonspecific phosphatases.
DL-1,4-Anhydroribitol 5-phosphate
-
competitive inhibition to D-ribose-5-phosphate
FAD
-
51% inhibition at 1 mM
GDP
-
64% inhibition at 5 mM
GDP
-
below 3-4 mM, linear competitive inhibition with respect to ATP
GDP
-
when PAP39 complexes with PRSI or PRSII, the sensitivity to ADP inhibition is lowered
GDP
-
even in the presence of stabilizing agents such as albumin, EDTA and dithiothreitol
GDP
-
one of the most effective
GDP
-
no inhibition
GDP
-
; 5 mM, less than 1% residual activity
GDP
-
the enzyme is weakly sensitive to GDP
glyceraldehyde 3-phosphate
-
14% inhibition at 1 mM
glyceraldehyde 3-phosphate
-
no inhibition
GMP
-
88% inhibition at 5 mM
GMP
-
no inhibition
GMP
-
27% inhibition at 1 mM
GMP
-
no effect at 1 mM
GMP
-
no inhibition
GSH
-
marked inhibition of enzyme in crude extract at 1 mM
GTP
-
no inhibition
GTP
-
51% inhibition at 1 mM
GTP
-
below 3-4 mM, linear competitive inhibition with respect to ATP
GTP
-
weak inhibition at 1 mM
GTP
-
no inhibition
GTP
-
substrate inhibition
guanosine
-
20% inhibition at 1 mM
guanosine
-
no inhibition
IDP
-
47% inhibition at 1 mM
IDP
-
below 3-4 mM, linear competitive inhibition with respect to ATP
IMP
-
21% inhibition at 1 mM
ITP
-
36% inhibition at 1 mM
ITP
-
below 3-4 mM, linear competitive inhibition with respect to ATP
L-histidine
-
weak inhibition or no inhibition
L-histidine
-
no inhibition
L-histidine
-
no inhibition
L-histidine
-
no inhibition
L-tryptophan
-
weak inhibition or no inhibition
L-tryptophan
-
no inhibition
L-tryptophan
-
no inhibition
L-tryptophan
-
no inhibition
NAD+
-
100% inhibition at 1 mM
NADH
-
72% inhibition at 1 mM
NADPH
-
100% inhibition at 1 mM
Nucleotides
-
-
-
Nucleotides
-
nucleoside tri- and diphosphates are more effective than nucleoside monophosphates, ribonucleotides more effective than deoxynucleotides; purines more effective than pyrimidines
-
Nucleotides
-
purines more effective than pyrimidines
-
Nucleotides
-
enzyme from HTC cells has an altered sensitivity to feedback inhibition by purine and pyrimidine nucleotides
-
phosphate
-
IC50 of 28 mM
phosphate
-
inhibition at high concentrations, more pronounced in the reverse reaction
phosphate
-
inhibition at low concentrations of D-ribose 5-phosphate
PRPP synthetase-associated proteins
-
inhibit catalytic and perhaps regulatory functions of the enzyme
-
PRPP synthetase-associated proteins
-
inhibit catalytic and perhaps regulatory functions of the enzyme
-
SO42-
-
1 M, strong inhibition
TDP
-
100% inhibition at 1 mM
TDP
-
the enzyme in MAU V cells is less sensitive than the enzyme in extracts of wild-type cells, competitive with respect to ATP
TTP
-
47% inhibition at 1 mM
UDP
-
no inhibition
UDP
-
no effect at 1 mM
UDP
-
10%-16% inhibition at 1 mM
UDP
-
10%-16% inhibition at 1 mM
UDP
-
no inhibition
UMP
-
no inhibition
UMP
-
10%-18% inhibition at 1 mM
UMP
-
10%-18% inhibition at 1 mM
UMP
-
no inhibition
UTP
-
substrate inhibition
UTP
-
weak inhibition at 1 mM
UTP
-
no inhibition
UTP
-
5.0 mM, significant inhibition
XDP
-
36% inhibition at 1 mM
XTP
-
22% inhibition at 1 mM
Mn2+
-
complete inhibition above 0.4 mM
additional information
-
GSH, 2-mercaptoethanol, 2,3-dimercaptopropanol, dithiothreitol, at 1 mM, have no effect or slightly inhibit the highly purified enzyme
-
additional information
-
-
-
additional information
-
purines are more effective than pyrimidines, nucleoside tri and diphosphates are more effective than monophosphates, ribonucleotides are more effective than deoxynucleotides
-
additional information
-
Ba2+, Fe2+, Mn2+ and Zn2+ do not inhibit at concentrations below 1 mM; purines are more effective than pyrimidines, nucleoside tri and diphosphates are more effective than monophosphates, ribonucleotides are more effective than deoxynucleotides
-
additional information
-
inhibition by pair of inhibitors tested is not greater than the sum of the inhibition produced by each alone
-
additional information
-
6-phosphogluconate, 3-phosphoglycerate, phosphoenolpyruvate and ribulose-5-phosphate have no effect on the activity; D-glucose-6-phosphate have no effects on the enzyme activity; purines are more effective than pyrimidines, nucleoside tri and diphosphates are more effective than monophosphates, ribonucleotides are more effective than deoxynucleotides
-
additional information
-
native enzyme is less sensitive to nucleotide inhibition than the major component of the enzyme, rPRSI
-
additional information
-
pyrimidine, pyridine and purine nucleotides and reaction products
-
additional information
-
D-glucose-6-phosphate have no effects on the enzyme activity; dihydroxyacetone phosphate, D-glucose-1-phosphate, fructose-6-phosphate, ribose, sucrose, glutamine, glutamic acid, aspartic acid, alanine, alpha-ketoglutarate, pyruvate, citrate, malate, fumarate, succinate, cytidine, uridine, adenine, orotate, guanine, cytosine and xanthine have no effects on the enzyme activity
-
additional information
-
no inhibitory effects are shown by the presence of pyrimidine nucleoside mono- or diphosphates or of histidine, up to 2 mM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-Aminoethylphosphonate
-
0.1 M, 13% of the activity with phosphate
arsenate
-
0.1 M, 43% of the activity with phosphate
arsenate
-
can partially replace phosphate in activation
DTT
-
requirement
phosphate
-
