Information on EC 2.7.6.1 - ribose-phosphate diphosphokinase

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

EC NUMBER
COMMENTARY hide
2.7.6.1
-
RECOMMENDED NAME
GeneOntology No.
ribose-phosphate diphosphokinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diphosphate transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
histidine metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
Pentose phosphate pathway
-
-
PRPP biosynthesis I
-
-
Purine metabolism
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:D-ribose-5-phosphate diphosphotransferase
dATP can also act as donor.
CAS REGISTRY NUMBER
COMMENTARY hide
9015-83-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Culex pipiens subsp. pallens
UniProt
Manually annotated by BRENDA team
chicken
-
-
Manually annotated by BRENDA team
rubber tree
-
-
Manually annotated by BRENDA team
mouse
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
lingcod
-
-
Manually annotated by BRENDA team
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-
-
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
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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)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
(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
(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
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
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
9-(2-phosphonylmethoxyethyl)adenine + 5-phospho-alpha-D-ribose 1-diphosphate
9-(2-phosphonylmethoxyethyl)adenine-diphosphate + D-ribose 5-phosphate
show the reaction diagram
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
ATP + D-ribose 5-phosphate
show the reaction diagram
ATP + 1,2,3-trihydroxy-4-cyclopentanemethanol-6-phosphate
?
show the reaction diagram
ATP + 1,4,5-trihydroxy-3-cyclopent-2-enemethanol-6-phosphate
?
show the reaction diagram
ATP + 6-deoxyhomoribose 6-phosphonate
AMP + 6-deoxyhomoribose 6-phosphonate 1-diphosphate
show the reaction diagram
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
ATP + D-ribose 5-phosphothionate
AMP + 5-phosphotionate-alpha-D-ribose 1-diphosphate
show the reaction diagram
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
D-ribose 5-phosphate + ATP
5-phospho-alpha-D-ribose 1-diphosphate + AMP
show the reaction diagram
biosynthesis of purines and pyrimidines
-
-
?
D-ribose 5-phosphate + ATP
phosphoribosyldiphosphate + AMP
show the reaction diagram
dATP + D-ribose 5-phosphate
dAMP + 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
ITP + D-ribose 5-phosphate
IMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Mg-ATP2- + D-ribose 5-phosphate
Mg-AMP2- + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
Mn-ATP2- + D-ribose 5-phosphate
Mn-AMP2- + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
ribose-5-phosphate + ATP
phosphoribosyldiphosphate + AMP
show the reaction diagram
first step in purine metabolic pathway
-
-
?
UTP + D-ribose 5-phosphate
UMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + D-ribose 5-phosphate
AMP + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
D-ribose 5-phosphate + ATP
5-phospho-alpha-D-ribose 1-diphosphate + AMP
show the reaction diagram
P60891
biosynthesis of purines and pyrimidines
-
-
?
D-ribose 5-phosphate + ATP
phosphoribosyldiphosphate + AMP
show the reaction diagram
ribose-5-phosphate + ATP
phosphoribosyldiphosphate + AMP
show the reaction diagram
P60891
first step in purine metabolic pathway
-
-
?
additional information
?
-
P60891
the phosphoribosyl pyrophosphate synthetase enzyme critical for nucleotide biosynthesis
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-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
the AMP moiety of ATP binds at the ATP-binding site, structure, overview. A Cd2+ ion binds at the active site and in a position to interact with the beta- and gamma -phosphates of ATP
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
activity is 5-10% of the activity with Mg2+
Ni2+
can serve as substitutes for Mg2+ with relatively lower activity
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2,3-trihydroxy-4-cyclopentanemethanol-6-phosphate
