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Information on EC 2.4.2.3 - uridine phosphorylase
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2.4.2.3 uridine phosphorylaseIUBMB Comments
The enzyme participates the the pathways of pyrimidine ribonucleosides degradation and salvage. The mammalian enzyme also accepts 2'-deoxyuridine.
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Word Map
- 2.4.2.3
- pyrimidine
- nucleoside
- thymidine
- uracil
- 5-fluorouracil
-
phosphorolysis
-
salvage
-
phosphoribosyltransferase
- orotate
-
phosphorylases
- cytidine
- thymidylate
-
fluoropyrimidine
- udp
-
dihydropyrimidine
- 5'-deoxy-5-fluorouridine
- ribose-1-phosphate
- 5-fluoro-2'-deoxyuridine
- acyclonucleoside
- 5-fluorouridine
-
mete
-
uridine-cytidine
- orotidine
- capecitabine
-
fdurd
- dthdpase
- 5-methyluridine
- dihydrouracil
- drug development
- synthesis
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
upase, uph, urdpase, stuph, uridine phosphorylase 1, l-urdpase, upase-2, uridine phosphorylase-2, uridine phosphorylase-1, up type 1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
apUP
phosphorylase, uridine
-
-
-
-
pynpase
pyrimidine nucleoside phosphorylase
pyrimidine phosphorylase
-
-
-
-
UDRPase
-
-
-
-
UP1
UPase
UPase-2
UPH
UrdPase
-
-
-
-
uridine phosphorylase
uridine phosphorylase-1
uridine phosphorylase-2
uridine:orthophosphate alpha-D-ribosyltransferase
-
-
-
-
additional information
the enzyme belongs to the NP1 subfamily of the nucleoside phosphorylase, NP, superfamily of enzymes
UPase
-
-
-
-
UPH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
sequential rather than ping-pong mechanism, addition of substrate is random
-
uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
ordered bi-bi mechanism, phosphate binds before uridine and alpha-D-ribose 1-phosphate is released after uracil
-
uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
ordered bi-bi mechanism
-
uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
rapid-equilibrium random mechanism
-
uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
random mechanism
-
uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
ordered bi-bi mechanism; phosphate binds before uridine and ribose 1-phosphate is released after uracil
-
uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
sequential mechanism
-
uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
sequential mechanism
-
uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
sequential mechanism
-
uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
steady-state random kinetic mechanism. Reaction follows an ANDN/SN2 mechanism where chemistry contributes significantly to the overall rate-limiting step of the reaction. No kinetically significant proton transfer step is involved at the transition state. Proton transfer to neutralize the leaving group is not part of transition state formation, consistent with an enzyme-stabilized anionic uracil as the leaving group. Kinetic analysis as a function of pH indicates one protonated group essential for catalysis and for substrate binding
-
uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
binding isotope effects indicate ground-state stabilization in the Michaelis complex, such as bonding environment, ribosyl pucker, and natural bond orbital charges
-
uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
rapid-equilibrium random mechanism
Escherichia coli B / ATCC 11303
-
-
uridine + phosphate = uracil + alpha-D-ribose 1-phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
pentosyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
uridine:phosphate alpha-D-ribosyltransferase
The enzyme participates the the pathways of pyrimidine ribonucleosides degradation and salvage. The mammalian enzyme also accepts 2'-deoxyuridine.
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CAS REGISTRY NUMBER
COMMENTARY
9030-22-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-deoxy-5-fluorouridine + alpha-D-ribose 1-phosphate
5'-deoxy-5-fluorouridine + phosphate
-
-
-
-
?
5-fluoro-2'-deoxyuridine + phosphate
5-fluorouracil + 2-deoxy-alpha-D-ribose 1-phosphate
-
-
-
?
5-fluoro-2'-deoxyuridine + phosphate
5-fluorouracil + 2-deoxy-D-ribose-1-phosphate
-
-
also accepts 2'-deoxypyrimidine nucleosides in higher organisms
-
r
5-fluorouracil + alpha-D-ribose 1-phosphate
5-fluorouridine + phosphate
-
-
-
-
?
5-methyluridine + phosphate
thymine + alpha-D-ribose 1-phosphate
-
19% of the activity with uridine
-
-
?
