Information on EC 2.4.2.22 - xanthine phosphoribosyltransferase

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

EC NUMBER
COMMENTARY
2.4.2.22
-
RECOMMENDED NAME
GeneOntology No.
xanthine phosphoribosyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
XMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + xanthine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
xanthine and xanthosine salvage
-
-
purine metabolism
-
-
Purine metabolism
-
-
Metabolic pathways
-
-
Biosynthesis of secondary metabolites
-
-
SYSTEMATIC NAME
IUBMB Comments
XMP:diphosphate 5-phospho-alpha-D-ribosyltransferase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5-phospho-alpha-D-ribose-1-diphosphate:xanthine phospho-D-ribosyltransferase
-
-
-
-
phosphoribosyltransferase, xanthine
-
-
-
-
Xan phosphoribosyltransferase
-
-
-
-
xanthine PRT
-
-
xanthosine 5'-phosphate pyrophosphorylase
-
-
-
-
xanthylate pyrophosphorylase
-
-
-
-
xanthylic pyrophosphorylase
-
-
-
-
XGPRT
-
-
-
-
XMP pyrophosphorylase
-
-
-
-
XPRT
-
-
-
-
XPRTase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9023-10-3
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-phospho-alpha-D-ribose 1-diphosphate + 4,6-dihydroxypyrazolo[3,4-d]pyrimidine
?
show the reaction diagram
-
at 0.064% of the activity with xanthine
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + 5,7-dihydroxy-v-triazolo[4,5-d]pyrimidine
?
show the reaction diagram
-
at 16.8% of the activity with xanthine
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + adenine
AMP + diphosphate
show the reaction diagram
-
at 0.25% of the activity with xanthine
-
?
5-phospho-alpha-D-ribose 1-diphosphate + adenine
AMP + diphosphate
show the reaction diagram
-
less than 1% of the activity with xanthine
-
?
5-phospho-alpha-D-ribose 1-diphosphate + guanine
GMP + diphosphate
show the reaction diagram
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + guanine
GMP + diphosphate
show the reaction diagram
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + guanine
GMP + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + guanine
GMP + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + guanine
GMP + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + guanine
GMP + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + guanine
GMP + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
show the reaction diagram
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
show the reaction diagram
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
show the reaction diagram
-
-
-
r
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
show the reaction diagram
-
at 0.19% of the activity with xanthine
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
show the reaction diagram
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
show the reaction diagram
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
in a sequential reaction mechanism XPRTase binds first 5-phospho-alpha-D-ribose 1-diphosphate, stabilizing its active dimeric form, and subsequently xanthine
-
?
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
show the reaction diagram
-
-
-
?
IMP + diphosphate
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
show the reaction diagram
-
-
-
r
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
9-(5-phospho-beta-D-ribosyl)xanthine + diphosphate
show the reaction diagram
-
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
-
?
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
efficiency is equal to Mn2+
Co2+
-
less efficient in activation than Mn2+
Co2+
-
efficiency is equal to Mn2+
Co2+
-
less efficient in activation than Mn2+
Mg2+
magnesium and sulfate can bind together in the active site, in the absence of other products or substrates. The magnesium interacts with a highly conserved aspartate residue
Mg2+
-
maximal catalytic activity with 0.06 mM
Mn2+
-
maximal catalytic activity with 0.06 mM. Substitution of Mn2+ for Mg2+ results in ca. 2fold increase in the XPRT turnover rate without altering the xanthine Km value. Replacement of Mg2+ with Mn2+ increases the 5-phospho-alpha-D-ribose 1-diphosphate Km value ca. 2fold. XPRT-catalyzed hypoxanthine phosphoribosylation reveals that substitution of Mg2+ with Mn2+ results in a ca. 4fold increase in the hypoxanthine kcat value and ca. 3fold decrease in the hypoxanthine Km value
