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5-phospho-alpha-D-ribose 1-diphosphate + 4,6-dihydroxypyrazolo[3,4-d]pyrimidine
?
-
at 0.064% of the activity with xanthine
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + 5,7-dihydroxy-v-triazolo[4,5-d]pyrimidine
?
-
at 16.8% of the activity with xanthine
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + adenine
AMP + diphosphate
5-phospho-alpha-D-ribose 1-diphosphate + guanine
GMP + diphosphate
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
XMP + diphosphate
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
guanosine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
IMP + diphosphate
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
-
-
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
additional information
?
-
5-phospho-alpha-D-ribose 1-diphosphate + adenine
AMP + diphosphate
-
at 0.25% of the activity with xanthine
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + adenine
AMP + diphosphate
-
less than 1% of the activity with xanthine
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + guanine
GMP + diphosphate
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + guanine
GMP + diphosphate
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + guanine
GMP + diphosphate
-
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + guanine
GMP + diphosphate
-
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + guanine
GMP + diphosphate
-
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + guanine
GMP + diphosphate
-
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
-
at 0.19% of the activity with xanthine
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
-
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
-
-
-
-
r
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
-
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
-
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
-
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
-
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
in a sequential reaction mechanism XPRTase binds first 5-phospho-alpha-D-ribose 1-diphosphate, stabilizing its active dimeric form, and subsequently xanthine
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
-
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
-
the enzyme is involved in purine nucleotide synthesis via phosphorylation of purines acquisited from the host, since Leishmania donovani is not able to perform de novo biosynthesis of purine nucleotides
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
-
the enzymes catalyzing the transribosylation from 5-phospho-alpha-D-ribose 1-diphosphate to guanine, hypoxanthine and xanthine are inseparable
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
-
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
-
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
XMP + diphosphate
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
XMP + diphosphate
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
XMP + diphosphate
-
-
-
-
?
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
guanine + 5-phospho-alpha-D-ribose 1-diphosphate
GMP + diphosphate
-
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
low activity, reaction of EC 2.4.2.8
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
reaction of EC 2.4.2.8
-
-
?
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
reaction of EC 2.4.2.8
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
reaction of EC 2.4.2.8
-
-
r
hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate
IMP + diphosphate
reaction of EC 2.4.2.8
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
?
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
r
xanthine + 5-phospho-alpha-D-ribose 1-diphosphate
XMP + diphosphate
-
-
-
r
additional information
?
-
Escherichia coli xanthine-guanine phosphoribosyltransferase (EcXGPRT) prefers guanine and xanthine
-
-
-
additional information
?
-
-
either hypoxanthine-guanine phosphoribosyltransferase or xanthine phosphoribosyltransferase is absolutely essential for purine acquisition, parasite viability, and parasite infectivity of mouse macrophages
-
-
?
additional information
?
-
-
xanthine phosphoribosyltransferase is involved in acquirement of purine nutrients of Leimania from the host, the enzyme is not essential for purine salvage or viability
-
-
?
additional information
?
-
substrate specificity, overview. TtXPRT is confirmed as a xanthine phosphoribosyltransferase. Furthermore, TtXPRT can also slightly recognize hypoxanthine and guanine as substrates, but the activity is low. No activity with adenine
-
-
-
additional information
?
-
substrate specificity, overview. TtXPRT is confirmed as a xanthine phosphoribosyltransferase. Furthermore, TtXPRT can also slightly recognize hypoxanthine and guanine as substrates, but the activity is low. No activity with adenine
-
-
-
additional information
?
