EC Number   |
Protein Variants |
Reference |
|---|
    1.1.1.205 | A251T |
is 4fold less sensitive to mycophenolic acid but 40fold more sensitve to mizoribine monophosphate. Mutation does not affect kcat but decreases Km values for both substrates, is catalytically more efficient. Mutation renders the enzyme resistant to NAD+ substrate inhibition, stabilizes the closed conformation, which has opposing effects on enzyme susceptiblities to mycophenolic acid and mizoribine monophosphate |
701583 |
| 1.1.1.205 | A251T |
the mutation affects the enzyme structure so that the mutant shows altered sensitivity to inhibitors compared to the wild-type enzyme |
-, 669310 |
| 1.1.1.205 | A267S |
the mutant enzyme is inhibited by mycophenolic acid |
762347 |
| 1.1.1.205 | A285T |
site-directed mutagenesis of IMPDH1, similar activity and protein stability compared to the wild-type enzyme |
667508 |
| 1.1.1.205 | A462T |
increase in the Ki for mycophenolic acid |
347953 |
| 1.1.1.205 | C305A |
the guaBDELTACBS phenotype can be complemented in trans by a mutant guaB allele, which encodes the catalytically disabled IMPDHC305A protein containing an intact Bateman domain |
704629 |
| 1.1.1.205 | C319S |
is essentially inactive, two-step binding process for inosine 5'-phosphate remains |
701583 |
| 1.1.1.205 | C331A |
mutated type 2 isozyme in the inosine 5'-phosphate binding site, which results in less than 0.1% activity |
701583 |
| 1.1.1.205 | D13A |
is activated by Mg2+ and Ca2+ in lieu of K+ |
701583 |
| 1.1.1.205 | D199N |
site-directed mutagenesis, mutant structure analysis |
739794 |