6-methyluridine + phosphate
6-methyluracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
arabinofuranosyl-5-ethyluracil + phosphate
5-ethyluracil + arabinose-1-phosphate
-
weak substrate
-
-
?
cytidine + phosphate
cytosine + alpha-D-ribose 1-phosphate
-
-
-
-
?
guanosine + phosphate
guanine + alpha-D-ribose 1-phosphate
10% of the activity with uridine
-
-
r
inosine + phosphate
hypoxanthine + alpha-D-ribose 1-phosphate
-
-
-
?
pyrimidine nucleoside + phosphate
pyrimidine base + alpha-D-ribose 1-phosphate
-
most pyrimidine nucleosides except for 4-amino-substituted species like deoxycytidine
or alpha-D-deoxyribose 1-phosphate
-
r
2'-deoxyuridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
2'-deoxyuridine + phosphate
uracil + alpha-D-ribose 1-phosphate
Shewanella oneidensis MR-1 / ATCC 700550
-
-
-
-
?
2'-deoxyuridine + phosphate
uracil + deoxyribose 1-phosphate
-
6% of the activity with uridine
-
?
2'-deoxyuridine + phosphate
uracil + deoxyribose 1-phosphate
-
activities of uridine, deoxyuridine and thymidine phosphorylase from Giardia lamblia remain associated throughout purification suggesting that a single enzyme is responsible for the 3 activities
-
-
?
2'-deoxyuridine + phosphate
uracil + deoxyribose 1-phosphate
-
12% of the activity with uridine
-
-
?
2'-deoxyuridine + phosphate
uracil + deoxyribose 1-phosphate
-
18% of the activity with uridine
-
-
?
2'-deoxyuridine + phosphate
uracil + deoxyribose 1-phosphate
-
catalyzed by a different protein or by a different active center of the same enzyme
-
r
2'-deoxyuridine + phosphate
uracil + deoxyribose 1-phosphate
-
unlike cytosolic enzyme, enzyme from plasma membranes shows little or no deoxyuridine-cleaving activity
-
-
?
2'-deoxyuridine + phosphate
uracil + deoxyribose 1-phosphate
-
-
-
-
?
5'-deoxy-5-fluorouridine + phosphate
5-fluorouracil + 5-deoxyribose-1-phosphate
-
-
-
-
?
5'-deoxy-5-fluorouridine + phosphate
5-fluorouracil + 5-deoxyribose-1-phosphate
-
25% of the activity with uridine
-
-
?
5-bromo-2'-deoxyuridine + phosphate
5-bromouracil + 2-deoxribose 1-phosphate
-
27% of the activity with uridine
-
-
?
5-bromo-2'-deoxyuridine + phosphate
5-bromouracil + 2-deoxribose 1-phosphate
-
75% of the activity with uridine
-
-
?
5-bromouracil + deoxyribose 1-phosphate
5-bromodeoxyuridine + phosphate
-
-
-
-
-
5-bromouracil + deoxyribose 1-phosphate
5-bromodeoxyuridine + phosphate
-
-
-
-
?
5-bromouridine + phosphate
5-bromouracil + alpha-D-ribose 1-phosphate
-
69% of the activity with uridine
-
-
?
5-bromouridine + phosphate
5-bromouracil + alpha-D-ribose 1-phosphate
-
40% of the activity with uridine
-
-
?
5-bromouridine + phosphate
5-bromouracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
5-fluoro-2'-deoxyuridine + phosphate
5-fluorouracil + 2-deoxyribose-1-phosphate
-
14% of the activity with uridine
-
-
?
5-fluoro-2'-deoxyuridine + phosphate
5-fluorouracil + 2-deoxyribose-1-phosphate
-
15% of the activity with uridine
-
-
?
5-fluorouracil + alpha-D-ribose-1-phosphate
5-fluorouridine + phosphate
-
-
-
-
?
5-fluorouracil + alpha-D-ribose-1-phosphate
5-fluorouridine + phosphate
-
-
-
-
?
5-fluorouridine + phosphate
5-fluorouracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
5-fluorouridine + phosphate
5-fluorouracil + alpha-D-ribose 1-phosphate
-
-
-
-
r
5-fluorouridine + phosphate
5-fluorouracil + alpha-D-ribose-1-phosphate
-
-
-
?
5-fluorouridine + phosphate
5-fluorouracil + alpha-D-ribose-1-phosphate
-
15% of the activity with uridine
-
-
?
5-fluorouridine + phosphate
5-fluorouracil + alpha-D-ribose-1-phosphate
-
85% of the activity with uridine
-
-
?
5-fluorouridine + phosphate
5-fluorouracil + alpha-D-ribose-1-phosphate
-
-
-
-
?
5-methyluridine + phosphate
5-methyluracil + alpha-D-ribose 1-phosphate
-
92% compared to the activity with uridine
-
-
?
5-methyluridine + phosphate
5-methyluracil + alpha-D-ribose 1-phosphate
92% compared to the activity with uridine
-
-
?