-
substrate specificity, overview. TtXPRT is confirmed as a xanthine phosphoribosyltransferase. Furthermore, TtXPRT can also slightly recognize hypoxanthine and guanine as substrates, but the activity is low. No activity with adenine
-
-
-
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(2-[(2,3-dihydroxypropyl)[2-(6-oxo-1,6-dihydro-9H-purin-9-yl)ethyl]amino]ethyl)phosphonic acid
-
(2-[3-(8-bromoguanin-9-yl)-2-(2-(bishydroxyphosphoryl)-ethoxy)propoxy]ethyl)phosphonic acid
-
(2-[[2-(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)ethyl][2-(2-phosphonoethoxy)ethyl]amino]ethyl)phosphonic acid
-
([2-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-3-(2-phosphonoethoxy)propoxy]methyl)phosphonic acid
-
([2-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-3-(2-phosphonoethoxy)propoxy]methyl)phosphonic acid
-
([3-(7-deazaguanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
sodium salt
([3-(7-deazahypoxanthine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
sodium salt
([3-(8-bromoguanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
sodium salt
([3-(8-bromohypoxanthine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
sodium salt
([3-(guanine-9-yl)-2-((2-phosphonoethoxy)-methyl)propoxy]methyl)phosphonic acid
sodium salt
([3-(hypoxanthine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methyl)phosphonic acid
sodium salt
2,4-dihydroxy-5,6-tetramethylenepyrimidine
-
-
2,4-Dihydroxypteridine
-
-
2,4-dihydroxypyrido[2,3-d]pyrimidine
-
-
2,4-dihydroxypyrido[3,2-d]pyrimidine
-
-
2,4-dihydroxypyrido[3,4-d]pyrimidine
-
-
2,4-dihydroxypyrrolo[2,3-d]pyrimidine
-
-
2,6-dioxo-1,3,7-trimethylpurine
-
-
2,6-dioxo-1,3,9-trimethylpurine
-
-
2,6-dioxo-3-isobutyl-1-methylpurine
-
-
2,6-dioxo-7-(beta-hydroxypropyl)-1,3-dimethylpurine
-
-
2-amino-1-methylhypoxanthine
-
-
2-amino-1-methylpurine
-
-
2-amino-6-chloropurine
-
-
2-amino-7-deazahypoxanthine
-
-
2-amino-7-methylhypoxanthine
-
-
2-amino-9-deazahypoxanthine
-
-
2-amino-9-methylhypoxanthine
-
-
2-aminopurine-6-thione
-
-
2-aza-3-deazahypoxanthine
-
-
2-aza-6-amino-3-deazapurine
-
-
2-aza-6-thio-3-deazapurine
-
-
2-hydroxy-6-methylthiopurine
-
-
2-methylthio-6-hydroxypurine
-
-
2-oxo 7-methylhypoxanthine
-
-
2-oxo-1-methylhypoxanthine
-
-
2-oxo-3-methylhypoxanthine
-
-
2-oxohypoxanthine-N3-oxide
-
-
4,6-dihydroxypyrazolo[3,4-d]-pyrimidine
-
-
4-aminoimidazole-5-carboxamide
-
-
4-hydroxypyrazolo[3,4-d]pyrimidine
-
-
4-mercapto-6-hydroxypyrazolo[3,4-d]pyrimidine
-
-
4-mercaptopyrazolo[3,4-d]pyrimidine
-
-
5(4)-amino-4-imidazolecarboxamide
-
-
5,7-dihydroxy(1,2,5)thiadiazolo[3,4-d]pyrimidine
-
-
5,7-dihydroxy-v-triazolo[4,5-d]pyrimidine
-
-
5,7-dihydroxypyrazolo[4,3-d]pyrimidine
-
-
5-phospho-alpha-D-ribose 1-diphosphate
-
-
6-amino-1-methylpurine
-
-
6-amino-2,8-diaza-3-deazapurine
-
-
6-amino-2-chloropurine
-
-
6-amino-2-methylpurine
-
-
6-amino-7-deazapurine
-
-
6-amino-8-bromopurine
-
-
6-Hydroxymethylpterin
-
-
8-aza-1,3-dideazapurine
-
-
8-aza-1-nitro-1,3-dideazapurine
-
-
8-aza-2,6-diaminopurine
-
-
8-aza-2-aminohypoxanthine
-
-
8-aza-7-deaza-6-aminopurine
-
-
8-aza-7-deaza-6-thiopurine
-
-
8-aza-7-deazahypoxanthine
-
-
8-bromo-2-aminohypoxanthine
-
-
9-[(N-phosphonoethyl-N-phosphonobutyl)-2-aminoethyl]hypoxanthine
-
9-[(N-phosphonoethyl-N-phosphonoethoxyethyl)-2-aminoethyl]-hypoxanthine
-
9-[(N-phosphonoethyl-N-phosphonomethoxyethyl)-2-aminoethyl]hypoxanthine
-
9-[(N-phosphonoethyl-N-phosphonomethyl)-2-aminoethyl]-hypoxanthine
-
ATP
-
1 mM, 11% inhibition
CDP
-
1 mM, 10% inhibition
CTP
-
1 mM, 27% inhibition
diethyl (2S,15S)-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-8-[(4-oxo-3,4-dihydro-7H-pyrrolo[2,3-d]pyrimidin-7-yl)methyl]-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-8-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-2,15-dibenzyl-8-[(8-bromo-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-4,13-bis[[(2S)-1-ethoxy-1-oxo-4-phenylbutan-2-yl]amino]-4,13-dioxo-8-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-2,15-bis(2-phenylethyl)-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
-
diethyl (2S,15S)-8-[(2-amino-4-oxo-3,4-dihydro-7H-pyrrolo[2,3-d]pyrimidin-7-yl)methyl]-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-8-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-8-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-7,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
diethyl (2S,15S)-8-[(2-amino-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-4,13-bis[[(2S)-1-ethoxy-1-oxo-4-phenylbutan-2-yl]amino]-4,13-dioxo-2,15-bis(2-phenylethyl)-6,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