1,4,5-trihydroxy-3-cyclopent-2-enemethanol-6-phosphate
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate
2,3-diphosphoglycerate
2-deoxy-D-ribose 5-phosphate
-
92% inhibition at 1 mM
5-phospho-alpha-D-ribose 1-diphosphate
9-(2-phosphonylmethoxyethoxy)adenine
9-(2-phosphonylmethoxyethyl)adenine
adenosine
adenosine 5'-(beta,gamma-imido)-triphosphate
-
inhibition at 1 mM
allopurinol ribonucleotides
-
23% inhibition at 1 mM
alpha,beta-methylene ATP
-
alpha,beta-methyleneATP
D-fructose 1,6-diphosphate
D-Fructose 1-phosphate
D-ribose 1-phosphate
-
13% inhibition at 1 mM
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
glyceraldehyde 3-phosphate
GSH
-
marked inhibition of enzyme in crude extract at 1 mM
guanosine
IMP
-
21% inhibition at 1 mM
L-histidine
L-tryptophan
Mn2+
-
complete inhibition above 0.4 mM
NAD+
-
100% inhibition at 1 mM
NADH
-
72% inhibition at 1 mM
NADPH
-
100% inhibition at 1 mM
nucleotides
phosphate
PRPP synthetase-associated proteins
SO42-
-
1 M, strong inhibition
TTP
-
47% inhibition at 1 mM
XDP
-
36% inhibition at 1 mM
XTP
-
22% inhibition at 1 mM
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-Aminoethylphosphonate
-
0.1 M, 13% of the activity with phosphate
arsenate
DTT
-
requirement
EDTA
-
prevents inhibition by traces of cations
phosphate
sulfate
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.29 - 3.571
(R)9-(2-phosphonylmethoxypropyl)adenine
1.14 - 1.923
(R)9-(3-fluoro-2-phosphonylmethoxypropyl)adenine
1.54 - 2.174
(S)9-(2-phosphonylmethoxypropyl)adenine
0.575 - 3.636
(S)9-(3-fluoro-2-phosphonylmethoxypropyl)adenine
0.317 - 0.377
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate
0.0289 - 0.0418
5-phospho-alpha-D-ribose 1-diphosphate
0.29
5-phospho-D-ribose diphosphate
0.308 - 0.789
9-(2-phosphonylmethoxyethoxy)adenine
0.656 - 1.47
9-(2-phosphonylmethoxyethyl)adenine
0.117 - 0.4
AMP
0.007 - 2.6
ATP
0.116
CTP
-
pH 7.6, 37C, isoenzyme 3
0.0082 - 2.8
D-ribose 5-phosphate
0.233
dATP
-
pH 7.6, 37C, isoenzyme 3
0.65
GTP
-
pH 7.6, 37C, isoenzyme 3
0.0002 - 1.5
Mg2+
0.014 - 2.9
MgATP2-
0.06 - 0.35
MnATP2-
0.008 - 40
phosphate
0.033
ribose 5-phosphate
0.137
UTP
-
pH 7.6, 37C, isoenzyme 3
additional information
additional information
-
increasing phosphate concentrations, increases Km values for ATP and D-ribose-5-phosphate
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.66
ATP
Mycobacterium tuberculosis
-
in 50 mM Tris-HCl pH 8.0, at 25C
35.1 - 60.68
D-ribose 5-phosphate
34.6 - 44.3
Mg-ATP2-
45.1 - 46.3
Mn-ATP2-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
26
ATP
Mycobacterium tuberculosis
-
in 50 mM Tris-HCl pH 8.0, at 25C
4
59 - 7430
D-ribose 5-phosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.41 - 0.55
2',3'-dideoxy-2',3'-didehydro-adenosine-5'-monophosphate
0.03 - 2.2
5-phospho-alpha-D-ribose 1-diphosphate
1.4
9-(2-phosphonylmethoxyethoxy)adenine
-
pH 8.0, 37C
0.37 - 1.9
9-(2-phosphonylmethoxyethyl)adenine
0.01 - 1.22
ADP
0.85
alpha,beta-methylene ATP
pH and temperature not specified in the publication
0.03
alpha,beta-methyleneATP
-
pH and temperature conditions not mentioned
0.01 - 5.6
AMP
0.167 - 1.089
ATP
0.032 - 0.11
Ca2+
0.211 - 1.18
D-ribose 5-phosphate
10
DL-1,4-Anhydroribitol 5-phosphate
-
pH and temperature conditions not mentioned
0.02
Mn2+
-
pH 7.5, 37C
0.15 - 0.75
TDP
additional information
additional information
-
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.86 - 2.5
9-(2-phosphonylmethoxyethoxy)adenine
1.9 - 2.1
9-(2-phosphonylmethoxyethyl)adenine
0.07 - 0.84
ADP
0.05
Ca2+
Salmonella enterica subsp. enterica serovar Typhimurium
-
IC50 of 0.05 mM
0.4 - 5
GDP
28 - 100
phosphate
3
UMP
Mycobacterium tuberculosis
-
in 50 mM Tris-HCl pH 8.0, at 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2 - 7.4
-
erythrocyte enzyme
8.1 - 8.6
-
for either the Mg2+ or the Mn2+ supported reaction
8.8
-
isoenzyme PRSI
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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 - 9.5
-
pH 6.5: about 25% of maximal activity, pH 9.5: about 80% of maximal activity
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
7 - 9.5
10
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 RANGE
ORGANISM
UNIPROT
COMMENTARY