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Information on EC 2.4.2.22 - xanthine phosphoribosyltransferase and Organism(s) Bacillus subtilis and UniProt Accession P42085

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.22 xanthine phosphoribosyltransferase
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Bacillus subtilis
UNIPROT: P42085 not found.
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
xprt, xgprt, xanthine phosphoribosyltransferase, hgxprt, hypoxanthine-guanine-xanthine phosphoribosyltransferase, xprtase, pf hgxprt, hypoxanthine-guanine-(xanthine) phosphoribosyltransferase, ecxgprt, xanthine prt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-phospho-alpha-D-ribose-1-diphosphate:xanthine phospho-D-ribosyltransferase
-
-
-
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phosphoribosyltransferase, xanthine
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-
-
-
Xan phosphoribosyltransferase
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-
-
-
xanthosine 5'-phosphate pyrophosphorylase
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-
-
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xanthylate pyrophosphorylase
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-
-
-
xanthylic pyrophosphorylase
-
-
-
-
XGPRT
-
-
-
-
XMP pyrophosphorylase
-
-
-
-
XPRT
-
-
-
-
XPRTase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
XMP:diphosphate 5-phospho-alpha-D-ribosyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-10-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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 + 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
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-
?
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
XMP + diphosphate
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-phospho-alpha-D-ribose 1-diphosphate + xanthine
XMP + diphosphate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
10 mM used in assay conditions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GMP
competitive against 5-phospho-alpha-D-ribose 1-diphosphate
pGpp
competitive inhibitor
ppGpp
competitive inhibitor
pppGpp
competitive inhibitor
Pyrophosphate
noncompetitive
XMP
competitive against 5-phospho-alpha-D-ribose 1-diphosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 0.069
5-phospho-alpha-D-ribose 1-diphosphate
0.281
guanine
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1.25
hypoxanthine
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0.0022
xanthine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5
hypoxanthine
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025
pppGpp
at pH 7.6 and 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00096
pGpp
Bacillus subtilis
at pH 7.6 and 25°C
0.0033
ppGpp
Bacillus subtilis
at pH 7.6 and 25°C
0.0564
pppGpp
Bacillus subtilis
at pH 7.6 and 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 8.5
substrate: xanthine
9.5
substrate: hypoxanthine
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of the dimeric XPRTase-GMP complex was determined to 2.05 A resolution
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57.3
melting temperature
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA spin column chromatography
purification and formation of nucleotide free, GMP and XMP saturated complexes
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
J. Mol. Biol.
432
4108-4126
2020
Bacillus subtilis (P42085), Bacillus subtilis, Bacillus subtilis 168 (P42085)
Manually annotated by BRENDA team