-
diethyl (2S,15S)-8-[(2-amino-8-bromo-6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]-2,15-dibenzyl-4,13-bis[[(2S)-1-ethoxy-1-oxo-3-phenylpropan-2-yl]amino]-4,13-dioxo-7,10-dioxa-3,14-diaza-4lambda5,13lambda5-diphosphahexadecane-1,16-dioate
prodrug
GDP
-
1 mM, 93 inhibition
GTP
-
1 mM, 91% inhibition
pGpp
competitive inhibitor
ppGpp
competitive inhibitor
pppGpp
competitive inhibitor
Pyrophosphate
noncompetitive
TDP
-
1 mM, 18% inhibition
TTP
-
1 mM, 13% inhibition
UDP
-
1 mM, 15% inhibition
UTP
-
1 mM, 17% inhibition
XDP
-
1 mM, 89% inhibition
XTP
-
1 mM, 92% inhibition
[3-(guanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methylphosphonic acid
-
[[2-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]propane-1,3-diyl]bis(oxymethylene)]bis(phosphonic acid)
[[[(4-oxo-4,5-dihydro-3H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]azanediyl]di(propane-3,1-diyl)]bis(phosphonic acid)
-
adenine
-
-
GMP
competitive against 5-phospho-alpha-D-ribose 1-diphosphate
GMP
-
1 mM, 89% inhibition
GMP
-
inhibition of the xanthine phosphoribosylation
guanine
-
-
hypoxanthine
-
-
Uracil
-
-
xanthine
-
-
XMP
competitive against 5-phospho-alpha-D-ribose 1-diphosphate
XMP
-
1 mM, 92% inhibition
[[2-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]propane-1,3-diyl]bis(oxymethylene)]bis(phosphonic acid)
-
[[2-[(6-oxo-1,6-dihydro-9H-purin-9-yl)methyl]propane-1,3-diyl]bis(oxymethylene)]bis(phosphonic acid)
-
additional information
EcXGPRT inhibitor design, synthesis and optimization. Several acyclic nucleoside phosphonates (ANPs) have previously been identified as inhibitors of EcXGPRT and EcHPRT and the most potent of these have Ki values as low as 10 nM for EcXGPRT and 0.8 mM for EcHPRT
-
additional information
synthesis and evaluation of asymmetric acyclic nucleoside bisphosphonates as inhibitors of Plasmodium falciparum hypoxanthine-guanine-(xanthine) phosphoribosyltransferase. Low Ki values are achieved by inserting an extra carbon atom in the linker connecting the N9 atom of guanine to one of the phosphonate groups
-
additional information
-
synthesis and evaluation of asymmetric acyclic nucleoside bisphosphonates as inhibitors of Plasmodium falciparum hypoxanthine-guanine-(xanthine) phosphoribosyltransferase. Low Ki values are achieved by inserting an extra carbon atom in the linker connecting the N9 atom of guanine to one of the phosphonate groups
-
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Herpes Simplex
Both early and late control sequences of SV40 and polyoma promote transcription of Escherichia coli gpt gene in transfected cells.
Infections
A conditional mutant deficient in hypoxanthine-guanine phosphoribosyltransferase and xanthine phosphoribosyltransferase validates the purine salvage pathway of Leishmania donovani.
Infections
Human T cell recognition of the blood stage antigen Plasmodium hypoxanthine guanine xanthine phosphoribosyl transferase (HGXPRT) in acute malaria.
Malaria
Acyclic immucillin phosphonates: second-generation inhibitors of Plasmodium falciparum hypoxanthine-guanine-xanthine phosphoribosyltransferase.
Malaria
Evaluating Iso-Mukaadial Acetate and Ursolic Acid Acetate as Plasmodium falciparum Hypoxanthine-Guanine-Xanthine Phosphoribosyltransferase Inhibitors.
Malaria
Evidence for multiple active states of Plasmodium falciparum hypoxanthine-guanine-xanthine phosphoribosyltransferase.
Malaria
Human T cell recognition of the blood stage antigen Plasmodium hypoxanthine guanine xanthine phosphoribosyl transferase (HGXPRT) in acute malaria.
Malaria
Inhibition of hypoxanthine-guanine phosphoribosyltransferase by acyclic nucleoside phosphonates: a new class of antimalarial therapeutics.
Malaria
The purine salvage enzyme hypoxanthine guanine xanthine phosphoribosyl transferase is a major target antigen for cell-mediated immunity to malaria.
Malaria
Transition-state analogs as inhibitors of human and malarial hypoxanthine-guanine phosphoribosyltransferases.
Neoplasms
Adjuvant Chemotherapy with or without Concurrent Radiotherapy for Patients with Stage IB Gastric Cancer: a Subgroup Analysis of the Adjuvant Chemoradiotherapy in Stomach Tumors (ARTIST) Phase III Trial.
Neuroblastoma
Purification and characterization of guanine phosphoribosyltransferase from Giardia lamblia.
Starvation
Genetic diversity and population structure of food-borne Staphylococcus carnosus strains.