5-methyluridine + phosphate
5-methyluracil + alpha-D-ribose 1-phosphate
-
27% of the activity with uridine
-
-
?
5-methyluridine + phosphate
5-methyluracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
5-methyluridine + phosphate
5-methyluracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
5-methyluridine + phosphate
5-methyluracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
5-methyluridine + phosphate
5-methyluracil + alpha-D-ribose 1-phosphate
Shewanella oneidensis MR-1 / ATCC 700550
-
-
-
-
?
deoxyuridine + phosphate
uracil + 2-deoxy-alpha-D-ribose 1-phosphate
-
-
-
?
deoxyuridine + phosphate
uracil + 2-deoxy-alpha-D-ribose 1-phosphate
14% of the activity with uridine
-
-
r
deoxyuridine + phosphate
uracil + deoxy-D-ribose 1-phosphate
-
66% compared to the activity with uridine
-
-
?
deoxyuridine + phosphate
uracil + deoxy-D-ribose 1-phosphate
66% compared to the activity with uridine
-
-
?
fluorouridine + phosphate
fluorouracil + alpha-D-ribose-1-phosphate
-
-
-
-
?
thymidine + phosphate
thymine + alpha-D-ribose 1-phosphate
-
60% compared to the activity with uridine
-
-
?
thymidine + phosphate
thymine + alpha-D-ribose 1-phosphate
60% compared to the activity with uridine
-
-
?
thymidine + phosphate
thymine + alpha-D-ribose 1-phosphate
-
2% of the activity with uridine
-
-
?
thymidine + phosphate
thymine + alpha-D-ribose 1-phosphate
-
the activities of uridine, deoxyuridine and thymidine phosphorylases from Giardia lamblia remain associated throughout purification, suggesting that a single enzyme is responsible for the 3 activities
-
-
?
thymidine + phosphate
thymine + alpha-D-ribose 1-phosphate
-
21% of the activity with uridine
-
-
?
thymidine + phosphate
thymine + alpha-D-ribose 1-phosphate
-
to a lesser extent compared to uridine
-
-
?
thymidine + phosphate
thymine + alpha-D-ribose 1-phosphate
-
22% of the activity with uridine
-
-
?
thymidine + phosphate
thymine + alpha-D-ribose 1-phosphate
-
to a lesser extent compared to uridine
-
-
?
thymidine + phosphate
thymine + alpha-D-ribose 1-phosphate
-
-
-
-
?
thymidine + phosphate
thymine + alpha-D-ribose 1-phosphate
-
-
-
?
thymidine + phosphate
thymine + alpha-D-ribose 1-phosphate
Shewanella oneidensis MR-1 / ATCC 700550
-
-
-
-
?
uracil + alpha-D-ribose 1-phosphate
uridine + phosphate
-
uridine prevents the glucose deprivation-induced death of immunostimulated astrocytes via the action of uridine phosphorylase
-
-
?
uracil arabinoside + phosphate
uracil + arabinose-1-phosphate
-
10% of the activity with uridine
-
-
?
uracil arabinoside + phosphate
uracil + arabinose-1-phosphate
-
10% of the activity with uridine
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
r
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
the optimal substrate for the enzyme is uridine. It shows no activity for 5-fluorouridine, cytidine, or 2-deoxycytidine
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
the optimal substrate for the enzyme is uridine. It shows no activity for 5-fluorouridine, cytidine, or 2-deoxycytidine
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
key enzyme in pyrimidine-salvage pathway
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
liver enzyme is highly specific to uridine
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
equilibrium position favouring nucleoside synthesis
-
r
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
broader specificity than human enzyme
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
enzyme of pyrimidine salvage pathway
-
-
-
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
-
r
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
in conjunction with uridine kinase, the enzyme provides a route for the conversion of uracil to UMP via uridine
-
-
-
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
role in degradation of pyrimidine nucleosides as well as in the salvage pathway for nucleic acid synthesis
-
-
-
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
cleavage of the N-glycosidic bond
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
enzyme of pyrimidine salvage pathway
-
-
-
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
Shewanella oneidensis MR-1 / ATCC 700550
-
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
best substrate, active site structure, overview
-
-
r
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
?
additional information
?
-
-
no substrates are: thymidine, deoxyuridine, fluorodeoxyuridiune, 5'-deoxyfluorouridine
-
-
-
additional information
?
-
-
no substrate: 5-substituted-2,2'-anhydrouridine
-
-
-
additional information
?
-
-
catalyzes the first step of uridine degradation to beta-alanine in liver
-
-
-
additional information
?
-
UPP catalyzes the reversible phosphorolysis of uracil ribosides and analogous compounds to their respective nucleobases and ribose-1-phosphate, structural mechanisms, overview
-
-
-
additional information
?
