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Information on EC 2.4.2.9 - uracil phosphoribosyltransferase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q980Q4

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.9 uracil phosphoribosyltransferase
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This record set is specific for:
Saccharolobus solfataricus
UNIPROT: Q980Q4 not found.
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Word Map
The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
uracil phosphoribosyltransferase, uprt, uprtase, uracil phosphoribosyl transferase, cd-uprt, cytosine deaminase/uracil phosphoribosyltransferase, ump pyrophosphorylase, mtuprt, cytosine deaminase-uracil phosphoribosyltransferase, uridine monophosphate pyrophosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoribosyltransferase, uracil
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-
-
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UMP pyrophosphorylase
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-
-
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UMP:pyrophosphate phosphoribosyltransferase
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-
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UPRT
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-
-
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UPRTase
uridine 5'-phosphate pyrophosphorylase
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-
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uridine monophosphate pyrophosphorylase
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-
-
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uridylate pyrophosphorylase
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-
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uridylic pyrophosphorylase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
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-
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PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
UMP:diphosphate phospho-alpha-D-ribosyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9030-24-4
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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
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
show the reaction diagram
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
show the reaction diagram
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-
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-
?
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
uracil + 5-phospho-alpha-D-ribose 1-diphosphate
UMP + diphosphate
show the reaction diagram
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-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CTP
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powerful inhibitor in combination with UMP. CTP and UMP can be bound simultaneously
UMP
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powerful inhibitor in combination with CTP. CTP and UMP can be bound simultaneously
additional information
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the enzyme undergoes a transition from a weakly active or inactive T-state, favored by binding of UMP and CTP, to an active R-state, favored by binding of GTP and 5-phosphoribosyl 1-diphosphate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GTP
activating allosteric regulation by GTP. The regulatory triphosphate binds at a site in the center of the tetramer changing the quaternary arrangement. The effector contacts Pro94 at the beginning of a long beta-strand in the dimer interface, which extends into a flexible loop over the active site. In the GTP-bound state, two flexible loop residues, Tyr123 and Lys125, bind the diphosphate moiety of PRPP in the neighboring subunit and contribute to catalysis. The C-terminal Gly216 participates in a hydrogen-bond network in the dimer interface that stabilizes the inhibited, but not the activated, state
GTP
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strong stimulation, binds cooperatively with 5-phosphoribosyl 1-diphosphate
additional information
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the enzyme undergoes a transition from a weakly active or inactive T-state, favored by binding of UMP and CTP, to an active R-state, favored by binding of GTP and 5-phosphoribosyl 1-diphosphate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.36 - 6.1
5-phospho-alpha-D-ribose 1-diphosphate
0.36 - 6.1
Uracil
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8
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pH 3.8: no activity, pH 5.5: optimum, pH 8: about 20% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
98000
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sucrose density gradient centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with UMP, enzyme in complex with CTP, structure with UMP bound in half of the active sites. Hanging-drop vapour-diffusion method
two structures of the activated state enzyme in complex with GTP, X-ray diffraction structure determination and analysis at 2.8 A resolution, the first structure which contains PRPP in all active sites, and 2.9 A resolution, for the second structure with PRPP in two sites and the hydrolysis products ribose-5-phosphate and diphosphate in the other sites, respectively, and a third structure of the enzyme in complex with UMP and the allosteric inhibitor CTP
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arent, S.; Harris, P.; Jensen, K.F.; Larsen, S.
Allosteric regulation and communication between subunits in uracil phosphoribosyltransferase from Sulfolobus solfataricus
Biochemistry
44
883-892
2005
Saccharolobus solfataricus (Q980Q4), Saccharolobus solfataricus
Manually annotated by BRENDA team
Jensen, K.F.; Arent, S.; Larsen, S.; Schack, L.
Allosteric properties of the GTP activated and CTP inhibited uracil phosphoribosyltransferase from the thermoacidophilic archaeon Sulfolobus solfataricus
FEBS J.
272
1440-1453
2005
Saccharolobus solfataricus
Manually annotated by BRENDA team
Christoffersen, S.; Kadziola, A.; Johansson, E.; Rasmussen, M.; Willemoes, M.; Jensen, K.F.
Structural and kinetic studies of the allosteric transition in Sulfolobus solfataricus uracil phosphoribosyltransferase: Permanent activation by engineering of the C-terminus
J. Mol. Biol.
393
464-477
2009
Saccharolobus solfataricus (Q980Q4), Saccharolobus solfataricus
Manually annotated by BRENDA team