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-Methylxanthine
-
-
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-Diaminopurine
-
-
2,6-dichloropurine
-
-
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
-
-
2,6-dithiopurine
-
-
2,6-dithioxanthine
-
-
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-aminohypoxanthine
-
-
2-Aminopurine
-
-
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-Hydroxypurine
-
-
2-mercaptopurine
-
-
2-methylhypoxanthine
-
-
2-methylthio-6-hydroxypurine
-
-
-
2-oxo 7-methylhypoxanthine
-
-
2-oxo-1-methylhypoxanthine
-
-
2-oxo-3-methylhypoxanthine
-
-
2-oxo-6-thiopurine
-
-
2-oxohypoxanthine
-
-
2-oxohypoxanthine-N3-oxide
-
-
2-oxopurine
-
-
2-thiohypoxanthine
-
-
2-Thioxanthine
-
-
3-Methylxanthine
-
-
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
-
-
4-oxopyrimidine
-
-
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-acetamidouracil
-
-
5-Aminouracil
-
-
5-anilinouracil
-
-
5-fluorocytosine
-
-
5-formamidouracil
-
-
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-2-oxopurine
-
-
6-amino-7-deazapurine
-
-
6-amino-8-bromopurine
-
-
6-benzylaminopurine
-
-
6-Chloropurine
-
-
6-Hydroxymethylpterin
-
-
6-Mercaptopurine
-
-
6-methoxypurine
-
-
6-Methylaminopurine
-
-
6-Thiopurine
-
-
6-Thioxanthine
-
-
7-methylxanthine
-
-
8-aza-1,3-dideazapurine
-
-
8-aza-1-nitro-1,3-dideazapurine
-
-
8-aza-2,6-diaminopurine
-
-
8-aza-2-aminohypoxanthine
-
-
8-aza-6-aminopurine
-
-
8-aza-7-deaza-6-aminopurine
-
-
8-aza-7-deaza-6-thiopurine
-
-
8-aza-7-deazahypoxanthine
-
-
8-Azahypoxanthine
-
-
8-bromo-2-aminohypoxanthine
-
-
8-mercaptoxanthine
-
-
8-methylxanthine
-
-
8-oxohypoxanthine
-
-
8-thiohypoxanthine
-
-
9-methylxanthine
-
-
ATP
-
1 mM, 11% inhibition
Benzonitrile
-
-
CDP
-
1 mM, 10% inhibition
CTP
-
1 mM, 27% inhibition
cytosine
-
-
GDP
-
1 mM, 93 inhibition
GMP
-
1 mM, 89% inhibition
GMP
competitive against 5-phospho-alpha-D-ribose 1-diphosphate
GMP
-
inhibition of the xanthine phosphoribosylation
GTP
-
1 mM, 91% inhibition
hypoxanthine
-
-
hypoxanthine
-
-
isocytosine
-
-
isoguanine
-
-
Pyrophosphate
noncompetitive
TDP
-
1 mM, 18% inhibition
TTP
-
1 mM, 13% inhibition
UDP
-
1 mM, 15% inhibition
UTP
-
1 mM, 17% inhibition
xanthine
-
-
XDP
-
1 mM, 89% inhibition
XMP
-
1 mM, 92% inhibition
XMP
competitive against 5-phospho-alpha-D-ribose 1-diphosphate
XTP
-
1 mM, 92% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.019
5,7-dihydroxy-v-triazolo[4,5-d]pyrimidine
-
-
0.0034
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E198D/E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
0.0073
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E198D/E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
0.0162
5-phospho-alpha-D-ribose 1-diphosphate
-
wild-type, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
0.0181
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
0.023
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E215Q, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
0.0244
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
0.0251
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E198D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
0.0288
5-phospho-alpha-D-ribose 1-diphosphate
-
wild-type, at 25C, 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 25C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
0.045
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E215Q, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
0.053
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.139
5-phospho-alpha-D-ribose 1-diphosphate
-
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
0.0029
adenine
-
-
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
-
-
0.0043
Guanine
-
0.0049
Guanine
-
mutant E198D/E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.025
Guanine
-
mutant E215Q, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.1
Guanine
-
mutant E198D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate; mutant E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.281
Guanine
-
0.0012
hypoxanthine
-
-
0.0021
hypoxanthine
-
mutant E198D/E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.0908
hypoxanthine
-
0.129
hypoxanthine
-
mutant E215Q, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.448
hypoxanthine
-
-
0.458
hypoxanthine
-
wild-type, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.524