appears to have an effect on the stability of the enzyme as well as a specific catalytic effect; specific and absolute requirement; the enzyme has 2 sites for phosphate, one of high affinity and one of lower affinity
phosphate
-
appears to have an effect on the stability of the enzyme as well as a specific catalytic effect; specific and absolute requirement
phosphate
-
specific and absolute requirement
phosphate
-
activates at low concentrations; appears to have an effect on the stability of the enzyme as well as a specific catalytic effect; specific and absolute requirement
phosphate
-
specific and kinetically complex requirement, 25-50 mM required for optimal 5-phospho-alpha-D-ribose 1-diphosphate synthesis, 5 mM optimal for reverse reaction
phosphate
-
requirement
phosphate
-
requirement; the optimum concentration at pH 8.2 is 50-60 mM, higher concentrations are inhibitory
phosphate
-
no activity at phosphate concentrations lower than 0.4 mM; requirement
phosphate
-
optimal activity at 100 mM, slight stabilizing effect; requirement
phosphate
-
-
phosphate
-
no inhibition up to 75 mM; requirement; specific and absolute requirement
phosphate
-
activity of the enzyme is independent of phosphate. Without effect up to 80 mM
phosphate
-
its removal results in complete but reversible loss of activity; specific and absolute requirement
phosphate
-
specific and absolute requirement
phosphate
-
specific and absolute requirement
phosphate
-
activation at 1 mM of D-ribose 5-phosphate, maximal activity from 10 mM of D-ribose 5-phosphate
phosphate
-
isoenzymes PRS1 and PRS2 require phosphate for activity, isoenzymes PRS3 and PRS4 are phosphate independent
phosphate
-
isoenzyme 3 is independent of phosphate
phosphate
-
required, maximal activity at 50 mM, slowly reduced to 58% at 120 mM and 17% at 200 mM
phosphate
-
required for enzymatic activity by class 1 PRSs
phosphate
P60891
; required for enzymatic activity by class 1 PRSs
phosphate
-
the enzyme requires the presence of phosphate at a concentration of 50 mM for full activation
phosphate
-
the enzyme is dependent on phosphate for its activity. The optimal concentration ranges from 10 mM to 40 mM
phosphate
Q58761
activates, maximal activity at 190 mM phosphate
SO42-
-
can replace phosphate at about 30% of the maximal activity at a concentration of 0.5 M
SO42-
-
sulfate ions are able to stimulate the enzyme activity, but with respect to phosphate, are less effective. The optimal concentration ranges from 40 mM to 60 mM
sulfate
-
can partially replace phosphate in activation
sulfate
-
can partially replace phosphate in activation
sulfate
-
no activity observed
sulfate
P60891
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
EDTA
-
prevents inhibition by traces of cations
additional information
-
at 50 and 100 mM, KCl, KHCO3 and CH3COOK have no activating effects
-
additional information
-
no other sulfhydryl group protector or antioxidant can effectively replace DTT
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.29
-
(R)9-(2-phosphonylmethoxypropyl)adenine
-
pH 8.0, 37C
3.571
-
(R)9-(2-phosphonylmethoxypropyl)adenine
-
pH 8.0, 37C
1.14
-
(R)9-(3-fluoro-2-phosphonylmethoxypropyl)adenine
-
pH 8.0, 37C
1.923
-
(R)9-(3-fluoro-2-phosphonylmethoxypropyl)adenine
-
pH 8.0, 37C, isoenzyme I
1.54
-
(S)9-(2-phosphonylmethoxypropyl)adenine
-
pH 8.0, 37C
2.174
-
(S)9-(2-phosphonylmethoxypropyl)adenine
-
pH 8.0, 37C
0.575
-
(S)9-(3-fluoro-2-phosphonylmethoxypropyl)adenine
-
pH 8.0, 37C
3.636
-
(S)9-(3-fluoro-2-phosphonylmethoxypropyl)adenine
-
pH 8.0, 37C, isoenzyme I
0.317
-
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate
-
pH 8.0, 37C, isoenzyme II
0.323
-
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate
-
pH 8.0, 37C, isoenzyme I
0.377
-
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate
-
pH 8.0, 37C
0.0289
-
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 37C, native enzyme from liver
0.0402
-
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 37C, isoenzyme rPRSII
0.0418
-
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 37C, isoenzyme rPRSI
0.29
-
5-phospho-D-ribose diphosphate
-
pH and temperature conditions not mentioned
0.29
-
5-phospho-D-ribose diphosphate
-
pH and temperature conditions not mentioned
0.29
-
5-phospho-D-ribose diphosphate
-
pH 7.6, 37C
0.308
-
9-(2-phosphonylmethoxyethoxy)adenine
-
pH 8.0, 37C, isoenzyme I
0.422
-
9-(2-phosphonylmethoxyethoxy)adenine
-
pH 8.0, 37C
0.588
-
9-(2-phosphonylmethoxyethoxy)adenine
-
pH 8.0, 37C
0.789
-
9-(2-phosphonylmethoxyethoxy)adenine
-
pH 8.0, 37C, isoenzyme II
0.656
-
9-(2-phosphonylmethoxyethyl)adenine
-
pH 8.0, 37C, isoenzyme I
0.661
-
9-(2-phosphonylmethoxyethyl)adenine
-
pH 8.0, 37C
1.013
-
9-(2-phosphonylmethoxyethyl)adenine
-
pH 8.0, 37C, isoenzyme II
1.47
-
9-(2-phosphonylmethoxyethyl)adenine
-
pH 8.0, 37C
0.117
-
AMP
-
pH 7.4, 37C, native enzyme from liver
0.122
-
AMP
-
pH 8.0, 37C
0.123
-
AMP
-
pH 7.4, 37C, isoenzyme rPRSII
0.125
-
AMP
-
pH 7.4, 37C, isoenzyme rPRSI
0.132
-
AMP
-
pH 8.0, 37C
0.167
-
AMP
-
pH 8.0, 37C, isoenzyme II
0.263
-
AMP
-
pH 8.0, 37C, isoenzyme I
0.32
-
AMP
-
pH and temperature conditions not mentioned
0.007
-
ATP
-
pH 8.0, 37C
0.008
-
ATP
-
pH 8.0, 37C, isoenzyme I
0.023
-
ATP
-
pH 8.0, 37C
0.025
-
ATP
-
in 50 mM Tris-HCl pH 8.0, at 25C
0.044
-
ATP
-
pH 7.4, 37C, isoenzyme PRSI
0.044
-
ATP
-
pH 7.4, 37C, isoenzyme rPRSI
0.045
-
ATP
-
pH 7.4, 37C
0.049
-
ATP
-
pH 7.4, 37C, native enzyme from liver
