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Results 1 - 10 of 21 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 1.8.2.1Display the word mapDisplay the reaction diagram Show all sequences 1.8.2.1C185A the active site of the mutant is essentially catalytically inactive with ferricyctochrome c or ferricyanide as electron acceptor 711242
Show all pathways known for 1.8.2.1Display the word mapDisplay the reaction diagram Show all sequences 1.8.2.1C185S the active site of the mutant is essentially catalytically inactive with ferricyctochrome c or ferricyanide as electron acceptor 711242
Show all pathways known for 1.8.2.1Display the word mapDisplay the reaction diagram Show all sequences 1.8.2.1G473A mutant is able to dimerize and has steady-state activity comparable to that of the wild type, stopped-flow analysis of the reductive half-reaction of this variant yields a rate constant nearly 3 times higher than that of the wild type 667714
Show all pathways known for 1.8.2.1Display the word mapDisplay the reaction diagram Show all sequences 1.8.2.1G473D monomer, mutant is severely impaired both in the ability to bind sulfite and in catalysis, with a second-order rate constant 5 orders of magnitude lower than that of the wild type, significant random-coil formation 667714
Show all pathways known for 1.8.2.1Display the word mapDisplay the reaction diagram Show all sequences 1.8.2.1G473W monomer, mutant with 5fold higher activity than G473D and nearly wild-type activity at pH 7.0 when ferricyanide is the electron acceptor, significant random-coil formation 667714
Show all pathways known for 1.8.2.1Display the word mapDisplay the reaction diagram Show all sequences 1.8.2.1H57A heme potential is lowered from ca. 240 mV in wild-type to ca. 200 mV, the molybdenum redox potential is not affected. The catalytic potential is pH-independent 724418
Show all pathways known for 1.8.2.1Display the word mapDisplay the reaction diagram Show all sequences 1.8.2.1H57A mutant with reduced activity, Tyr-236 and His-57 are necessary to stabilize Arg-55 in a position for optimal hydrogen bonding to the heme 6-propionate 722663
Show all pathways known for 1.8.2.1Display the word mapDisplay the reaction diagram Show all sequences 1.8.2.1P105A the mutant enzyme shows increased catalytic efficiency compared to the wild type enzyme 711223
Show all pathways known for 1.8.2.1Display the word mapDisplay the reaction diagram Show all sequences 1.8.2.1P105A/P111A the mutant enzyme shows about 30% decreased catalytic efficiency compared to the wild type enzyme 711223
Show all pathways known for 1.8.2.1Display the word mapDisplay the reaction diagram Show all sequences 1.8.2.1P111A the mutant enzyme shows about 30% decreased catalytic efficiency compared to the wild type enzyme 711223
Results 1 - 10 of 21 > >>