EC Number   |
Protein Variants |
Reference |
|---|
    2.4.2.10 | D125N |
active site of enzyme requires D125 of one subunit and K103 of second subunit |
489726 |
| 2.4.2.10 | D131A |
severly reduced activity |
685117 |
| 2.4.2.10 | D131A/D132A |
severly reduced activity |
685117 |
| 2.4.2.10 | D132A |
severly reduced activity |
685117 |
| 2.4.2.10 | G133D |
no enzymic activity |
-, 658308 |
| 2.4.2.10 | G213A |
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 |
673120 |
| 2.4.2.10 | K103A |
active site of enzyme requires D125 of one subunit and K103 of second subunit |
489726 |
| 2.4.2.10 | more |
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 |
748831 |
| 2.4.2.10 | more |
deletion of 1-5 C-terminal amino acids, activities reduced to 22%-75% of wild type activity |
489729 |
| 2.4.2.10 | more |
mutational separation of catalytic activity of enzyme and EC4.1.1.23 activity results in active but unstable proteins |
4187 |