Tuberculosis
Inhibition of the Escherichia coli 6-Oxopurine Phosphoribosyltransferases by Nucleoside Phosphonates: Potential for New Antibacterial Agents.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.019
5,7-dihydroxy-v-triazolo[4,5-d]pyrimidine
-
-
0.0034 - 3.668
5-phospho-alpha-D-ribose 1-diphosphate
0.092 - 0.533
9-(5-phospho-beta-D-ribosyl)xanthine
0.0059 - 0.133
diphosphate
0.0012 - 1.25
hypoxanthine
0.0034
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E198D/E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
0.0073
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E198D/E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
0.0162
5-phospho-alpha-D-ribose 1-diphosphate
-
wild-type, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
0.0181
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
0.023
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E215Q, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
0.0244
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
0.0251
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E198D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
0.0288
5-phospho-alpha-D-ribose 1-diphosphate
-
wild-type, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
0.03
5-phospho-alpha-D-ribose 1-diphosphate
cosubstrate: xanthine
0.0382
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E198D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
0.045
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E215Q, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
0.053
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.053
5-phospho-alpha-D-ribose 1-diphosphate
-
IMP-activated wild type enzyme, at pH 7.4, temperature not specified in the publication
0.069
5-phospho-alpha-D-ribose 1-diphosphate
at pH 7.6 and 25°C
0.094
5-phospho-alpha-D-ribose 1-diphosphate
-
IMP-activated mutant enzyme W181Y, at pH 7.4, temperature not specified in the publication
0.139
5-phospho-alpha-D-ribose 1-diphosphate
-
0.233
5-phospho-alpha-D-ribose 1-diphosphate
-
IMP-activated mutant enzyme W181F, at pH 7.4, temperature not specified in the publication
0.251
5-phospho-alpha-D-ribose 1-diphosphate
-
IMP-activated mutant enzyme W181S, at pH 7.4, temperature not specified in the publication
1.084
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated wild type enzyme, at pH 7.4, temperature not specified in the publication
2.286
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated mutant enzyme W181S, at pH 7.4, temperature not specified in the publication
2.783
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated mutant enzyme W181Y, at pH 7.4, temperature not specified in the publication
3.668
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated mutant enzyme W181F, at pH 7.4, temperature not specified in the publication
0.092
9-(5-phospho-beta-D-ribosyl)xanthine
-
wild-type, in TM buffer
0.094
9-(5-phospho-beta-D-ribosyl)xanthine
-
mutant E215Q, in TM buffer
0.358
9-(5-phospho-beta-D-ribosyl)xanthine
-
mutant E198D, in TM buffer
0.396
9-(5-phospho-beta-D-ribosyl)xanthine
-
mutant E215D, in TM buffer
0.533
9-(5-phospho-beta-D-ribosyl)xanthine
-
mutant E198D/E215D, in TM buffer
0.0059
diphosphate
-
mutant E198D/E215D, in the presence of 1 mM 9-(5-phospho-beta-D-ribosyl)xanthine
0.028
diphosphate
-
mutant E215Q, in the presence of 1 mM 9-(5-phospho-beta-D-ribosyl)xanthine
0.039
diphosphate
-
wild-type, in the presence of 1 mM 9-(5-phospho-beta-D-ribosyl)xanthine
0.074
diphosphate
-
mutant E198D/E215D, in the presence of 8 mM IMP
0.115
diphosphate
-
mutant E215D, in the presence of 1 mM 9-(5-phospho-beta-D-ribosyl)xanthine
0.133
diphosphate
-
mutant E198D, in the presence of 1 mM 9-(5-phospho-beta-D-ribosyl)xanthine
0.0013
guanine
-
-
0.0049
guanine
-
mutant E198D/E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.025
guanine
-
mutant E215Q, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.1
guanine
-
mutant E198D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.1
guanine
-
mutant E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.0012
hypoxanthine
-
-
0.0021
hypoxanthine
-
mutant E198D/E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.091
hypoxanthine
pH and temperature not specified in the publication
0.129
hypoxanthine
-
mutant E215Q, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.458
hypoxanthine
-
wild-type, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.524
hypoxanthine
-
mutant E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.567
hypoxanthine
-
mutant E198D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.0078
IMP
-
mutant E198D/E215D, at 25°C, in TM buffer
0.008
IMP
-
mutant E198D, at 25°C, in TM buffer
0.008
IMP
-
mutant E215D, at 25°C, in TM buffer
0.008
IMP
-
mutant E215Q, at 25°C, in TM buffer
0.008
IMP
-
wild-type, at 25°C, in TM buffer
0.001
xanthine
-
-
0.0043
xanthine
