2.4.2.10: orotate phosphoribosyltransferase
This is an abbreviated version!
For detailed information about orotate phosphoribosyltransferase, go to the full flat file.
Word Map on EC 2.4.2.10
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2.4.2.10
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pyrimidine
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5-fluorouracil
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thymidylate
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dihydropyrimidine
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uridine
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thymidine
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uracil
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colorectal
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dihydroorotase
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pyre
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fluoropyrimidine
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4.1.1.23
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orotidine-5'-monophosphate
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5-fluoroorotic
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transcarbamoylase
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5-fu-based
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leucovorin
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phosphoribosylpyrophosphate
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5-fluorouracil-based
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5-fu-related
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prototrophy
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tegafur
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odcase
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dihydrouracil
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succinate-grown
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5-phosphoribosyl
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fdump
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5-fu-resistant
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podospora
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phosphoribosyltransferases
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5-fluoro-2'-deoxyuridine
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fluoropyrimidine-based
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ompdc
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5-phosphoribosyl-1-pyrophosphate
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anserina
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1-pyrophosphate
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5-fluorouridine
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pyrophosphorolysis
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medicine
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diagnostics
- 2.4.2.10
- pyrimidine
- 5-fluorouracil
- thymidylate
- dihydropyrimidine
- uridine
- thymidine
- uracil
- colorectal
- dihydroorotase
-
pyre
-
fluoropyrimidine
-
4.1.1.23
- orotidine-5'-monophosphate
-
5-fluoroorotic
-
transcarbamoylase
-
5-fu-based
- leucovorin
-
phosphoribosylpyrophosphate
-
5-fluorouracil-based
-
5-fu-related
-
prototrophy
-
tegafur
- odcase
- dihydrouracil
-
succinate-grown
-
5-phosphoribosyl
- fdump
-
5-fu-resistant
- podospora
-
phosphoribosyltransferases
- 5-fluoro-2'-deoxyuridine
-
fluoropyrimidine-based
- ompdc
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5-phosphoribosyl-1-pyrophosphate
- anserina
- 1-pyrophosphate
- 5-fluorouridine
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pyrophosphorolysis
- medicine
- diagnostics
Reaction
Synonyms
More, OMP synthase, OPRT, OPRTase, orotate phosphoribosyl pyrophosphate transferase, orotate phosphoribosyl transferase, orotate phosphoribosyltransferase, orotate PRTase, orotic acid phosphoribosyltransferase, orotidine 5'-monophosphate pyrophosphorylase, orotidine 5'-phosphate pyrophosphorylase, orotidine monophosphate pyrophosphorylase, orotidine phosphoribosyltransferase, orotidine-5'-phosphate pyrophosphorylase, orotidylate phosphoribosyltransferase, orotidylate pyrophosphorylase, orotidylic acid phosphorylase, orotidylic acid pyrophosphorylase, orotidylic phosphorylase, orotidylic pyrophosphorylase, phosphoribosyltransferase, orotate, Pyr5, PyrE, rv0382c, type I phosphoribosyltransferase, ura5
ECTree
2.4.2.10 orotate phosphoribosyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.4.2.10 - orotate phosphoribosyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G213A
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OPRT, the gene polymorphism predicts toxicity in patients treated with bolus 5-fluorouracil regimen, the Ala allele in the enzyme G213A polymorphism and the two tandem repeats in the TYMS promoter polymorphism are associated with grade 3 to 4 neutropenia and diarrhea, distribution in 69 patients samples, genotyping, relationship between OPRT mRNA expression and the OPRT G213A polymorphism, overview
G133D
D125N
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active site of enzyme requires D125 of one subunit and K103 of second subunit
K103A
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active site of enzyme requires D125 of one subunit and K103 of second subunit
additional information
additional information
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mutational separation of catalytic activity of enzyme and EC4.1.1.23 activity results in active but unstable proteins
additional information
construction of a chimeric fusion enzyme from the last two enzymes in the pyrimidine biosynthetic pathway in the inversed order by having a C-terminal orotate phosphoribosyltransferase (OPRT) and an N-terminal orotidine 5'-monophosphate decarboxylase (OMPDC) as OMPDC-OPRT in Plasmodium falciparum, the chimeric mutant acts as a bifunctional enzyme. The activitiy, although unstable, is stabilized by the substrate and product during purification and long-term storage. The kcat is selectively enhanced up to three orders of magnitude, while the Km is not much affected and remains at low micromolar levels when compared to the monofunctional enzymes. The fusion of the two enzymes creates a super-enzyme with perfect catalytic power and more flexibility
additional information
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construction of a chimeric fusion enzyme from the last two enzymes in the pyrimidine biosynthetic pathway in the inversed order by having a C-terminal orotate phosphoribosyltransferase (OPRT) and an N-terminal orotidine 5'-monophosphate decarboxylase (OMPDC) as OMPDC-OPRT in Plasmodium falciparum, the chimeric mutant acts as a bifunctional enzyme. The activitiy, although unstable, is stabilized by the substrate and product during purification and long-term storage. The kcat is selectively enhanced up to three orders of magnitude, while the Km is not much affected and remains at low micromolar levels when compared to the monofunctional enzymes. The fusion of the two enzymes creates a super-enzyme with perfect catalytic power and more flexibility
additional information
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point mutations for negative complementation of enzyme activity
additional information
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deletion of 1-5 C-terminal amino acids, activities reduced to 22%-75% of wild type activity