hypoxanthine
-
mutant E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.567
hypoxanthine
-
mutant E198D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
1.25
hypoxanthine
-
0.0078
IMP
-
mutant E198D/E215D, at 25C, in TM buffer
0.008
IMP
-
mutant E198D, at 25C, in TM buffer; mutant E215D, at 25C, in TM buffer; mutant E215Q, at 25C, in TM buffer; wild-type, at 25C, in TM buffer
0.001
xanthine
-
-
0.0022
xanthine
-
0.003
xanthine
-
-
0.0071
xanthine
-
-
0.0073
xanthine
-
wild-type, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.0078
xanthine
-
mutant E198D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.0199
xanthine
-
mutant E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.02
xanthine
-
-
0.0305
xanthine
-
0.035
xanthine
-
mutant E215Q, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
0.0913
xanthine
-
mutant E198D/E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.1
5-phospho-alpha-D-ribose 1-diphosphate
Leishmania donovani
-
mutant E215Q, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
2.6
5-phospho-alpha-D-ribose 1-diphosphate
Leishmania donovani
-
mutant E215Q, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
3.6
5-phospho-alpha-D-ribose 1-diphosphate
Leishmania donovani
-
mutant E198D/E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
3.9
5-phospho-alpha-D-ribose 1-diphosphate
Leishmania donovani
-
wild-type, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine; wild-type, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
6.7
5-phospho-alpha-D-ribose 1-diphosphate
Leishmania donovani
-
mutant E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
8.4
5-phospho-alpha-D-ribose 1-diphosphate
Leishmania donovani
-
mutant E198D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
12.3
5-phospho-alpha-D-ribose 1-diphosphate
Leishmania donovani
-
mutant E198D/E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
15.1
5-phospho-alpha-D-ribose 1-diphosphate
Leishmania donovani
-
mutant E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
20.7
5-phospho-alpha-D-ribose 1-diphosphate
Leishmania donovani
-
mutant E198D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
112
5-phospho-alpha-D-ribose 1-diphosphate
Escherichia coli
P0A9M5
-
0.00367
9-(5-phospho-beta-D-ribosyl)xanthine
Leishmania donovani
-
mutant E215D, at 25C, in TM buffer
0.0103
9-(5-phospho-beta-D-ribosyl)xanthine
Leishmania donovani
-
mutant E198D, at 25C, in TM buffer
0.0148
9-(5-phospho-beta-D-ribosyl)xanthine
Leishmania donovani
-
mutant E198D/E215D, at 25C, in TM buffer
0.028
9-(5-phospho-beta-D-ribosyl)xanthine
Leishmania donovani
-
wild-type, at 25C, in TM buffer
0.043
9-(5-phospho-beta-D-ribosyl)xanthine
Leishmania donovani
-
mutant E215Q, at 25C, in TM buffer
0.0038
diphosphate
Leishmania donovani
-
mutant E215D, in the presence of 1 mM 9-(5-phospho-beta-D-ribosyl)xanthine
0.0045
diphosphate
Leishmania donovani
-
mutant E198D/E215D, in the presence of 8 mM IMP
0.0093
diphosphate
Leishmania donovani
-
mutant E198D, in the presence of 1 mM 9-(5-phospho-beta-D-ribosyl)xanthine
0.0118
diphosphate
Leishmania donovani
-
mutant E198D/E215D, in the presence of 1 mM 9-(5-phospho-beta-D-ribosyl)xanthine
0.0228
diphosphate
Leishmania donovani
-
wild-type, in the presence of 1 mM 9-(5-phospho-beta-D-ribosyl)xanthine
0.025
diphosphate
Leishmania donovani
-
mutant E215Q, in the presence of 1 mM 9-(5-phospho-beta-D-ribosyl)xanthine
0.03
Guanine
Bacillus subtilis
P42085
-
0.1
Guanine
Leishmania donovani
-
mutant E215Q, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
1.1
Guanine
Leishmania donovani
-
mutant E198D/E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
1.5
Guanine
Leishmania donovani
-
mutant E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
3.3
Guanine
Leishmania donovani
-
mutant E198D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
112
Guanine
Escherichia coli
P0A9M5
-
0.5
hypoxanthine
Bacillus subtilis
P42085
-
2.2
hypoxanthine
Leishmania donovani
-
mutant E198D/E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
2.4
hypoxanthine
Leishmania donovani
-
mutant E215Q, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
2.6
hypoxanthine
Leishmania donovani
-
-
3.1
hypoxanthine
Leishmania donovani
-
wild-type, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
7.1
hypoxanthine
Leishmania donovani
-