pH and temperature not specified in the publication
0.0073
xanthine
-
wild-type, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.0078
xanthine
-
mutant E198D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.0199
xanthine
-
mutant E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.035
xanthine
-
mutant E215Q, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.0913
xanthine
-
mutant E198D/E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.1 - 112
5-phospho-alpha-D-ribose 1-diphosphate
0.00367 - 0.043
9-(5-phospho-beta-D-ribosyl)xanthine
0.0038 - 0.025
diphosphate
0.006167
IMP
-
mutant E198D/E215D, at 25°C, in TM buffer
0.1
5-phospho-alpha-D-ribose 1-diphosphate
-
IMP-activated mutant enzyme W181F, at pH 7.4, temperature not specified in the publication
0.1
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated mutant enzyme W181Y, at pH 7.4, temperature not specified in the publication
0.2
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated mutant enzyme W181F, at pH 7.4, temperature not specified in the publication
0.2
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated wild type enzyme, at pH 7.4, temperature not specified in the publication
0.32
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated mutant enzyme W181S, at pH 7.4, temperature not specified in the publication
0.5
5-phospho-alpha-D-ribose 1-diphosphate
-
IMP-activated mutant enzyme W181Y, at pH 7.4, temperature not specified in the publication
0.67
5-phospho-alpha-D-ribose 1-diphosphate
-
IMP-activated mutant enzyme W181S, at pH 7.4, temperature not specified in the publication
1.6
5-phospho-alpha-D-ribose 1-diphosphate
-
IMP-activated wild type enzyme, at pH 7.4, temperature not specified in the publication
2.1
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E215Q, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
2.6
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E215Q, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
3.6
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E198D/E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
3.9
5-phospho-alpha-D-ribose 1-diphosphate
-
wild-type, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
3.9
5-phospho-alpha-D-ribose 1-diphosphate
-
wild-type, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
6.7
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
8.4
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E198D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
12.3
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E198D/E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
15.1
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
20.7
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E198D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
112
5-phospho-alpha-D-ribose 1-diphosphate
-
0.00367
9-(5-phospho-beta-D-ribosyl)xanthine
-
mutant E215D, at 25°C, in TM buffer
0.0103
9-(5-phospho-beta-D-ribosyl)xanthine
-
mutant E198D, at 25°C, in TM buffer
0.0148
9-(5-phospho-beta-D-ribosyl)xanthine
-
mutant E198D/E215D, at 25°C, in TM buffer
0.028
9-(5-phospho-beta-D-ribosyl)xanthine
-
wild-type, at 25°C, in TM buffer
0.043
9-(5-phospho-beta-D-ribosyl)xanthine
-
mutant E215Q, at 25°C, in TM buffer
0.0038
diphosphate
-
mutant E215D, in the presence of 1 mM 9-(5-phospho-beta-D-ribosyl)xanthine
0.0045
diphosphate
-
mutant E198D/E215D, in the presence of 8 mM IMP
0.0093
diphosphate
-
mutant E198D, in the presence of 1 mM 9-(5-phospho-beta-D-ribosyl)xanthine
0.0118
diphosphate
-
mutant E198D/E215D, in the presence of 1 mM 9-(5-phospho-beta-D-ribosyl)xanthine
0.0228
diphosphate
-
wild-type, in the presence of 1 mM 9-(5-phospho-beta-D-ribosyl)xanthine
0.025
diphosphate
-
mutant E215Q, in the presence of 1 mM 9-(5-phospho-beta-D-ribosyl)xanthine
0.03
guanine
-
0.1
guanine
-
mutant E215Q, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
1.1
guanine
-
mutant E198D/E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
1.5
guanine
-
mutant E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
3.3
guanine
-
mutant E198D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.5
hypoxanthine
-
2.2
hypoxanthine
-
mutant E198D/E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
2.4
hypoxanthine
-
mutant E215Q, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
3.1
hypoxanthine
-
wild-type, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
7.1
hypoxanthine
-
mutant E198D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
8.7
hypoxanthine
-
mutant E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
2
xanthine
-
mutant E215Q, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
3.5
xanthine
-
wild-type, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
16.4
xanthine
-
mutant E198D/E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
17.5
xanthine
-
mutant E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