0.05
-
ATP
-, E7EAU9
wild type enzyme, in 50 mM potassium phosphate at pH 7.5, 5 mM MgCl2, at 37C
0.051
-
ATP
-
pH 8.0, 37C, isoenzyme II
0.053
-
ATP
-
pH and temperature conditions not mentioned
0.057
-
ATP
-
mutant enzyme K199A
0.06
-
ATP
-
pH 7.4, 37C, isoenzyme PRSII
0.06
-
ATP
-
pH 7.4, 37C, isoenzyme rPRSII
0.06
-
ATP
-, E7EAU9
mutant enzyme N120S, in 50 mM potassium phosphate at pH 7.5, 5 mM MgCl2, at 37C
0.077
-
ATP
-
pH conditions not mentioned, 37C
0.083
-
ATP
-, E7EAU9
mutant enzyme D58H, in 50 mM potassium phosphate at pH 7.5, 5 mM MgCl2, at 37C
0.094
-
ATP
-, E7EAU9
mutant enzyme L135I, in 50 mM potassium phosphate at pH 7.5, 5 mM MgCl2, at 37C
0.12
-
ATP
-
mutant enzyme K197A
0.13
-
ATP
-
mutant enzyme P200A
0.14
-
ATP
-
pH 8.0, 37C
0.16
-
ATP
-
mutant enzyme V207A
0.17
-
ATP
-
pH 7.6, 37C, isoenzyme 3
0.19
-
ATP
-
mutant enzyme R198A; mutant enzyme V204A
0.191
-
ATP
-
wild-type enzyme
0.2
-
ATP
-
pH 7.5, 37C
0.23
-
ATP
-
mutant enzyme M208A
0.29
-
ATP
-
mutant enzyme P202A
0.48
-
ATP
-
mutant enzyme E206A
0.56
-
ATP
-
mutant enzyme R201A
0.66
-
ATP
-
pH 8.2, 37C
0.87
-
ATP
-
mutant enzyme N203A
1.127
-
ATP
-
pH 8.0, 37C
2.6
-
ATP
Q58761
pH and temperature not specified in the publication
0.116
-
CTP
-
pH 7.6, 37C, isoenzyme 3
0.0082
-
D-ribose 5-phosphate
-
at pH 7.5 and 37C
0.014
-
D-ribose 5-phosphate
-
cosubstrate ATP, in 50 mM Tris-HCl pH 8.0, at 25C
0.038
-
D-ribose 5-phosphate
-
pH and temperature conditions not mentioned
0.04
-
D-ribose 5-phosphate
-
pH 7.4, 37C, isoenzyme PRSI
0.04
-
D-ribose 5-phosphate
-
pH 7.4, 37C, isoenzyme rPRSI
0.04
-
D-ribose 5-phosphate
-
pH 7.5, 37C
0.048
-
D-ribose 5-phosphate
-
pH conditions not mentioned, 37C
0.05
0.13
D-ribose 5-phosphate
-
pH 7.5, 37C
0.052
-
D-ribose 5-phosphate
-
pH 7.5, 37C, isoenzyme PRSI
0.052
-
D-ribose 5-phosphate
-
pH and temperature conditions not mentioned, rPRSI isoenzyme
0.06
-
D-ribose 5-phosphate
-
in the presence of 5 mM Mn2+, in 50 mM potassium phosphate pH 8.0, at 37C
0.064
-
D-ribose 5-phosphate
-
pH 7.4, 37C, native enzyme from liver
0.07
-
D-ribose 5-phosphate
-
in the presence of 5 mM Mg2+, in 50 mM potassium phosphate pH 8.0, at 37C
0.071
-
D-ribose 5-phosphate
-
in the absence of Mg2+ or Mn2+, in 50 mM potassium phosphate pH 8.0, at 37C
0.073
-
D-ribose 5-phosphate
-
pH 7.4, 37C, isoenzyme PRSII
0.073
-
D-ribose 5-phosphate
-
pH 7.4, 37C, isoenzyme rPRSII
0.083
-
D-ribose 5-phosphate
-
pH 7.5, 37C, isoenzyme PRSII
0.083
-
D-ribose 5-phosphate
-
pH and temperature conditions not mentioned, rPRSII isoenzyme
0.105
-
D-ribose 5-phosphate
-, E7EAU9
wild type enzyme, in 50 mM potassium phosphate at pH 7.5, 5 mM MgCl2, at 37C
0.107
-
D-ribose 5-phosphate
-
mutant enzyme K199A
0.11
-
D-ribose 5-phosphate
-
pH 7.6, 37C, isoenzyme 3
0.135
-
D-ribose 5-phosphate
-
pH 8.0, 37C
0.157
-
D-ribose 5-phosphate
-, E7EAU9
mutant enzyme D58H, in 50 mM potassium phosphate at pH 7.5, 5 mM MgCl2, at 37C
0.16
-
D-ribose 5-phosphate
-
pH and temperature conditions not mentioned
0.18
-
D-ribose 5-phosphate
-, E7EAU9
mutant enzyme N120S, in 50 mM potassium phosphate at pH 7.5, 5 mM MgCl2, at 37C
0.189
-
D-ribose 5-phosphate
-, E7EAU9
mutant enzyme L135I, in 50 mM potassium phosphate at pH 7.5, 5 mM MgCl2, at 37C
0.19
-
D-ribose 5-phosphate
-
pH 8.0, 37C, phosphate 50 mM
0.2
-
D-ribose 5-phosphate
-
pH 7.4, 37C
0.217
-
D-ribose 5-phosphate
-
mutant enzyme K197A
0.23
-
D-ribose 5-phosphate
-
wild-type enzyme
0.298
-
D-ribose 5-phosphate
-
pH 8.0, 37C
0.41
-
D-ribose 5-phosphate
-
pH conditions not mentioned, 37C, mutant enzyme
0.48
-
D-ribose 5-phosphate
-
pH 8.2, 37C
0.53
-
D-ribose 5-phosphate
-
-
0.57
-
D-ribose 5-phosphate
-
pH conditions not mentioned, 37C, wild type enzyme
0.791
-
D-ribose 5-phosphate
-
pH 8.0, 37C
2.8
-
D-ribose 5-phosphate
Q58761
pH and temperature not specified in the publication
0.233
-
dATP
-
pH 7.6, 37C, isoenzyme 3
0.65
-
GTP
-
pH 7.6, 37C, isoenzyme 3
0.0002
-
Mg2+
-
pH 7.4, 37C
0.041
-
Mg2+
-
pH 8.0, 37C, phosphate 50 mM
0.059
-
Mg2+
-
pH 8.0, 37C, phosphate 5 mM
0.07
-
Mg2+
-
pH 7.5, 37C, isoenzyme PRSI
0.11
-
Mg2+
-
pH 7.5, 37C, isoenzyme PRSII
0.2
-
Mg2+
-
pH and temperature conditions not mentioned
0.6
-
Mg2+
-
pH and temperature conditions not mentioned
1.5
-
Mg2+
-
pH 7.5, 37C
0.014
-
MgATP2-
-
pH and temperature conditions not mentioned
0.014
-
MgATP2-
-
pH 7.4, 37C
0.021
-
MgATP2-
-
pH 7.5, 37C, isoenzyme PRSI
0.021
-
MgATP2-
-
pH and temperature conditions not mentioned, rPRSI isoenzyme
0.03
-
MgATP2-
-
pH conditions not mentioned, 37C, wild type and mutant enzyme
0.046
-
MgATP2-
-
pH and temperature conditions not mentioned
0.078
-
MgATP2-
-
pH 7.6, 37C, 100 mM phosphate
0.1
-
MgATP2-
-
pH 7.5, 37C, excess of Mg2+, bimodal kinetic behavior
0.22
-
MgATP2-
-
pH and temperature conditions not mentioned
0.22
-
MgATP2-
-
pH 7.6, 37C, excess of Mg2+
0.58
-
MgATP2-
-
pH 7.5, 37C, excess of Mg2+, bimodal kinetic behavior
2.9
-
MgATP2-
-
pH 7.5, 37C, no excess of Mg2+
0.06
-
MnATP2-
-
pH 7.5, 37C, excess of Mn2+
0.008
-
phosphate
-
pH 7.4, 37C
0.7
-
phosphate
-
pH 7.5, 37C, isoenzyme PRSI
2.1
-
phosphate
-
pH 7.5, 37C, isoenzyme PRSII
2.3
-
phosphate
-
pH 7.5, 37C, high affinity site
40
-
phosphate
-
pH 7.5, 37C, low affinity site
0.033
-
ribose 5-phosphate
-
pH and temperature conditions not mentioned
0.033
-
ribose 5-phosphate
-
pH 7.4, 37C
0.137
-
UTP
-
pH 7.6, 37C, isoenzyme 3
0.35
-
MnATP2-
-
