EC Number   |
Protein Variants |
Reference  |
|---|
    1.5.1.5 | R653Q |
mutant enzyme has normal substrate affinity but a 36% reduction in half-life at 42°C |
698187 |
| 1.5.1.5 | more |
successful double replacement of the DHCH1 gene is a result of double electroporation with two replacement fragments but an intact gene copy is retained (probably aneuploidy), additional metabolic complementation to bypass the requirement for DHCH1 is not successful either, ectopic addition of DHCH1 or formate-tetrahydrofolate ligase before the second replacement step finally results in a null mutant without chromosomal DHCH1 gene (dhch1-/pXNG4-DHCH1 or dhch1-/pXNG4-FTL) or addition to wild-type in overexpressing transfectants (WT/pXNG4-DHCH1 or WT/pXNG4-FTL) |
700281 |
| 1.5.1.5 | D133E |
mutant retains no dehydrogenase activity |
701402 |
| 1.5.1.5 | D133E |
no dehydrogenase activity retained, Mg2+ binding site |
701402 |
| 1.5.1.5 | K56Q/Q100K |
retaines two-third of dehydrogenase activity but no cyclohydrolase activity |
701402 |
| 1.5.1.5 | K56Q/Q100K |
site-directed mutagenesis shows that the double mutant has no cyclohydrolase activity but retains two-thirds of the normal dehydrogenase activity |
701402 |
| 1.5.1.5 | more |
asparagine-125 is required for folate-substrate binding, arginine-173 mutation causes 500fold increase in the Km for NADP, serine-197 mutation a 20fold increase |
701402 |
| 1.5.1.5 | more |
knockout mutant of MTHFD2 is embryonic lethal in mice at about 12 days gestation, no normal development of hematogenesis in the liver |
701402 |
| 1.5.1.5 | more |
mutation of arginine-166 leads to complete loss of dehydrogenase activity, is critically responsible for binding of the inorganic phosphate, with arginine-198 mutation some dehydrogenase activity is retained, it probably only assists in phosphate binding |
701402 |
| 1.5.1.5 | C58Y |
kcat/Km for 5,10-methenyltetrahydrofolate is 8.4fold lower than wild-type value |
744335 |