-
-
no substrates: 2-deoxyuridine, adenosine
-
-
-
additional information
?
-
-
no substrate: 5-substituted-2,2'-anhydrouridine
-
-
-
additional information
?
-
-
the enzyme is regulated by multiple lipid-sensing nuclear receptors, gene expression is diurnally regulated
-
-
-
additional information
?
-
-
no substrates: 3'-azido-2',3'-dideoxy-5-methyluridine, 3'-azido-2',3'-dideoxy-5-ethyluridine, 2',3'-dideoxy-5-ethyluridine, 3'-chloro-2',3'-dideoxy-5-ethyluridine, 3'-chloro-2',3'-dideoxy-5-methyluridine, 3'-bromo-2',3'-dideoxy-5-ethyluridine, 2'-deoxylyxofuranosyl-5-ethyluracil, 3'-O-acetyl-2,2'-anhydro-5-ethyluridine, 2,3'-anhydro-2'-deoxy-5-ethyluridine, 2,5'-anhydro-2'-deoxy-5-ethyluridine
-
-
-
additional information
?
-
-
catalyzes the first step of uridine degradation to beta-alanine in liver
-
-
-
additional information
?
-
-
no substrates: inosine, adenosine, guanosine, thymidine
-
-
-
additional information
?
-
-
the enzyme also activates pyrimidine-containing drugs, including 5-fluorouracil, mechanism of the enzyme-drug interaction, overview
-
-
-
additional information
?
-
-
no substrates: cytosine, deoxycytidine, orotidine
-
-
-
additional information
?
-
strict substrate specificty of the enzyme, overview. Deoxyadenosine, and deoxyguanosine are poor substrates, thymidine, cytidine, deoxycytidine, inosine, and adenosine are no substrates
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyrimidine nucleoside + phosphate
pyrimidine base + alpha-D-ribose 1-phosphate
-
most pyrimidine nucleosides except for 4-amino-substituted species like deoxycytidine
or alpha-D-deoxyribose 1-phosphate
-
r
uracil + alpha-D-ribose 1-phosphate
uridine + phosphate
-
uridine prevents the glucose deprivation-induced death of immunostimulated astrocytes via the action of uridine phosphorylase
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
key enzyme in pyrimidine-salvage pathway
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
enzyme of pyrimidine salvage pathway
-
-
-
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
in conjunction with uridine kinase, the enzyme provides a route for the conversion of uracil to UMP via uridine
-
-
-
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
role in degradation of pyrimidine nucleosides as well as in the salvage pathway for nucleic acid synthesis
-
-
-
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
enzyme of pyrimidine salvage pathway
-
-
-
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
Shewanella oneidensis MR-1 / ATCC 700550
-
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
-
-
-
-
?
uridine + phosphate
uracil + alpha-D-ribose 1-phosphate
Q7AZX0
-
-
-
?
additional information
?
-
-
catalyzes the first step of uridine degradation to beta-alanine in liver
-
-
-
additional information
?
-
Q16831
UPP catalyzes the reversible phosphorolysis of uracil ribosides and analogous compounds to their respective nucleobases and ribose-1-phosphate, structural mechanisms, overview
-
-
-
additional information
?
-
-
the enzyme is regulated by multiple lipid-sensing nuclear receptors, gene expression is diurnally regulated
-
-
-
additional information
?
-
-
catalyzes the first step of uridine degradation to beta-alanine in liver
-
-
-
additional information
?