pH 7.5, 37C, no excess of Mn2+
additional information
-
additional information
-
increasing phosphate concentrations, increases Km values for ATP and D-ribose-5-phosphate
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.66
-
ATP
-
in 50 mM Tris-HCl pH 8.0, at 25C
35.1
-
D-ribose 5-phosphate
-
in the presence of 5 mM Mg2+, in 50 mM potassium phosphate pH 8.0, at 37C
37
-
D-ribose 5-phosphate
-
in the absence of Mg2+ or Mn2+, in 50 mM potassium phosphate pH 8.0, at 37C
44.7
-
D-ribose 5-phosphate
-
in the presence of 5 mM Mn2+, in 50 mM potassium phosphate pH 8.0, at 37C
60.68
-
D-ribose 5-phosphate
-
cosubstrate ATP, in 50 mM Tris-HCl pH 8.0, at 25C
34.6
-
Mg-ATP2-
-
in the presence of 5 mM Mg2+, in 50 mM potassium phosphate pH 8.0, at 37C
35.5
-
Mg-ATP2-
-
in the absence of free Mg2+ or Mn2+, in 50 mM potassium phosphate pH 8.0, at 37C
44.3
-
Mg-ATP2-
-
in the presence of 5 mM Mn2+, in 50 mM potassium phosphate pH 8.0, at 37C
45.1
-
Mn-ATP2-
-
in the presence of 5 mM Mn2+, in 50 mM potassium phosphate pH 8.0, at 37C
46.3
-
Mn-ATP2-
-
in the absence of free Mg2+ or Mn2+, in 50 mM potassium phosphate pH 8.0, at 37C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
26
-
ATP
-
in 50 mM Tris-HCl pH 8.0, at 25C
4
59
-
D-ribose 5-phosphate
-
cosubstrate ATP, in 50 mM Tris-HCl pH 8.0, at 25C
183
501.4
-
D-ribose 5-phosphate
-
in the presence of 5 mM Mg2+, in 50 mM potassium phosphate pH 8.0, at 37C
183
521
-
D-ribose 5-phosphate
-
in the absence of Mg2+ or Mn2+, in 50 mM potassium phosphate pH 8.0, at 37C
183
745
-
D-ribose 5-phosphate
-
in the presence of 5 mM Mn2+, in 50 mM potassium phosphate pH 8.0, at 37C
183
7430
-
D-ribose 5-phosphate
-
at pH 7.5 and 37C
183
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.41
-
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate
-
pH 8.0, 37C
0.55
-
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate
-
pH 8.0, 37C
0.03
-
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.5, 37C
0.1
-
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.4, 37C
0.16
-
5-phospho-alpha-D-ribose 1-diphosphate
-
pH conditions not mentioned, 37C, ATP as substrate, Kis value
0.33
-
5-phospho-alpha-D-ribose 1-diphosphate
-
pH conditions not mentioned, 37C, D-ribose 5-phosphate as substrate, Kis value
0.52
-
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.6, 37C, ATP as substrate, isoenzyme 3
0.82
-
5-phospho-alpha-D-ribose 1-diphosphate
-
pH 7.6, 37C, 5-phospho-alpha-D-ribose 1-diphosphate as substrate, isoenzyme 3
2.2
-
5-phospho-alpha-D-ribose 1-diphosphate
-
pH conditions not mentioned, 37C, D-ribose 5-phosphate as substrate, Kii value
1.4
-
9-(2-phosphonylmethoxyethoxy)adenine
-
pH 8.0, 37C
0.37
-
9-(2-phosphonylmethoxyethyl)adenine
-
pH 8.0,37C
1.9
-
9-(2-phosphonylmethoxyethyl)adenine
-
pH 8.0, 37C
0.01
-
ADP
-
pH 7.4, 37C, wild-type cells
0.01
-
ADP
-
pH conditions and temperature conditions not mentioned
0.057
-
ADP
Q58761
pH and temperature not specified in the publication
0.11
-
ADP
-
pH conditions not mentioned, 37C, ATP as substrate, Kis value
0.15
-
ADP
-
pH and temperature conditions not mentioned
0.175
-
ADP
-
pH 7.4, 37C, MAU V cells
0.334
-
ADP
-
pH 8.0, 37C, D-ribose 5-phosphate 0.5 mM, Kii value
0.522
-
ADP
-
at pH 7.5 and 37C
0.68
-
ADP
-
pH 7.6, 37C, ATP as substrate, isoenzyme 3
1.22
-
ADP
-
pH 7.6, 37C, 5-phospho-alpha-D-ribose 1-diphosphate as substrate, isoenzyme 3
0.85
-
alpha,beta-methylene ATP
Q58761
pH and temperature not specified in the publication
0.03
-
alpha,beta-methyleneATP
-
pH and temperature conditions not mentioned
0.01
-
AMP
-
pH 7.4, 37C, wild-type cells
0.1
-
AMP
-
pH 7.4, 37C, MAU V cells
0.3
-
AMP
-
pH 7.4, 37C, with D-ribose-5-phosphate
0.38
-
AMP
-
pH conditions not mentioned, 37C, D-ribose 5-phosphate as substrate, Kis value
0.4
-
AMP
-
pH 7.4, 37C, with MgATP2-
0.43
-
AMP
-
pH conditions not mentioned, 37C, ATP as substrate, Kis value
0.45
-
AMP
-
pH 7.6, 37C, 5-phospho-alpha-D-ribose 1-diphosphate as substrate, isoenzyme 3
1.62
-
AMP
-
pH 7.6, 37C, ATP as substrate, isoenzyme 3
3.9
-
AMP
-
pH conditions not mentioned, 37C, D-ribose 5-phosphate as substrate, Kii value
5.6
-
AMP
-
pH conditions not mentioned, 37C, ATP as substrate, Kii value
0.167
-
ATP
-
mutant enzyme K197A
0.323
-
ATP
-
mutant enzyme K199A
1.089
-
ATP
-
wild-type enzyme
0.032
-
Ca2+
-
pH 8.0, 37C, D-ribose 5-phosphate 5 mM, Kis value
0.047
-
Ca2+
-
pH 8.0, 37C, D-ribose 5-phosphate 5 mM, Kii value
0.053
-
Ca2+
-
pH 8.0, 37C, D-ribose 5-phosphate 0.5 mM, Kis value
0.11
-
Ca2+
-
pH 8.0, 37C, D-ribose 5-phosphate 0.5 mM, Kii value
0.211
-
D-ribose 5-phosphate
-
cosubstrate ATP, in 50 mM Tris-HCl pH 8.0, at 25C
0.716
-
D-ribose 5-phosphate
-
pH 8.0, 37C, Kii value
1.18
-
D-ribose 5-phosphate
-
pH 8.0, 37C, Kis value
10
-
DL-1,4-Anhydroribitol 5-phosphate
-
pH and temperature conditions not mentioned
0.15
-
TDP
-
pH 7.4, 37C, wild-type cells
0.75
-
TDP
-
pH 7.4, 37C, MAU V cells
0.02
-
Mn2+
-
pH 7.5, 37C
additional information
-
additional information
-
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.86
-
9-(2-phosphonylmethoxyethoxy)adenine
-
IC50 of 0.86 mM
2.5
-
9-(2-phosphonylmethoxyethoxy)adenine
-
IC50 of more than 2.5 mM
1.9
-
9-(2-phosphonylmethoxyethyl)adenine
-
IC50 of 1.9 mM
2.1
-
9-(2-phosphonylmethoxyethyl)adenine
-
IC50 of 2.1 mM
0.07
-
ADP
-, E7EAU9
mutant enzyme D58H, in 50 mM potassium phosphate at pH 7.5, 5 mM MgCl2, at 37C
0.07
-