mutant E198D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
8.7
hypoxanthine
Leishmania donovani
-
mutant E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
54.8
hypoxanthine
Escherichia coli
P0A9M5
-
0.006167
IMP
Leishmania donovani
-
mutant E198D/E215D, at 25C, in TM buffer
2
xanthine
Leishmania donovani
-
mutant E215Q, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
3.5
xanthine
Leishmania donovani
-
-
3.5
xanthine
Leishmania donovani
-
wild-type, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
11
xanthine
Bacillus subtilis
P42085
-
16.4
xanthine
Leishmania donovani
-
mutant E198D/E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
17.5
xanthine
Leishmania donovani
-
mutant E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
23.3
xanthine
Leishmania donovani
-
mutant E198D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
150
xanthine
Escherichia coli
P0A9M5
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
-
0.067
2-Aminopurine
-
-
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
-
-
0.57
2-oxopurine
-
-
0.068
2-thiohypoxanthine
-
-
0.38
2-Thioxanthine
-
-
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
-
-
0.1
6-Chloropurine
-
-
3.4
6-Hydroxymethylpterin
-
-
0.38
6-methoxypurine
-
-
0.97
6-Methylaminopurine
-
-
0.006
6-Thiopurine
-
-
0.34
6-Thioxanthine
-
-
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
-
-
2
8-Azahypoxanthine
-
-
0.54
8-bromo-2-aminohypoxanthine
-
-
0.39
8-mercaptoxanthine
-
-
4.1
8-oxohypoxanthine
-
-
0.42
8-thiohypoxanthine
-
-
0.87
Benzonitrile
-
-
0.286
cytosine
-
-
0.039
GMP
-
wild-type
0.044
GMP
-
mutant E215D
0.067
GMP
-
mutant E198D/E215D
0.1
Guanine
-
-
0.0035
hypoxanthine
-
-
1.06
isocytosine
-
-
0.808
Uracil
-
-
0.024
xanthine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
-
reaction with hypoxanthine and guanine
7.8
-
reaction with xanthine
8 - 8.5
substrate: xanthine
8 - 9.5
-
reaction with adenine
9.5
substrate: hypoxanthine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.9 - 9.1
-
80% of maximal activity at pH 6.9 and 9.1
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
deletion of the peroxisomal targeting sequence is not required for activity
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
additional information
-
immunohistologic subcellular localization study
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27000
-
gel filtration
704046
42000
-
gel filtration
638005
54000
-
in absence of 5-phospho-alpha-D-ribose 1-diphosphate, gel filtration
638004
62000
-
in presence of 5-phospho-alpha-D-ribose 1-diphosphate, gel filtration
638004
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of the dimeric XPRTase-GMP complex was determined to 2.05 A resolution
hanging drop vapor diffusion method
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6 - 10
-
stable
638005
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
pH 5.6-10, stable for 30 min
638005
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
increase in potassium phosphate buffer concentration from 1-50 mM increases stability
-
stabilizing compounds are: 5-phospho-alpha-D-ribose 1-diphosphate, XMP, 6-oxo-substituted purine nucleotides
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, stable for 6 months in intacts cells
-
-80C, 10 mM Tris-HCl buffer, pH 7.5
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification and formation of nucleotide free, GMP and XMP saturated complexes
by gel filtration, more than 95% pure
-
recombinant full length and C-terminally truncated enzymes from Escherichia coli by affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Escherichia coli Sphi606 or Sphi609 cells transformed with pSelect-LdXPRT, pSelectldxprtE198D, pSelect-ldxprtE215D, pSelect-ldxprtE215Q and pSelectldxprtE198,215D
-
expression in Escherichia coli
-
expression of full length and C-terminally truncated enzymes in Escherichia coli
-
isolation and characterization of the XPT1 gene
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E198D
-
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
-
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
-
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
-
can accommodate GMP in the active site
additional information
-
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
the enzyme lacks a mammalian counterpart and is, therefore, a potential target for antiparasitic therapy