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EC Number
Amino acid exchange
Commentary
Reference
K213E
decrease in activity against dichlorophenolindophenol
K296A
disturbance of intermolecular salt bridge, mutant retains almost complete activity
K296E
disturbance of intermolecular salt bridge, mutant activity is severely impaired
L71F
reaction is somehow slower than for wild-type, binding of dihydroorotate is much tighter than with wild-type
L71F/C130S/V133T
addition of the two residues comprising the conserved proton-transfer network of Class 2 dihydroorotate dehydrogenase from Escherichia coli to the C130S Class 1A enzyme of Lactococcus lacits. Mutation does not did not restore the function of the active site base or rapid flavin reduction. Kd for dihydroorotate is about three times tighter than the wild-type
L71F/V133T
reaction is drastically slower forwith wild-type, Kd for dihydroorotate is iabout eight-fold tighter than the wild-type
more
deletions of N-terminal residues from 2 down to 40 result in generally unstable proteins with apo protein quickly precipitating and FMN remaining in solution. A truncated protein lacking residues 2 to 30 is sufficiently stable, has near to wild-type activity using molecular oxygen and 20fold lower activity using 2,6-dichlorophenolindophenol as electron acceptor
more
DHOD-knockout Trypanosoma cruzi do not express the enzyme protein and can not survive even in the presence of pyrimidine nucleosides, suggesting a vital role of fumarate reductase activity in the regulation of cellular redox balance
N127A
reduced activity
N193A
drastically reduced activiy
<< < Results 11 - 20 of 31 > >>