ADP
-
in 50 mM Tris-HCl pH 8.0, at 25C
0.08
-
ADP
-, E7EAU9
wild type enzyme, in 50 mM potassium phosphate at pH 7.5, 5 mM MgCl2, at 37C
0.44
-
ADP
-, E7EAU9
mutant enzyme N120S, in 50 mM potassium phosphate at pH 7.5, 5 mM MgCl2, at 37C
0.84
-
ADP
-, E7EAU9
mutant enzyme L135I, in 50 mM potassium phosphate at pH 7.5, 5 mM MgCl2, at 37C
0.4
-
GDP
-
in 50 mM potassium phosphate pH 8.0, at 37C
0.45
-
GDP
-, E7EAU9
wild type enzyme, in 50 mM potassium phosphate at pH 7.5, 5 mM MgCl2, at 37C
0.51
-
GDP
-, E7EAU9
mutant enzyme D58H, in 50 mM potassium phosphate at pH 7.5, 5 mM MgCl2, at 37C
0.9
-
GDP
-
in 50 mM Tris-HCl pH 8.0, at 25C
1
-
GDP
-, E7EAU9
IC50 above 1 mM, mutant enzyme L135I, in 50 mM potassium phosphate at pH 7.5, 5 mM MgCl2, at 37C; IC50 above 1 mM, mutant enzyme N120S, in 50 mM potassium phosphate at pH 7.5, 5 mM MgCl2, at 37C
5
-
GDP
-
in 50 mM potassium phosphate pH 8.0, at 37C
28
-
phosphate
-
IC50 of 28 mM
100
-
phosphate
-
in 50 mM potassium phosphate pH 8.0, at 37C
3
-
UMP
-
in 50 mM Tris-HCl pH 8.0, at 25C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.001
-
-
mitochondria preparation
0.004
-
-
chloroplast preparation
0.01
-
-
wild-type strain
0.011
0.012
-
mutant strain GPD-PRS2,4, engineered gene AGR371C
0.014
-
-
isoenzyme PRS1, without phosphate and ADP
0.016
-
-
mutant enzyme G209V, at pH 7.5 and 37C
0.017
0.018
-
mutant strain GPD-PRS3, engineered gene AGL080C
0.018
-
-
isoenzyme PRS2, in the presence of phosphate 50 mM, and ADP 1 mM
0.025
-
-
isoenzyme PRS2, without phosphate and ADP
0.027
-
-
mutant enzyme D224A, at pH 7.5 and 37C
0.028
-
-
crude extract, in 50 mM Tris-HCl pH 8.0, at 25C
0.032
-
-
mutant enzyme G50D, at pH 7.5 and 37C
0.041
-
-
mutant enzyme E306K, at pH 7.5 and 37C
0.054
-
-
mutant enzyme A181D, at pH 7.5 and 37C
0.072
-
-
isoenzyme PRS4, in the presence of phosphate 50 mM, and ADP 1 mM
0.074
-
-
isoenzyme PRS1, in the presence of phosphate 50 mM, and ADP 1 mM
0.08
-
-
isoenzyme PRS4, in the presence of phosphate 50 mM, without ADP
0.089
-
-
isoenzyme PRS4, without phosphate and ADP
0.094
-
-
wild type enzyme, at pH 7.5 and 37C
0.099
-
-
isoenzyme PRS4, in the presence of ADP 1 mM, without phosphate
0.14
-
-
isoenzyme PRS2, in the presence of phosphate 50 mM, without ADP
0.191
-
-
isoenzyme PRS1, in the presence of phosphate 50 mM, without ADP
0.88
-
-
isoenzyme PRS3, in the presence of phosphate 50 mM, and ADP 1 mM
0.884
-
-
isoenzyme PRS3, in the presence of ADP 1 mM, without phosphate
1.06
-
-
isoenzyme PRS3, in the presence of phosphate 50 mM, without ADP
1.16
-
-
after 41.4fold purification, in 50 mM Tris-HCl pH 8.0, at 25C
1.26
-
-
isoenzyme PRS3, without phosphate and ADP
2.45
-
-
native enzyme from liver, reverse reaction, pH 8.6
3.59
-
-
native enzyme from liver, reverse reaction, pH 7.4
3.65
-
-
wild type enzyme
4.24
-
-
isoenzyme rPRSII, reverse reaction, pH 8.6
4.5
-
-
isoenzyme rPRSI, reverse reaction, pH 8.6
7.48
-
-
isoenzyme rPRSI, reverse reaction, pH 7.4
8.04
-
-
isoenzyme rPRSII, reverse reaction, pH 7.4
8.17
-
-
mutant enzyme
8.3
-
-
isoenzyme rPRSII, pH 8.6
10.4
-
-
liver enzyme complex with PAP39 and PRS at a mass ratio of 0.34
16.2
-
-
native enzyme from liver, pH 8.6
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
25.7
-
-
isoenzyme PRSI
34.5
-
-
isoenzyme PRSII
35.7
-
-
isoenzyme PRSII
39.1
-
-
isoenzyme rPRSI, pH 8.6
190
-
-
30fold to 50fold more activity in the cloned enzyme than in the enzyme from the wild-type cells
additional information
-
-
26.8 U/mg protein, purified enzyme, 400fold to 450fold the activity of crude extract
additional information
-
-
10fold greater in cytosol than in the particulate fraction
additional information
-
-
the enzyme activity rises at the start of the S phase of the cell cycle, apparently in association with the rate of DNA synthesis
additional information
-
-
the specific activity of the catalytic subunit is lower in the complexes where the amount of PRPP synthetase-associated protein of 39000 Da, PAP39, is higher. Increasing amounts of PAP39 have strong inhibitory effects on the catalytic activity
additional information
-
-
-
additional information
-
-
33400 U/mg and 46200 U/mg for PRSI and PRSII purified isoenzymes, respectively; purified enzyme has an activity of 7280 U/mg
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.2
7.4
-
erythrocyte enzyme
7.4
-
-
isoenzyme PRSII
7.4
-
-
rPRSII
7.5
-
-
at 40-50 mM phosphate, isoenzymes PRSI and PRSII
7.5
-
-
assay at
7.6
-
-
activity increases up to pH 7.2 and decreases above pH 7.6
8
-
P60891
assay at
8
-
-
the enzyme shows an optimum at a pH value close to 8.0
8.1
8.6
-
for either the Mg2+ or the Mn2+ supported reaction
8.5
-
-
native enzyme from liver
8.5
-
-
37C, in Tris/ClH buffer
8.7
-
-
rPRSI
8.8
-
-
isoenzyme PRSI
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
9.5
-
the enzyme shows activity across a broad range of pH levels (4.5-9.5) and is only found to be inactive at high pH 10.5
6
9.5
-
very low activity below and above
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
6.5
9.5
-
pH 6.5: about 25% of maximal activity, pH 9.5: about 80% of maximal activity
7
9.5
-
at pH 7 and pH 9.5, about 35% and 85% of the maximal activity, respectively
7
9.5
-
the enzyme possesses nearly 70% of its maximal activity at pH 9.5. The activity at pH 7 is 57% of the maximal one at pH 8.0
10
-
Q58761
