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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6A184C/A301C/T394C kcat/KM is comparable to wild-type value 762731
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6A184C/T239C/A407C/A465C kcat/KM is 1.1fold lower than wild-type value 762731
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6A32C/S129C/T371C/A423C kcat/KM is 2.55fold lower than wild-type value 762731
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6A32C/T168C/S312C/A465C kcat/KM is 2.1fold lower than wild-type value 762731
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6E311D mutations of Glu311 cause a switch in the basic kinetic mechanism of the reaction of reduced cholesterol oxidase with dioxygen: wild-type cholesterol oxidase shows a saturation behavior with increasing oxygen concentration, while for Glu311 mutants a linear dependence is found that is assumed to reflect a simple second order process 687754
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6E311L mutations of Glu311 cause a switch in the basic kinetic mechanism of the reaction of reduced cholesterol oxidase with dioxygen: wild-type cholesterol oxidase shows a saturation behavior with increasing oxygen concentration, while for Glu311 mutants a linear dependence is found that is assumed to reflect a simple second order process 687754
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6E311Q mutations of Glu311 cause a switch in the basic kinetic mechanism of the reaction of reduced cholesterol oxidase with dioxygen: wild-type cholesterol oxidase shows a saturation behavior with increasing oxygen concentration, while for Glu311 mutants a linear dependence is found that is assumed to reflect a simple second order process 687754
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6E361A site-directed mutagenesis, the mutant shows no dehydrogenase activity 725743
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6E361Q H447Q mutant shows wild-type activity in isomerization, kcat for oxidation reaction is reduced 120fold, Km increases 2fold compared to wild-type, E361Q mutant has no isomerization activity, kcat is 30fold slower than for wild-type, Glu361 may therefore act as general base in oxidation reaction 287672
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.6E361Q turnover number for cholesterol is decreased 31.4fold compared to wild-type enzyme, 1.8fold increase in Km-value for cholesterol compared to wild-type enzyme 654343
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