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Results 1 - 10 of 62 > >>
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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.17A21V site-directed mutagenesis in the FAD binding site -, 724047
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.17A21V/G62D site-directed mutagenesis, the mutant shows 1.93fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and slightly reduced activity with choline compared to the wild-type enzyme 724047
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.17A21V/G62D/I69V site-directed mutagenesis, the mutant shows 1.68fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme 724047
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.17A21V/G62D/I69V/S348L site-directed mutagenesis, the mutant shows 3.45fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and highly reduced activity with choline compared to the wild-type enzyme 724047
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.17A21V/G62D/S348C site-directed mutagenesis, the mutant shows 5.18fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and reduced activity with choline compared to the wild-type enzyme 724047
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.17A21V/G62D/S348L site-directed mutagenesis, the mutant shows 3.72fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and highly reduced activity with choline compared to the wild-type enzyme 724047
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.17A21V/G62D/S348L/V349L site-directed mutagenesis, the mutant shows 5.75fold increased activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate and highly reduced activity with choline compared to the wild-type enzyme 724047
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.17A21V/K394R site-directed mutagenesis, the mutant shows 85% activity with tris-(2-hydroxyethyl)-methylammonium methylsulfate compared to the wild-type enzyme 724047
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.17E312A generated for investigation of the negative charge on Glu312, enzyme inactive 685213
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.17E312D generated for investigation of the negative charge on Glu312, kcat values about 230times lower and and kcat/Km values about 35times lower than in the wild-type, solvent viscosity and substrate kinetic isotope effects indicates presence of internal equilibrium prior to the hydride transfer reaction 685213
Results 1 - 10 of 62 > >>
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