the activity profile declines steeply above pH 10. At least in part, this reduction in activity at high pH values may be caused by the formation of a magnesium phosphate precipitate, and consequently cause Mg2+ depletion. At lower pH the activity increases more or less linearly from pH 6.0 to pH 9.5
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
30
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
P60891
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
72
95
Q58761
70% of maximal activity at 72C and 95C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.3
4.4
-
isoenzyme rPRSII
4.4
-
-
isoenzyme rPRSI
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
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
isoenzymes PRSI and PRSII
Manually annotated by BRENDA team
-
isoenzyme PRSI
Manually annotated by BRENDA team
-
from normal patients and patients with excessive activity of the enzyme
Manually annotated by BRENDA team
-
fetal, RSa cells, UV sensitive clonal cells
Manually annotated by BRENDA team
-
initiated from normal skin biopsies
Manually annotated by BRENDA team
-
cell line of rat hepatoma cells in continuous culture, clone MAU V with an inreased ability to salvage exogenous purines
Manually annotated by BRENDA team
-
isoenzyme PRSII
Manually annotated by BRENDA team
-
isoenzyme PRSII
Manually annotated by BRENDA team
-
isoenzymes PRSI and PRSII
Manually annotated by BRENDA team
-
isoenzymes PRSI and PRSII
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
more than 95% of the total activity
Manually annotated by BRENDA team
-
60% of the total activity, fractionation by discontinuous sucrose density gradient centrifugation
Manually annotated by BRENDA team
-
also known as latex in specialized cells
Manually annotated by BRENDA team
-
30% of the total activity, fractionation by discontinuous sucrose density gradient centrifugation
-
Manually annotated by BRENDA team
-
80% of the liver enzyme is found in the mitochondria
Manually annotated by BRENDA team
-
15% of the liver enzyme is found in the nucleus
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Burkholderia pseudomallei (strain K96243)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
55000
-
Q97CA5, -
gel filtration
147000
-
Q58761
gel filtration
186000
-
-, E7EAU9
gel filtration
200000
340000
-
sucrose density gradient sedimentation
200000
-
-
gel filtration
220000
-
-
gel filtration
250000
600000
-
sucrose density gradient sedimentation
280000
-
-
gel filtration
500000
700000
-
gel filtration
540000
-
-
sucrose density gradient sedimentation
550000
-
-
gel filtration, cloned and purified rPRSII
700000
1200000
-
sucrose density gradient sedimentation and gel filtration
700000
1200000
-
-
700000
1200000
-
gel filtration, cloned and purified rPRSI
1000000
-
-
gel filtration, isoenzymes PRSI and PRSII
1000000
-
-
gel filtration
1000000
-
-
HPLC, in the presence of Mg2+ and ATP
1000000
-
-
-
1000000
-
-
chromatography on DEAE-Toyopearl
additional information
-
-
enzyme occurs in multiple states of aggregation; the distribution among the states of aggregation is altered by a variety of conditions
additional information
-
-
enzyme occurs in multiple states of aggregation
additional information
-
-
-
additional information
-
-
enzyme occurs in multiple states of aggregation
additional information
-
-
purified enzyme is in an aggregated state
additional information
-
-
enzyme occurs in multiple states of aggregation
additional information
-
-
-
additional information
-
-
-
additional information
-
-
enzyme occurs in multiple states of aggregation
additional information
-
-
purified enzyme appears to exist as complex aggregates composed of heterogeneous components
additional information
-
-
the catalytic subunit complexes with the PRPP synthetase-associated protein of 39000 Da, PAP39, to form highly aggregated forms
additional information
-
-
enzyme occurs in multiple states of aggregation; 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
additional information
-
-
-
additional information
-
-
the catalytic subunit complexes with the PRPP synthetase-associated protein of 39000 Da, PAP39, to form highly aggregated forms
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 50000 + x * 34000 + x * 39000 + x * 41000, subunit of 34000 Da is the catalytic subunit
?
-
x * 34500, SDS-PAGE; x * 43000, sucrose density gradient sedimentation in the presence of urea 2 M combined with values of gel filtration; x * 53000, sucrose density gradient sedimentation in the presence of NaCl, 1 M, combined with values of gel filtration; x * 60000, sucrose density gradient sedimentation in phosphate buffer combined with values of gel filtration
?
-
x * 40000, SDS-PAGE with mercaptoethanol
?
-
x * 30400, sedimentation equilibrium analysis of enzyme dissociated in 6 M guanidine hydrochloride; x * 33800, SDS-PAGE
?
-
x * 34000, SDS-PAGE, cloned and purified isoenzymes PRSI and PRSII
?
-
x * 40500, disc gel electrophoresis in SDS
?
-
x * 32000, SDS-PAGE
?
-
x * 34000 + x * 38000 + x * 40000, SDS-PAGE, the 34000 Da subunit is the catalytic subunit
?
-
x * 34600, isoenzyme PRSII; x * 34700, isoenzyme PRSI
?
-
x * 34000 + x * 39000 + x * 41000, SDS-PAGE, the 34000 Da subunit is the catalytic subunit which appears as PRSI or PRSII; x * 68000, gel filtration in the presence of MgCl2 1 M
?
-
x * 57000, SDS-PAGE
?
Salmonella enterica subsp. enterica serovar Typhimurium LT-2
-
-
-
?