23.3
xanthine
-
mutant E198D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.36 - 30.1
5-phospho-alpha-D-ribose 1-diphosphate
0.0065
guanine
pH and temperature not specified in the publication
0.0012
xanthine
pH and temperature not specified in the publication
0.36
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated mutant enzyme W181Y, at pH 7.4, temperature not specified in the publication
0.4
5-phospho-alpha-D-ribose 1-diphosphate
-
IMP-activated mutant enzyme W181F, at pH 7.4, temperature not specified in the publication
0.54
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated mutant enzyme W181F, at pH 7.4, temperature not specified in the publication
1.39
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated mutant enzyme W181S, at pH 7.4, temperature not specified in the publication
1.84
5-phospho-alpha-D-ribose 1-diphosphate
-
unactivated wild type enzyme, at pH 7.4, temperature not specified in the publication
2.6
5-phospho-alpha-D-ribose 1-diphosphate
-
IMP-activated mutant enzyme W181S, at pH 7.4, temperature not specified in the publication
5.3
5-phospho-alpha-D-ribose 1-diphosphate
-
IMP-activated mutant enzyme W181Y, at pH 7.4, temperature not specified in the publication
30.1
5-phospho-alpha-D-ribose 1-diphosphate
-
IMP-activated wild type enzyme, at pH 7.4, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.024
2,4-Dihydroxypteridine
-
-
0.0041
2,4-dihydroxypyrido[3,2-d]pyrimidine
-
-
0.41
2,6-dichloropurine
-
-
1.5
2,6-dioxo 3-isobutyl-1-methylpurine
-
-
1
2,6-dioxo-1,3,7-trimethylpurine
-
-
5.3
2,6-dioxo-1,3,9-trimethylpurine
-
-
1.9
2,6-dioxo-7-(beta-hydroxypropyl)-1,3-dimethylpurine
-
-
0.42
2,6-dithiopurine
-
-
0.15
2,6-dithioxanthine
-
-
0.04
2-amino 1-methylhypoxanthine
-
-
0.29
2-amino 1-methylpurine
-
-
0.23
2-amino-6-chloropurine
-
-
0.026
2-amino-7-deazahypoxanthine
-
-
3.1
2-amino-7-methylhypoxanthine
-
-
0.014
2-amino-9-deazahypoxanthine
-
-
0.23
2-amino-9-methylhypoxanthine
-
-
0.012
2-aminohypoxanthine
-
-
0.002
2-aminopurine-6-thione
-
-
0.022
2-aza-3-deazahypoxanthine
-
-
0.231
2-aza-6-amino-3-deazapurine
-
-
0.03
2-aza-6-thio-3-deazapurine
-
-
0.17
2-hydroxy-6-methylthiopurine
-
-
1.4
2-oxo 1-methylhypoxanthine
-
-
1.9
2-oxo 7-methylhypoxanthine
-
-
0.246
2-oxo-6-thiopurine
-
-
0.014
2-oxohypoxanthine
-
-
1.3
2-oxohypoxanthine-N3-oxide
-
-
0.068
2-thiohypoxanthine
-
-
0.62
3-Methylxanthine
-
-
0.31
4,6-dihydroxypyrazolo[3,4-d]-pyrimidine
-
-
0.2
4-mercapto-6-hydroxypyrazolo[3,4-d]pyrimidine
-
-
0.379
4-oxopyrimidine
-
-
0.0079
5(4)-amino-4-imidazolecarboxamide
-
-
0.032
5,7-dihydroxy(1,2,5)thiadiazolo[3,4-d]pyrimidine
-
-
0.11
5,7-dihydroxy-v-triazolo[4,5-d]pyrimidine
-
-
0.0022
5,7-dihydroxypyrazolo[4,3-d]pyrimidine
-
-
0.657
5-fluorocytosine
-
-
0.021
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.31
6-amino 1-methylpurine
-
-
0.437
6-amino-2,8-diaza-3-deazapurine
-
-
2.2
6-amino-2-chloropurine
-
-
0.37
6-amino-2-methylpurine
-
-
0.053
6-amino-2-oxopurine
-
-
1.7
6-amino-7-deazapurine
-
-
0.75
6-amino-8-bromopurine
-
-
1.1
6-benzylaminopurine
-
-
3.4
6-Hydroxymethylpterin
-
-
0.97
6-Methylaminopurine
-
-
5.2
8-aza-1,3-dideazapurine
-
-
0.39
8-aza-1-nitro-1,3-dideazapurine
-
-
0.85
8-aza-2,6-diaminopurine
-
-
2.6
8-aza-2-aminohypoxanthine
-
-
2.5
8-aza-6-aminopurine
-
-
0.88
8-aza-7-deaza 6-thiopurine
-
-
0.081
8-aza-7-deaza-6-aminopurine
-
-
0.035
8-aza-7-deazahypoxanthine
-
-
0.54
8-bromo-2-aminohypoxanthine
-
-
0.39
8-mercaptoxanthine
-
-
4.1
8-oxohypoxanthine
-
-
0.42
8-thiohypoxanthine
-
-
0.0025
pppGpp
at pH 7.6 and 25°C
0.000006
[3-(guanine-9-yl)-2-((2-phosphonoethoxy)methyl)propoxy]methylphosphonic acid
pH 7.4, temperature not specified in the publication
0.033
GMP
Kis
0.067
GMP
-
mutant E198D/E215D
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
metabolism
in Escherichia coli, the purine salvage pathway has two 6-oxopurine phosphoribosyltransferases (PRTs), xanthine-guanine PRT (EcXGPRT, EC 2.4.2.22) and hypoxanthine PRT (EcHPRT, EC 2.4.2.8). Escherichia coli can utilize both purine salvage and de novo pathways for the production of the nucleoside monophosphates required for incorporation into DNA and RNA. Escherichia coli is highly unusual in that it is one of only a few organisms that possess two distinct salvage enzymes for 6-oxopurine nucleoside monophosphate production
evolution
conserved XPRT PRPP motif sequence comparisons
evolution
-
conserved XPRT PRPP motif sequence comparisons
-
evolution
-
conserved XPRT PRPP motif sequence comparisons
-
physiological function
-
Sphi609 cells expressing wild-type XPRT grow in minimal medium supplemented with xanthine but not in medium containing hypoxanthine or guanine. In contrast, Escherichia coli Sphi609 transformed with E198D or E215D exhibit vigorous growth with xanthine or hypoxanthine but notably less growth with guanine. Sphi609 transformants expressing E215Q or E198D/E215D proliferate robustly in xanthine, hypoxanthine, and guanine
