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Results 1 - 10 of 27 > >>
EC Number
Amino acid exchange
Commentary
Reference
A86H
in wild-type enzyme FAD is non-covalenly-bound. In the enzyme containing a mutant A86H flavoprotein subunit the FAD is covalently bound
C247
mutation in flavoprotein subunit FrdA. Increase in fumarate reduction rate, slight increase in succinate oxidation. Residue C247 of FrdA is responsible for the N-ethylmaleimide sensitivity shown by fumarate reductase but is not required for catalytic activity or the tight-binding of oxalacetate
E180Q
site-diirected mutagenesis, the mutant catalyzes the electron transfer from succinate to methylene blue, but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate
E29F
mutation in subunit FrdC, dramatic decrease in enzymatic reactions with menaqunione. Elimination of the negative charge in E29 mutant enzymes results in significantly increased stabilization of both ubiquinone and menaquinone semiquinones
E29L
mutation in subunit FrdC, alters hydrogen bonding to menaquinone
E29L
mutation in subunit FrdC, dramatic decrease in enzymatic reactions with menaqunione. Elimination of the negative charge in E29 mutant enzymes results in significantly increased stabilization of both ubiquinone and menaquinone semiquinones
E49A
decrease in catalytic efficiency of both fumarate reduction and succinate oxidation
E49Q
decrease in catalytic efficiency of both fumarate reduction and succinate oxidation
E66Q
site-diirected mutagenesis, the mutant catalyzes the electron transfer from succinate to methylene blue, but not from 2,3-dimethyl-1,4-naphthoquinol to fumarate
H232S
mutation in flavoprotein subunit FrdA. Decrease in fumarate reduction, strong decrease in succinate oxidation. Residue H232 is the general acid-base catalyst
Results 1 - 10 of 27 > >>