Salmonella enterica subsp. enterica serovar Typhimurium Su 422
-
; x * 30400, sedimentation equilibrium analysis of enzyme dissociated in 6 M guanidine hydrochloride; x * 33800, SDS-PAGE
-
heterodimer
Emericella nidulans
-
-
heterodimer
Emericella nidulans WJA01
-
-
-
hexamer
-
6 * 34497, MALDI-TOF
hexamer
-
the enzyme predominates as a hexamer, glutaraldehyde cross-linking
hexamer
Mycobacterium tuberculosis Rv1017c
-
the enzyme predominates as a hexamer, glutaraldehyde cross-linking
-
homodimer
P60891
-
homohexamer
-
6 * 35000, SDS-PAGE
octamer
-
8 * 34000, SDS-PAGE
pentamer
-
5 * 31000, physical and electron microscopic studies
pentamer
Salmonella enterica subsp. enterica serovar Typhimurium LT-2, Salmonella enterica subsp. enterica serovar Typhimurium Su 422
-
5 * 31000, physical and electron microscopic studies
-
tetramer
Q58761
4 * 32229, calculated from sequence
homohexamer
Mycobacterium tuberculosis Rv1017
-
6 * 35000, SDS-PAGE
-
additional information
-
from X-ray diffraction, the structure is determined to be an hexamer
additional information
-
three catalytic isoenzymes of identical length and two PRPP synthetase-associated proteins of 39000 and 41000 Da
additional information
-
the functional form of the enzyme is a homohexamer
additional information
-
the molecular mass of the enzyme corresponds to about 30 subunits, six times larger than a pentamer which is the smallest active oligomer known
additional information
-
expression of the five PRS genes individually in an Escherichia coli PRPP-less strain shows that a single PRS gene product has no PRPP synthase activity. Certain pairwise combinations of subunits produce an active enzyme, yeast PRPP synthase requires at least three different subunits to be stable in vitro
additional information
P60891
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging-drop vapour diffusion method
-
in combination with dynamic light scattering studies
-
in the presence of Mg2+
-
sitting drop vapor diffusion
-
X-ray diffraction
-
hanging-drop vapour diffusion method; purified recombinant enzyme in complex with Cd2+, ATP or sulfate, hanging drop vapour diffusion method, 20C, X-ray diffraction structure determination and analysis at 2.20 A resolution
P60891
hanging-drop vapour-diffusion technique
Q58761
hanging-drop vapour-diffusion method. Orthorhombic system, with space group P2(1)2(1)2 and unit-cell parameters a = 213.2, b = 152.6, c = 149.3 A. The crystals diffract to a maximum resolution of 3.3 A
-
in complex with its substrate D-ribose 5-phosphate and with substrate analogs beta,gamma-methylene ATP and ADP, hanging drop vapor diffusion method, using 2 M ammonium sulfate, pH 4.0 or 30% (w/v) polyethylene glycol 600, pH 7.5
Q97CA5, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
the enzyme retains over 70% of the activity
7.4
-
-
85% of maximal activity, isoenzyme PRSI
7.4
-
-
62% of maximal activity, native enzyme from liver; 66% of maximal activity, isoenzyme rPRSI
8.7
-
-
20% of maximal activity, isoenzyme rPRSII
8.8
-
-
41% of maximal activity, isoenzyme PRSII
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
49
-
-
half-life of 0.5 min and 90 min for isoenzymes rPRSII and rPRSI, respectively
49
-
-
half-life of 250 min, 90 min and 0.5 min for native enzyme, isoenzymes rPRSI and rPRSII, respectively
49
-
-
-
49
-
-
half-life of 250 min, 90 min and 0.5 min for native enzyme, isoenzymes rPRSI and rPRSII, respectively
55
-
-
isoenzyme PRSII is more thermolabile than PRSI. After 10 min, isoenzyme PRSI loses about 30% of activity, isoenzyme PRSII, about 85% of activity
55
-
-
inactivation of mutant enzyme proceeds faster than that of normal enzyme
61
-
-
transition temperature of mutant enzyme K197A is 61.2C
62
74
-
a highly stable enzyme, losing 50% of its activity in 10 min of incubation at 62C, and showing a Tm of 69.3C (without ligands) to 74.5C (in the presence of 5 mM Mg-ATP)
63
-
-
transition temperature of wild-type enzyme is 62.8C, transition temperature of mutant enzyme R199A is 62.6C
65
-
-
half-life: 26 min; half-life: 60 s
85
-
Q58761
at pH 9.0, half-life: 8 min
additional information
-
-
isoenzyme PRSII is more thermolabile than PRSI
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Lys197 and Arg199 are important in stabilization of the transition state
-
relatively stable in absence of phosphate
-
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 4C. Dilution of isoenzyme PRSI to 0.1 mg/ml lacking Mg2+ and ATP results in loss of 10% activity after 3h at 4C
-
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
-
dialysis against buffers such as 50 mM Tris-HCl, pH 8.0 or 50 mM HEPES-NaOH, pH 8.0 without phosphate results in a protein precipitation and complete loss of activity. The addition of 50 mM ammonium sulfate or 5 mM Mg-ATP to Tris-HCl, pH 8.0 allows the enzyme to preserve 20% of initial activity after a period of 16 h, whereas full activity is maintained with the addition of 50 mM phosphate
-
addition of albumin, EDTA or sulfhydryl compounds to the assay prevents loss of activity
-
high enzyme concentration, albumin, 0.05 mg/ml, EDTA, 1 mM or DTT, 1 mM stabilizes during assay
-
completely inactivated when phosphate is removed by dialysis
-
repeated freezing and thawing slowly denatures the enzyme. Irreversible denaturation by reduction of the phosphate concentration to less than 5 mM, requires 25 mM phosphate or higher for complete stability. Mg2+ ions and ATP stabilize the enzyme but will not replace phosphate
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-70C, glycerol 10%, stable
-
stored and diluted in the presence of phosphate 50 mM to maintain stability. With 2 mM MgATP2- or more, the enzyme is fully stable upon dilution and subsequent incubation at 37C
-
4C or -20C in 25 mM TrisHCl (pH 7.6), 50% (v/v) glycerol, purified enzyme is stable for at least 90 days when stored at
Q58761
-80C, 50 mM Tris-HCl (pH 7.5), up to 7 months, no loss of activity
-
-80C, potassium phosphate 50 mM, pH 7.4
-
-80C, potassium phosphate buffer, pH 7.4, stable
-
4C, 50% loss of activity after 2 months. -20C, rapid loss of activity
-
4C, 50% loss of activity after 2 months. -20C, more rapid loss of activity. Presence of substrates enhances stability during storage
-
4C, without stabilizing agents, half-life of inactivation of 21, 8 and 1 hours for native enzyme, isoenzymes rPRSI and rPRSII, respectively
-
-20C, 50 mM potassium phosphate buffer, pH 7.5 after rapid freezing in CO2-acetone, quite stable
-
0C or -10C, 50 mM potassium phosphate buffer, pH 7.4, stable for weeks
-
-20C, Tris/HCl buffer 50 mM, pH 7.6, 50% glycerol, stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
HisTrap column chromatography and Sephadex G-25 gel filtration
-, E7EAU9
recombinant
-
streptomycin-heat treatment, ammonium sulfate fractionation, chromatography on DEAE-Sepharose and affinity chromatography
-
ammonium sulfate fractionation, chromatography on Sephacryl S300 HR and on Protein-Pak DEAE 40 HR and affinity chromatography
-
4500fold purification
-
partial, 400fold purification
-
recombinant His-tagged PRS1 from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
P60891
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
-
ammonium sulfate precipitation, Q-Sepharose column chromatography, Superdex 200 gel filtration, and Mono Q column chromatography
-
His-Trap HP column chromatography and Superdex 200 gel filtration
-
Ni2+-NTA agarose column chromatography
-
acetone powder, acid and streptomycin precipitation, ammonium sulfate fractionation, heat treatment and agarose gel filtration, 3400fold purification, presence of substrates enhances stability during purification