physiological function
hypoxanthine-guanine-(xanthine) phosphoribosyltransferases, HG(X)PRTs, catalyze the formation of the 6-oxopurine nucleoside monophosphates from a nucleobase and from 5'-phospho-alpha-D-ribosyl-1-pyrophosphate
physiological function
purine phosphoribosyltransferases, purine PRTs, are essential enzymes in the purine salvage pathway of living organisms. They are involved in the formation of C-N glycosidic bonds in purine nucleosides-5'-monophosphate (NMPs) through the transfer of the 5-phosphoribosyl group from 5-phospho-alpha-D-ribosyl-1-diphosphate (PRPP) to purine nucleobases in the presence of Mg2+
physiological function
-
purine phosphoribosyltransferases, purine PRTs, are essential enzymes in the purine salvage pathway of living organisms. They are involved in the formation of C-N glycosidic bonds in purine nucleosides-5'-monophosphate (NMPs) through the transfer of the 5-phosphoribosyl group from 5-phospho-alpha-D-ribosyl-1-diphosphate (PRPP) to purine nucleobases in the presence of Mg2+
-
physiological function
-
purine phosphoribosyltransferases, purine PRTs, are essential enzymes in the purine salvage pathway of living organisms. They are involved in the formation of C-N glycosidic bonds in purine nucleosides-5'-monophosphate (NMPs) through the transfer of the 5-phosphoribosyl group from 5-phospho-alpha-D-ribosyl-1-diphosphate (PRPP) to purine nucleobases in the presence of Mg2+
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E198D
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increases the turnover rates of the xanthine phosphoribosyltransferase without altering purine nucleobase specificity, converts the xanthine phosphoribosyltransferase into a broad-specificity enzyme capable of utilizing guanine, hypoxanthine, and xanthine as substrates. Can accommodate GMP in the active site
E198D/E215D
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catalyzes robust guanine phosphoribosylation. Exhibits similar kinetic parameters in the presence of Mg2+ or Mn2+ as the wild-type. Substitution of Mg2+ with Mn2+ does not alter the hypoxanthine phosphoribosylation activity
E215D
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increases the turnover rates of the xanthine phosphoribosyltransferase without altering purine nucleobase specificity, converts the xanthine phosphoribosyltransferase into a broad-specificity enzyme capable of utilizing guanine, hypoxanthine, and xanthine as substrates. Can accommodate GMP in the active site
E215Q
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can accommodate GMP in the active site
W181F
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the mutant retains its ability to catalyse the phosphoribosylation of hypoxanthine, guanine and xanthine, albeit with significantly lower specific activities than the wild type enzyme. The mutant shows an increase in Km for 5-phospho-alpha-D-ribose 1-diphosphate by 3.4fold under unactivated condition and a decrease in catalytic efficiency by 76fold under activated condition as compared to that of the wild type enzyme
W181Y
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the mutant retains its ability to catalyse the phosphoribosylation of hypoxanthine, guanine and xanthine, albeit with significantly lower specific activities than the wild type enzyme. The mutant shows an increase in Km for 5-phospho-alpha-D-ribose 1-diphosphate by 2.6fold under unactivated condition and a decrease in catalytic efficiency by more than 5fold under activated condition as compared to that of the wild type enzyme
additional information
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deletion of the glycosomal targeting sequence, a C-terminal tripeptide, leads to mislocation of the enzyme in the cytosol, where the enzyme nevertheless is still active
W181S
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the mutant retains its ability to catalyse the phosphoribosylation of hypoxanthine, guanine and xanthine, albeit with significantly lower specific activities than the wild type enzyme. The mutant shows 10fold reduced xanthine phosphoribosylation activity compared to the wild type enzyme
W181S
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the mutant retains its ability to catalyze the phosphoribosylation of hypoxanthine, guanine and xanthine, albeit with significantly lower specific activities than the wild type enzyme. The mutant shows an increase in Km for 5-phospho-alpha-D-ribose 1-diphosphate by 2.1fold under unactivated condition and a decrease in catalytic efficiency by more than 11fold under activated condition as compared to that of the wild type enzyme
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Krenitsky, T.A.; Neil, S.M.; Miller, R.L.