-
-
the enzyme also activates pyrimidine-containing drugs, including 5-fluorouracil, mechanism of the enzyme-drug interaction, overview
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
stabilizes the enzyme, which possesses an intermolecular metal-binding site, structure, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-((2-pyrrolidine-1-yl)ethyl)uracil
inhibits both enzymic activity and growth of Plasmodium falciparum
1-(1',2'-dihydroxypropyl)-5,6-tetramethyleneuracil
-
only the R-enantiomer inhibits, but not the S-enantiomer
1-(1',3'-dihydroxy-2'-propoxy)methyl-5,6-tetramethyleneuracil
-
inhibits forward and reverse reaction
1-(1',3'-dihydroxy-2'-propoxy)methyl-5-benzyluracil
-
i.e. DHPBU, competitive
3-((2-pyrrolidine-1-yl)ethyl)uracil
inhibits both enzymic activity and growth of Plasmodium falciparum
4-benzyl-6-hydroxy-2-oxo-1,2-dihydropyridine-3-carbonitrile
-
2% inhibition at 0.001 mM
4-ethyl-6-hydroxy-2-oxo-1,2-dihydropyridine-3-carbonitrile
-
25% inhibition at 0.001 mM
4-hydroxy-5-[[(2-hydroxyethyl)amino]methyl]-3,4-dihydropyrimidin-2(1H)-one
-
2% inhibition at 0.001 mM
5-Azauracil
-
reaction is inhibited in the direction of deoxyuridine synthesis more than in the direction of their cleavage at the same concentration of 5-azauracil
5-benzyl-1-(2'-hydroxyethoxymethyl)uracil
-
competitive inhibition with respect to uridine, noncompetitive inhibition with respect to phosphate
5-benzyl-6-hydroxy-4-methyl-2-oxo-1,2-dihydropyridine-3-carbonitrile
-
43% inhibition at 0.001 mM
5-[(diethylamino)methyl]-6-hydroxy-4-methyl-2-oxo-1,2-dihydropyridine-3-carbonitrile
-
25% inhibition at 0.001 mM
5-[(dimethylamino)methyl]-6-hydroxy-4-methyl-2-oxo-1,2-dihydropyridine-3-carbonitrile
-
81% inhibition at 0.001 mM
5-[[(1,3-dihydroxypropan-2-yl)amino]methyl]-6-hydroxy-4-methyl-2-oxo-1,2-dihydropyridine-3-carbonitrile
-
82% inhibition at 0.001 mM
5-[[(2,3-dihydroxypropyl)amino]methyl]-6-hydroxy-4-methyl-2-oxo-1,2-dihydropyridine-3-carbonitrile
-
78% inhibition at 0.001 mM
6-hydroxy-2-oxo-4-(propan-2-yl)-1,2-dihydropyridine-3-carbonitrile
-
31% inhibition at 0.001 mM
6-hydroxy-2-oxo-4-phenyl-1,2-dihydropyridine-3-carbonitrile
-
42% inhibition at 0.001 mM
6-hydroxy-2-oxo-4-propyl-1,2-dihydropyridine-3-carbonitrile
-
16% inhibition at 0.001 mM
6-hydroxy-4-methyl-2-oxo-1,2-dihydropyridine-3-carbonitrile
-
70% inhibition at 0.001 mM
6-hydroxy-4-methyl-2-oxo-5-phenyl-1,2-dihydropyridine-3-carbonitrile
-
12% inhibition at 0.001 mM
6-hydroxy-4-methyl-2-oxo-5-[(piperidin-1-yl)methyl]-1,2-dihydropyridine-3-carbonitrile
-
49% inhibition at 0.001 mM
6-hydroxy-4-methyl-5-[(morpholin-4-yl)methyl]-2-oxo-1,2-dihydropyridine-3-carbonitrile
-
51% inhibition at 0.001 mM
6-hydroxy-5-(((2-hydroxyethyl) amino) methyl)-4-methyl-1H-pyridin-2-one-3-carbonitrile
-
6-hydroxy-5-(((2-hydroxyethyl)amino)methyl)-4-methyl-1H-pyridin-2-one-3-carbonitrile
-
80% inhibition at 0.001 mM
Acyclonucleoside analogues
-
consisting of 5- and 5,6-substituted uracils and different acyclic chains
-
Deoxyglucosylthymine
-
phosphorolysis of uridine and deoxyuridine, synthesis of uridine at concentrations of 0.10 mM, 0.018 mM and 0.14 mM, not: phosphorolysis of deoxyuridine or thymidine at 0.19 mM
guanidine hydrochloride
-
50% loss of activity at 1.04 M, only little residual activity between 2 and 6 M
potassium 5-cyano-4-methyl-6-oxo-1,6-dihydropyridin-2-olate
-
60% inhibition at 0.001 mM
5-benzylacyclouridine
-
0.01 mM, 90% inhibition of normal tissues, 40-60% inhibition of carcinoma tissue
5-benzylacyclouridine
an UPP1-specific inhibitor. Binding of the inhibitor to the UPP1 active site, structure, overview
alpha-D-ribose 1-phosphate
product inhibition pattern, noncompetitive versus uridine, competitive versus phosphate, overview
alpha-D-ribose 1-phosphate
-
product inhibition, noncompetitive with respect to uridine and phosphate
Uracil
product inhibition pattern, noncompetitive versus uridine and phosphate, overview
Uracil
-
product inhibition, oncompetitive with respect to uridine and phosphate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
UPase expression is up-regulated by glucose deprivation in mRNA as well as protein levels
-
additional information
-
UPase expression is up-regulated by glucose deprivation in mRNA as well as protein levels
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.121
2'-deoxyuridine
-
in 50 mM potassium phosphate buffer, pH 7.5, 25°C
0.036
5-fluorouracil
-
cosubstrate: alpha-D-ribose-1-phosphate, enzyme from liver
0.046
5-fluorouracil
-
