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Results 1 - 10 of 13 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 1.5.8.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.2C-terminal truncations C-terminal truncations of 5, 10 or 17 residues do not affect dimer stability, but compromise the ability of the enzyme to become covalently coupled with FMN in the active site -, 393892
Show all pathways known for 1.5.8.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.2C30A binds FMN non-covalently -, 393888, 393897
Show all pathways known for 1.5.8.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.2C30A mutant shows highly increased activity to oxidate of the cofactor FMN to 6-hydroxyFMN compared to the wild-type enzyme 654971
Show all pathways known for 1.5.8.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.2C30A removal of the 6-S-cysteinyl-FMN bond, diminishes limiting rate for the first of three observed kinetic phases -, 393886
Show all pathways known for 1.5.8.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.2H172Q no change of turnover, but 25fold increase of Km-value -, 393893
Show all pathways known for 1.5.8.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.2V344I increase of Km-value, decrease of turnover -, 393895
Show all pathways known for 1.5.8.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.2Y442F - -, 393898
Show all pathways known for 1.5.8.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.2Y442F 1.4fold reduction of electron transfer -, 393891
Show all pathways known for 1.5.8.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.2Y442G - -, 393895, 393898
Show all pathways known for 1.5.8.2Display the word mapDisplay the reaction diagram Show all sequences 1.5.8.2Y442G 30.5fold reduction of electron transfer -, 393891
Results 1 - 10 of 13 > >>