Guanine and xanthine phosphoribosyltransfer activities of Lactobacillus casei and Escherichia coli. Their relationship to hypoxanthine and adenine phosphoribosyltransfer activities
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Escherichia coli, Lacticaseibacillus casei
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Xanthine phosphoribosyltransferase in Leishmania: divalent cation activation
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Leishmania braziliensis, Leishmania donovani, Leishmania mexicana, Leishmania tarentolae
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Purine phosphoribosyltransferases from Leishmania donovani
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Leishmania donovani
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Xanthine phosphoribosyltransferase from Streptococcus faecalis. Properties and specificity
Arch. Biochem. Biophys.
165
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Enterococcus faecalis
brenda
Vos, S.; de Jersey, J.; Martin, J.L.
Crystal structure of Escherichia coli xanthine phosphoribosyltransferase
Biochemistry
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Escherichia coli (P0A9M5), Escherichia coli
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Guetsova, M.L.; Crother, T.R.; Taylor, M.W.; Daignan-Fornier, B.
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Saccharomyces cerevisiae
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Structure-activity relationships for the binding of ligands to xanthine or guanine phosphoribosyltransferase from Toxoplasma gondii
Biochem. Pharmacol.
50
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Toxoplasma gondii
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Jardim, A.; Bergeson, S.E.; Shih, S.; Carter, N.; Lucas, R.W.; Merlin, G.; Myler, P.J.; Stuart, K.; Ullman, B.
Xanthine phosphoribosyltransferase from Leishmania donovani. Molecular cloning, biochemical characterization, and genetic analysis
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274
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Leishmania donovani
brenda
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Subcellular localization of adenine and xanthine phosphoribosyltransferases in Leishmania donovani
Mol. Biochem. Parasitol.
134
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2004
Leishmania donovani
brenda
Arent, S.; Kadziola, A.; Larsen, S.; Neuhard, J.; Jensen, K.F.
The extraordinary specificity of xanthine phosphoribosyltransferase from Bacillus subtilis elucidated by reaction kinetics, ligand binding, and crystallography
Biochemistry
45
6615-6627
2006
Bacillus subtilis (P42085), Bacillus subtilis
brenda
Boitz, J.M.; Ullman, B.
A conditional mutant deficient in hypoxanthine-guanine phosphoribosyltransferase and xanthine phosphoribosyltransferase validates the purine salvage pathway of Leishmania donovani
J. Biol. Chem.
281
16084-16089
2006
Leishmania donovani
brenda
Boitz, J.M.; Ullman, B.
Leishmania donovani singly deficient in HGPRT, APRT or XPRT are viable in vitro and within mammalian macrophages
Mol. Biochem. Parasitol.
148
24-30
2006
Leishmania donovani
brenda
Ullman, B.; Cyr, N.; Choi, K.; Jardim, A.
Acidic residues in the purine binding site govern the 6-oxopurine specificity of the Leishmania donovani xanthine phosphoribosyltransferase
Int. J. Biochem. Cell Biol.
42
253-262
2010
Leishmania donovani
brenda
Del Arco, J.; Martinez, M.; Donday, M.; Clemente-Suarez, V.; Fernandez-Lucas, J.
Cloning, expression and biochemical characterization of xanthine and adenine phosphoribosyltransferases from Thermus thermophilus HB8
Biocatal. Biotransform.
36
216-223
2018
Thermus thermophilus (Q5SKV8), Thermus thermophilus DSM 579 (Q5SKV8), Thermus thermophilus ATCC 27634 (Q5SKV8)
-
brenda
Eng, W.; Hockova, D.; Spacek, P.; Baszczynski, O.; Janeba, Z.; Naesens, L.; Keough, D.; Guddat, L.
Crystal structures of acyclic nucleoside phosphonates in complex with Escherichia coli hypoxanthine phosphoribosyltransferase
ChemistrySelect
1
6267-6276
2016
Escherichia coli (P0A9M5)
-
brenda
Spacek, P.; Keough, D.T.; Chavchich, M.; Dracinsky, M.; Janeba, Z.; Naesens, L.; Edstein, M.D.; Guddat, L.W.; Hockova, D.
Synthesis and evaluation of asymmetric acyclic nucleoside bisphosphonates as inhibitors of Plasmodium falciparum and human hypoxanthine-guanine-(xanthine) phosphoribosyltransferase
J. Med. Chem.
60
7539-7554
2017
Plasmodium falciparum (Q8IJS1), Plasmodium falciparum
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Anderson, B.W.; Hao, A.; Satyshur, K.A.; Keck, J.L.; Wang, J.D.
Molecular mechanism of regulation of the purine salvage enzyme XPRT by the alarmones pppGpp, ppGpp, and pGpp
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432
4108-4126
2020
Bacillus subtilis (P42085), Bacillus subtilis, Bacillus subtilis 168 (P42085)
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Roy, S.; Karmakar, T.; Nagappa, L.K.; Prahlada Rao, V.S.; Balasubramanian, S.; Balaram, H.
Role of W181 in modulating kinetic properties of Plasmodium falciparum hypoxanthine guanine xanthine phosphoribosyltransferase
Proteins
84
1658-1669
2016
Plasmodium falciparum
brenda