cosubstrate: alpha-D-ribose-1-phosphate, enzyme from colon tumor
0.06
5-fluorouracil
-
cosubstrate: alpha-D-ribose-1-phosphate, enzyme from colon tumor
0.065
5-methyluridine
-
in 50 mM potassium phosphate buffer, pH 7.5, 25°C
0.02
alpha-D-ribose-1-phosphate
-
cosubstrate: 5-fluorouracil, enzyme from liver
0.038
alpha-D-ribose-1-phosphate
-
cosubstrate: 5-fluorouracil, enzyme from colon tumor
0.04
alpha-D-ribose-1-phosphate
-
cosubstrate: 5-fluorouracil, enzyme from colon tumor
0.087
alpha-D-ribose-1-phosphate
-
cosubstrate: uracil, enzyme from colon tumor
0.0489
thymidine
pH and temperature not specified in the publication
0.367
Uracil
-
cosubstrate: alpha-D-ribose-1-phosphate, enzyme from colon tumor
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.41
thymidine
pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.38
thymidine
pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000018
5-(3'-Benzyloxybenzyl)-1-[(1'-aminomethyl-2'-hydroxyethoxy)methyl]uracil
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
pH dependence of enzyme activities with different substrates, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.4
7.5
8.2
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8 - 9
-
pH 5.8: about 50% of activity maximum, pH 9.0: about 40% of activity maximum
6 - 8.5
pH dependence of enzyme activities with different substrates, overview
6.5 - 10.5
-
pH 6.5: about 50% of activity maximum, pH 10.5: about 65% of activity maximum
7 - 7.75
-
pH 6.5: about 70% of activity maximum, pH 8.5: about 25% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 80
-
40°C: about 40% of activity maximum, 80°C: about 10% of activity maximum
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
638456, 638457, 638461, 638510, 638512, 638513, 658264, 673810, 674024, 674032, 676161, 684470, 705806
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
recombinant enzyme
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
colon 26 tumor cells transplanted in BALB/c mice
brenda
-
N-butyl-N-(4-hydoxybutyl) nitrosamine (BBN) treatment for 12 weeks induces invasive cancer development in mice
brenda
-
N-butyl-N-(4-hydoxybutyl) nitrosamine (BBN) treatment for 12 weeks induces superficial cancer development in rats
brenda
-
12, 16 and 20 weeks after initiation of BBN treatment: higher PyNpase level in invasive carcinoma and hyperplasia compared to controls
brenda
-
12 weeks after initiation of BBN treatment: higher PyNpase level in superficial cancer and hyperplasia compared to controls, 16 and 20 weeks after initiation of BBN treatment: higher PyNpase level in superficial cancer but not in hyperplasia compared to controls
brenda
-
negative correlation between UPase expression and the clinical outcome of breast cancer
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
associated with intermediate filament vimentin in fibroblasts and colon 26 cells
brenda
-
60-70% of the enzyme exists in the cytosol as a soluble protein
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
uridine phosphorylase is a key enzyme in the pyrimidine salvage pathway, catalyzing the reversible phosphorolysis of uridine to uracil and ribose-1-phosphate
metabolism
uridine phosphorylase is a ubiquitous enzyme involved in pyrimidine salvage and maintenance of uridine homeostasis
physiological function
uridine phosphorylase is a ubiquitous enzyme involved in pyrimidine salvage and maintenance of uridine homeostasis. UPP1 plays a role in the activation of pyrimidine nucleoside analogues used in chemotherapy, such as 5-fluorouracil and its prodrug, capecitabine
physiological function
-
the enzyme contributes to the antineoplastic activity of 5'-deoxy-5-fluorouridine. The peroxisome proliferator-activated receptor gamma coactivator-1alpha enhances antiproliferative activity of 5-deoxy-5-fluorouridine in cancer cells through induction of uridine phosphorylase, overview
Show AA Sequence and Transmembrane Helices (7003 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Actinobacillus succinogenes (strain ATCC 55618 / 130Z)
Aliivibrio fischeri (strain ATCC 700601 / ES114)
Escherichia coli (strain K12)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Shewanella oneidensis (strain MR-1)
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Yersinia pseudotuberculosis serotype I (strain IP32953)
Aliivibrio fischeri (strain ATCC 700601 / ES114)
Aliivibrio fischeri (strain ATCC 700601 / ES114)
Aliivibrio fischeri (strain ATCC 700601 / ES114)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26000