-
acetone powder, acid and streptomycin precipitation, heat treatment and agarose chromatography, 1500 to 3000fold purification
-
gel filtration
-
polyethylene glycol and acid precipitation
-
polyethylene glycol precipitation, hydroxyapatite fractionation, gel filtration on Toyopearl HW-65F, chromatography on DEAE-Toyopearl 650S and gel filtration
-
polyethylene glycol, acid precipitation and chromatography on DEAE-5PW HPLC, purification of the two isoforms PRSI and PRSII
-
Ni2+ resin column chromatography
-
ammonium sulfate and isoelectric precipitations, purified to near homogeneity
-
extraction, streptomycin-heat treatment, ammonium sulfate and acid precipitation, 450fold purification
-
extraction, streptomycin-heat treatment, ammonium sulfate and acid precipitation, affinity chromatography
-
ammonium sulfate and polyethylene glycol precipitation, affinity chromatography and anion exchange chromatography, purification of isoenzyme 3
-
ammonium sulfate fractionation, chromatography on DEAE-cellulose and ultrafiltration
-
streptomycin sulfate and ammonium sulfate precipitation, chromatography on Dyematrex Gel Blue B and DE52
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-, E7EAU9
expression in Escherichia coli
-
expression in Escherichia coli
-
produced in an Escherichia coli strain lacking endogenous phosphoribosyl diphosphate synthase activity
-
expressed in Aedes albopictus C6/36 cell line
-, H9D1K2
genes AGR371C and AGL080C, overexpression of wild-type and mutant deregulated isozymes Agr371cp and Agl080cp, phylogenetic tree of the PRS proteins from Ashbya gossypii and Saccharomyces cerevisiae
-
overexpression of wild-type and mutant enzymes in Arabidopsis thaliana and Nicotiana tabacum, ectopic expression of heterologous PRS activity in the cytosol
-
expression in Escherichia coli
-
expression of isoenzymes PRSI and PRSII in Escherichia coli
-
gene PRPS1, genomic structure, genotyping in European and Asian individuals
P60891
gene PRS1 from a cDNA library, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
P60891
expressed in Escherichia coli
Q58761
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3)pLysS cells
-
expressed in Escherichia coli C41 cells
-
expression in Escherichia coli
-
expression of isoenzymes PRSI and PRSII in Escherichia coli
-
expression of the five PRS genes individually in an Escherichia coli PRPP-less strain shows that a single PRS gene product has no PRPP synthase activity. Certain pairwise combinations of subunits produce an active enzyme, yeast PRPP synthase requires at least three different subunits to be stable in vitro
-
expressed in Escherichia coli BL21(AI) cells
-
expression in Escherichia coli
-
expression of isoenzyme 3 in Escherichia coli
-
expression of isoenzymes PRS1, PRS2, PRS3 and PRS4 in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
Q97CA5, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D58H
-, E7EAU9
the mutant exhibits nearly identical sensitivity to ADP and GDP as the wild-type protein and has a notably greater phosphate requirement for activation
L135I
-, E7EAU9
the mutation releases the enzyme from ADP and GDP inhibition and significantly increases its sensitivity to inorganic phosphate activation
N120S
-, E7EAU9
the mutation releases the enzyme from ADP and GDP inhibition and significantly increases its sensitivity to inorganic phosphate activation
D58H
Bacillus amyloliquefaciens IAM 1523
-
the mutant exhibits nearly identical sensitivity to ADP and GDP as the wild-type protein and has a notably greater phosphate requirement for activation
-
L135I
Bacillus amyloliquefaciens IAM 1523
-
the mutation releases the enzyme from ADP and GDP inhibition and significantly increases its sensitivity to inorganic phosphate activation
-
N120S
Bacillus amyloliquefaciens IAM 1523
-
the mutation releases the enzyme from ADP and GDP inhibition and significantly increases its sensitivity to inorganic phosphate activation
-
E206A
-
KM-value for ATP is 2.5fold higher than wild-type value
K197A
-
maximal velocity is reduced more than 30000fold compared to wild-type enzyme. The KM-values for ATP and ribose 5-phosphate are unchanged
M208A
-
KM-value for ATP is 1.2fold higher than wild-type value
N203A
-
KM-value for ATP is 5.6fold higher than wild-type value
P200A
-
KM-value for ATP is 1.5fold lower than wild-type value
P202A
-
KM-value for ATP is 1.5fold higher than wild-type value
R198A
-
KM-value for ATP is nearly identical to wild-type value
R199A
-
maximal velocity is reduced more than 24000fold compared to wild-type enzyme. The KM-values for ATP and ribose 5-phosphate are unchanged
R201A
-
KM-value for ATP is 2.9fold higher than wild-type value
V204A
-
KM-value for ATP is nearly identical to wild-type value
S132A
P60891
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
P60891
the mutants show altered ligand binding and regulation at the allosteric site compared to the wild-type enzyme, comparison of crystal structures, overview
A181D
-
the mutant shows reduced specific activity compared to the wild type enzyme
D224A
-
the mutant shows reduced specific activity compared to the wild type enzyme
E306K
-
the mutant shows reduced specific activity compared to the wild type enzyme
G209V
-
the mutant shows 45fold reduced specific activity compared to the wild type enzyme
G50D
-
the mutant shows reduced specific activity compared to the wild type enzyme
A181D
Salmonella enterica DM10373
-
the mutant shows reduced specific activity compared to the wild type enzyme
-
D224A
Salmonella enterica DM10373
-
the mutant shows reduced specific activity compared to the wild type enzyme
-
E306K
Salmonella enterica DM10373
-
the mutant shows reduced specific activity compared to the wild type enzyme
-
G209V
Salmonella enterica DM10373
-
the mutant shows 45fold reduced specific activity compared to the wild type enzyme
-
G50D
Salmonella enterica DM10373
-
the mutant shows reduced specific activity compared to the wild type enzyme
-
V207A
-
KM-value for ATP is 1.2fold lower than wild-type value
additional information
-
construction of engineered AGR371C and AGL080C mutant strains, which show increased riboflavin synthesis compared to the wild-type strain
additional information
-
overexpression of wild-type and mutant enzymes via Agrobacterium tumefaciens-mediated gene transfer in Arabidopsis thaliana and Nicotiana tabacum seedlings leads to increased phosphoribosyl pyrophosphate synthetase, PRS, activity in both transgenic plants and to a substantial increase in biomass accumulation under different standardized growth conditions. Growth enhancement is accompanied by significant changes in the amount of sugars and other metabolites, phenotypes, overview. Seed composition is unchanged in plants with ectopic expression of heterologous PRS activity in the cytosol, metabolite analysis reveals a negative correlation of sucrose content with biomass accumulation. Recycling of nucleobases is increased in Arabidopsis thaliana seedlings with higher PRS activity
E43D
P60891
naturally occuring mutation causes the Rosenberg-Chutorian syndrome, the disease locus CMTX5 is situated on the chromosome band Xq21.32-q24
additional information
P60891
mutations in PRPS1 cause hereditary peripheral neuropathy with hearing loss and optic neuropathy, more
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
the enzyme is useful in industrial production of the vitamin riboflavin using the fungus Ashbya gossypii