2.4.2.3: uridine phosphorylase
This is an abbreviated version!
For detailed information about uridine phosphorylase, go to the full flat file.
Word Map on EC 2.4.2.3
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2.4.2.3
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pyrimidine
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nucleoside
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thymidine
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uracil
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5-fluorouracil
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phosphorolysis
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salvage
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orotate
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phosphoribosyltransferase
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phosphorylases
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thymidylate
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fluoropyrimidine
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udp
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5'-deoxy-5-fluorouridine
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5-fluoro-2'-deoxyuridine
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dihydropyrimidine
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acyclonucleoside
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5-fluorouridine
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ribose-1-phosphate
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capecitabine
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5-methyluridine
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dthdpase
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fdurd
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orotidine
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dihydrouracil
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uridine-cytidine
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mete
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diagnostics
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medicine
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synthesis
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drug development
- 2.4.2.3
- pyrimidine
- nucleoside
- thymidine
- uracil
- 5-fluorouracil
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phosphorolysis
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salvage
- orotate
-
phosphoribosyltransferase
- phosphorylases
- thymidylate
-
fluoropyrimidine
- udp
- 5'-deoxy-5-fluorouridine
- 5-fluoro-2'-deoxyuridine
- dihydropyrimidine
- acyclonucleoside
- 5-fluorouridine
- ribose-1-phosphate
- capecitabine
- 5-methyluridine
- dthdpase
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fdurd
- orotidine
- dihydrouracil
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uridine-cytidine
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mete
- diagnostics
- medicine
- synthesis
- drug development
Reaction
Synonyms
apUP, EC 2.4.2.23, L-UrdPase, More, PcUP1, PcUP2, phosphorylase, uridine, pynpase, pyrimidine nucleoside phosphorylase, pyrimidine phosphorylase, pyrimidine/purine nucleoside phosphorylase, StUPh, udp, UDRPase
ECTree
2.4.2.3 uridine phosphorylaseAdvanced search results
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results (Engineering
Engineering on EC 2.4.2.3 - uridine phosphorylase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F162A
mutation causes a drastic decrease in uridine phosphorylase activity
T94A
mutation causes a drastic decrease in uridine phosphorylase activity
Y195G
mutation causes a drastic decrease in uridine phosphorylase activity
E237K
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
E248K
site-directed mutagenesis, almost inactive mutant enzyme
F202A
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
F211A
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
H19D
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
H32D
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
Q206L
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
Q215L
site-directed mutagenesis, the mutant enzyme shows highly reduced activity compared to the wild-type enzyme
R104E
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
R137E
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
R208D
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
R264E
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
R273E
site-directed mutagenesis, the mutant enzyme shows highly reduced activity compared to the wild-type enzyme
R39E
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
R59E
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
R63E
site-directed mutagenesis, the mutant enzyme shows highly reduced activity compared to the wild-type enzyme
R93E
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
T107A
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
T140A
site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
F211A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
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Q206L
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
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Q215L
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site-directed mutagenesis, the mutant enzyme shows highly reduced activity compared to the wild-type enzyme
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R264E
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
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R39E
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
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R59E
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
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R63E
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site-directed mutagenesis, the mutant enzyme shows highly reduced activity compared to the wild-type enzyme
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R93E
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
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T107A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
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T140A
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site-directed mutagenesis, the mutant enzyme shows reduced activity compared to the wild-type enzyme
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C212S
L211Q/C206S
site-directed mutagenesis, the double mutant is characterized not only by lower values of KM for phosphate with a slight increase in KM for uridine but also by the increased specific activity compared to the wild-type enzyme
T91A
site-directed mutagenesis, the replacement is nonsynonymous and leads to significant replacement of the side radical
C212S
Shewanella oneidensis MR-1 / ATCC 700550
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the mutation accounts for the lower affinity of the mutant for inorganic phosphate, while the affinity for uridine remains unchanged
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additional information
C212S
the mutation accounts for the lower affinity of the mutant for inorganic phosphate, while the affinity for uridine remains unchanged
C212S
site-directed mutagenesis, the replacement has no significant effect on the loop (217-227 ARs)
additional information
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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
additional information
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90% suppression of enzyme expression by RNAi does not lead to growth inhibition
additional information
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Thr93 is the residue, the modification of which will allow VchUPh to catalyze the biotechnologically important synthesis of 6-methyluridine from 6-methyluracil