27000
27500
26000
-
4 * 26000, SDS-PAGE in presence of 4 M urea and 0.5% 2-mercaptoethanol
26000
-
4 * 26000, SDS-PAGE in presence of 6 M urea, without 2-mercaptoethanol
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
isozyme UPP1, the N-terminus of the protein forms a strand-turn-strand structure bracketed by two short helices, structure, overview
hexamer
homodimer
homohexamer
monomer
tetramer
homodimer
each monomer is composed of a central 11-stranded mixed beta-sheet surrounded by 14 alpha-helices and two peripheral short, 2-stranded antiparallel beta-sheets
tetramer
-
4 * 26000, SDS-PAGE in presence of 4 M urea and 0.5% 2-mercaptoethanol
tetramer
-
4 * 26000, SDS-PAGE in presence of 6 M urea, without 2-mercaptoethanol
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion method, crystals of thymidine phosphate complex, 2'-deoxyuridine complex, 5-fluorouracil ribose 1-phosphate complex and native enzyme form
-
hanging-drop vapour-diffusion method, structures of 5-benzylacyclouridine, 5-phenylthioacyclouridine, 5-phenylselenylacyclouridine, 5-m-benzyloxybenzyl acyclouridine and 5-m-benzyloxybenzyl barbituric acid acyclonucleoside bound to the active site of the enzyme, resolutions ranging from 1.95 to 2.3 A
-
free enzyme and enzyme in complex with inhibitor 5-benzylacyclouridine, 3 mg/ml protein in absence or presence of 1 mM inhibitor from 17% PEG 3350, 100 mM Bis-Tris buffer, pH 5.5, 300 mM KCl, and 30 mM MgCl2, or for the ligand-free ezyme crystals from 1.2 M (NH4)2SO4, 100 mM Bis-Tris buffer pH 5.5, with 1-2% MPD, with 2-3 mg/ml protein, X-ray diffraction structure determination and analysis at 2.3 A and 1.9 A resolution, respectively
in complex with 5-fluorouridine, to 2.3 A resolution. The dimeric enzyme is capable of a large hinge motion between its two domains, facilitating ligand exchange and explaining observed cooperativity between the two active sites in binding phosphate-bearing substrates. A loop toward the back end of the uracil binding pocket flexibly adjusts to the varying chemistry of different compounds through an ‘induced-fit association mechanism
-
two crystallographic structures of human isoform UPP2 in distinctly active and inactive conformations, to 2.0 and 1.54 A resolution, respectively. The structures reveal that a conditional intramolecular disulfide bridge can form within the protein that dislocates critical phosphate-coordinating arginine residue R100 away from the active site, disabling the enzyme. The state of the disulfide bridge has further structural consequences for one face of the enzyme that suggest UPP2 may have additional functions in sensing and initiating cellular responses to oxidative stress
-
modeling of the inhibitors 1-((2-pyrrolidine-1-yl)ethyl)uracil and 3-((2-pyrrolidine-1-yl)ethyl)uracil into the active site of the protein, PDB entry 1NW4, by superposition of the uracil ring and the purine ring of Immucillin-H. Both compounds can fit adequately in the active site. In both cases the uracil base is predicted to be oriented in the nucleoside binding pocket by a pi-stacking similar to the purine base of Immucillin-H. The N1 of the uracil base in 1-((2-pyrrolidine-1-yl)ethyl)uracil and the N3 of the uracil base in 3-((2-pyrrolidine-1-yl)ethyl)uracil roughly superimpose with the C4 of Immucillin-H
complexed with 2,2-anhydrouridine, phosphate and potassium ions at 1.86 A resolution. The monomer is an alpha/beta-class polypeptide with a trilayer alpha/beta/alpha sandwich architecture. The potassium ion is located in the intermonomeric region of each homodimer on the local axis of second order of point group 32. The side chains of Glu49B and Ser73B and the carbonyl O atom of Ile69B in the B subunit, as well as symmetrical residues from the D subunit of the BD homodimer, coordinate K+. The residues in the phosphate binding site are Arg30B, Arg91B, Thr94B and Gly26B from the B subunit, and Arg48D from the D subunit
-
enzyme in complex with 5-fluorouracil, hanging-drop vapour-diffusion method, 0.5 ml of reservoir solution containing 0.34 ml 0.1 M Tris-maleate/NaOH buffer, pH 5.5, and 0.16 ml 40% w/v PEG 3350 is mixed with 2 ml protein solution containing 11.3 mg/ml enzyme in 10 mM Tris-HCl buffer, pH 7.3, 0.002 ml H2O, 0.0013 ml reservoir solution, 0.002 ml 100 mM 5-fluorouracil, and 0.0003 ml 2-propanol, 21°C, 1-2 weeks, X-ray diffraction structure determination and analysis at 2.2 A resolution, modeling
-
hanging drop vapour-diffusion method, 2.5 A resolution
-
