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 ACCESSION NO.
LITERATURE
XMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + xanthine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Metabolic pathways
-
Purine metabolism
-
xanthine and xanthosine salvage
-
SYSTEMATIC NAME
IUBMB Comments
XMP:diphosphate 5-phospho-alpha-D-ribosyltransferase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
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
-, P42085
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + guanine
GMP + diphosphate
show the reaction diagram
P0A9M5
-
-
-
?
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
-, P42085
-
-
-
?
5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
IMP + diphosphate
show the reaction diagram
P0A9M5
-
-
-
?
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
P0A9M5
-
-
-
?
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
-, P42085
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 ACCESSION NO.
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 ACCESSION NO.
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+
P0A9M5
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 ACCESSION NO.
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-thiohypoxanthine
-
-
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-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
-
-
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
GDP
-
1 mM, 93 inhibition
GMP
-
1 mM, 89% inhibition
GMP
-, P42085
competitive against 5-phospho-alpha-D-ribose 1-diphosphate
GMP
-
inhibition of the xanthine phosphoribosylation
GTP
-
1 mM, 91% inhibition
hypoxanthine
-
-
Pyrophosphate
-, P42085
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
XMP
-
1 mM, 92% inhibition
XMP
-, P42085
competitive against 5-phospho-alpha-D-ribose 1-diphosphate
XTP
-
1 mM, 92% inhibition
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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
-, P42085
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
P0A9M5
-
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
P0A9M5
-
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
-, P42085
-
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
P0A9M5
-
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
-, P42085
-
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
-, P42085
-
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
P0A9M5
-
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.1
-
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E215Q, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
2.6
-
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E215Q, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
3.6
-
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E198D/E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
3.9
-
5-phospho-alpha-D-ribose 1-diphosphate
-
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
-
mutant E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
8.4
-
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E198D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine
12.3
-
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E198D/E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
15.1
-
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
20.7
-
5-phospho-alpha-D-ribose 1-diphosphate
-
mutant E198D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine
112
-
5-phospho-alpha-D-ribose 1-diphosphate
P0A9M5
-
0.00367
-
9-(5-phospho-beta-D-ribosyl)xanthine
-
mutant E215D, at 25C, in TM buffer
0.0103
-
9-(5-phospho-beta-D-ribosyl)xanthine
-
mutant E198D, at 25C, in TM buffer
0.0148
-
9-(5-phospho-beta-D-ribosyl)xanthine
-
mutant E198D/E215D, at 25C, in TM buffer
0.028
-
9-(5-phospho-beta-D-ribosyl)xanthine
-
wild-type, at 25C, in TM buffer
0.043
-
9-(5-phospho-beta-D-ribosyl)xanthine
-
mutant E215Q, at 25C, 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
-, P42085
-
0.1
-
Guanine
-
mutant E215Q, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
1.1
-
Guanine
-
mutant E198D/E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
1.5
-
Guanine
-
mutant E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
3.3
-
Guanine
-
mutant E198D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
112
-
Guanine
P0A9M5
-
0.5
-
hypoxanthine
-, P42085
-
2.2
-
hypoxanthine
-
mutant E198D/E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
2.4
-
hypoxanthine
-
mutant E215Q, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
2.6
-
hypoxanthine
-
-
3.1
-
hypoxanthine
-
wild-type, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
7.1
-
hypoxanthine
-
mutant E198D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
8.7
-
hypoxanthine
-
mutant E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
54.8
-
hypoxanthine
P0A9M5
-
0.006167
-
IMP
-
mutant E198D/E215D, at 25C, in TM buffer
2
-
xanthine
-
mutant E215Q, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
3.5
-
xanthine
-
-
3.5
-
xanthine
-
wild-type, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
11
-
xanthine
-, P42085
-
16.4
-
xanthine
-
mutant E198D/E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
17.5
-
xanthine
-
mutant E215D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
23.3
-
xanthine
-
mutant E198D, at 25C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate
150
-
xanthine
P0A9M5
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
0.033
-
GMP
-, P42085
Kis
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
-
-
0.022
-
XMP
-, P42085
Kis
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
reaction with hypoxanthine and guanine
7.8
-
-
reaction with xanthine
8
8.5
-, P42085
substrate: xanthine
8
9.5
-
reaction with adenine
9.5
-
-, P42085
substrate: hypoxanthine
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.9
9.1
-
80% of maximal activity at pH 6.9 and 9.1
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
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
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
27000
-
-
gel filtration
42000
-
-
gel filtration
54000
-
-
in absence of 5-phospho-alpha-D-ribose 1-diphosphate, gel filtration
62000
-
-
in presence of 5-phospho-alpha-D-ribose 1-diphosphate, gel filtration
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure of the dimeric XPRTase-GMP complex was determined to 2.05 A resolution
-, P42085
hanging drop vapor diffusion method
P0A9M5
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.6
10
-
stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
pH 5.6-10, stable for 30 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
-70C, stable for 6 months in intacts cells
-
-80C, 10 mM Tris-HCl buffer, pH 7.5
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purification and formation of nucleotide free, GMP and XMP saturated complexes
-, P42085
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 ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
the enzyme lacks a mammalian counterpart and is, therefore, a potential target for antiparasitic therapy