hanging-drop vapour-diffusion method with PEG as precipitant, 2.9 A resolution
-
in complex with 5-fluorouridine, to 2.2 A resolution. The quaternary structure is represented by a hexamer comprised of six identical subunits. The packing of subunits in the hexamer can be described by the symmetry point group L33L2. The main structural and functional unit in the ligand-free state is a homodimer.The hexameric structure is formed by three homodimers with hydrophobic and hydrogen-bond interactions
-
in complex with with the inhibitor 2,2'-anhydrouridine, the substrate phosphate, and with both the inhibitor 2,2'-anhydrouridine and the substrate phosphate, to 2.38, 1.5 and 1.75 A resolution, respectively. The presence of the phosphate ion in the phosphate-binding site substantially changes the orientations of the side chains of the amino-acid residues Arg30, Arg91, and Arg48 coordinated to this ion. The highly flexible loop L9 is unstable
-
free isoform UPa and in complex with thymidine, uracil, thymine or 5-fluorouracil, sitting drop vapor diffusion method, using 100 mM trisodium citrate pH5.6, 16% (w/v) PEG4000 and 17.5% (v/v) isopropanol or 100 mM bis-Tris pH 5.5, 25% (w/v) PEG3350 and 200 mM ammonium sulfate
free enzyme and in complex with uridine, hanging drop vapor diffusion method, using 0.75 M ammonium sulfate, 0.075 M bis-Tris pH 5.5, 0.75% (w/v) PEG 3350, and 25% (v/v) glycerol
-
mutant enzyme C212S, hanging drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M Tris pH 8.5, and 25% (w/v) PEG 3350
-
to a resolution of 1.9 A from crystals of the free form grown on earth, 1.6 A from crystals of the complex with uridine and 0.95 A from crystals of the free form grown under microgravity. All crystals belong to the space group P21 and have similar unit-cell parameters
-
free selenomethionine-labeled enzyme, or enzyme in complex with uridine, X-ray diffraction structure determination and analysis at 2.7 A and 1.44 A resolution, respectively
in complex with 6-methyluracil, hanging drop vapor diffusion method, using 15% (w/v) PEG 4000, 0.1 M MgCl2, 0.1 M Tris-HCl pH 8.5
-
in complex with thymidine, crystals diffrat to 2.1 A resolution, space group P21
-
in silico model of the complex with 5-fluorouracil. The quaternary structure is represented by a hexamer comprised of six identical subunits. The packing of subunits in the hexamer can be described by the symmetry point group L33L2. The hexameric structure of the complex is stabilized by hydrophobic interactions and hydrogen bonds between the amino-acid residues of adjacent homodimers
-
sitting drop vapor diffusion method, using 1 M Tris, 5% (w/v) polyglutamic acid, 20% (w/v) PEG 2000, pH 7.8
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F162A
-
mutation causes a drastic decrease in uridine phosphorylase activity
Y195G
-
mutation causes a drastic decrease in uridine phosphorylase activity
C212S
additional information
C212S
-
the mutation accounts for the lower affinity of the mutant for inorganic phosphate, while the affinity for uridine remains unchanged
C212S
Shewanella oneidensis MR-1 / ATCC 700550
-
the mutation accounts for the lower affinity of the mutant for inorganic phosphate, while the affinity for uridine remains unchanged
-
additional information
-
evolvement of a mutant enzyme UPL8 by iterative saturation mutagenesis. Compared to the wild type enzyme, which has a temperature optimum of 40°C and a half-life of 9.89 h at 60°C, the selected mutant has a temperature optimum of 60°C and a half-life of 17.3 h at 60°C. Self-immobilization of the native enzyme as a Spherezyme shows a 3.3fold increase in thermostability while immobilized mutant enzyme shows a 4.4fold increase in thermostability
additional information
90% suppression of enzyme expression by RNAi does not lead to growth inhibition
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
60
65
-
aglycone substrates, nucleoside substrates, phosphate or pentose 1-phosphate ester substrates stabilize against heat inactivation
75
-
1 h, 3.7% residual activity for wild-type, 80.2% residual activity for mutant UPL8
55
inactivation after 50 min in presence of 2 mM EGTA, 60% of maximal activity remaining after 90 min in presence of Ca2+
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
aglycone substrates, nucleoside substrates, phosphate or pentose 1-phosphate ester substrates stabilize against heat inactivation
-
use of dithiothreitol and glycerol is necessary for stabilization during purification
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE