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Results 1 - 10 of 29 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.13A33N site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type 744220
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.13A4E site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows wild-type bioluminesce intensity 744220
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.13A4E/Q11R/A33K/V44I/A54F/P115E/Q124K/Y138I mutant is 29000fold brighter than mutant N166R. Western blot analysis shows that mutant A4E/Q11R/A33K/V44I/A54F/P115E/Q124K/Y138I is produced more efficiently than mutant N166R in cells. The increased expression is consistent with improved enzyme stability at 37°C, where the half-life of activity retention is increased 65fold over that of mutant N166R 727290
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.13A4E/Q11R/A33K/V44I/A54F/P115E/Q124K/Y138I/Q18L/F54I/F68Y/L72Q/M75K/I90V/L27V/K33N/K43R/Y68D mutant Nluc: Nluc paired with furimazine produces 2.5 millionfold brighter luminescence in mammalian cells relative to Oluc-19 with coelenterazine. The luminescence produced by Nluc decays with a half-life more than 2 h, significantly longer than for mutant A4E/Q11R/A33K/V44I/A54F/P115E/Q124K/Y138I. Nluc increased luminescence is gained mostly through improvements in protein stability, where Nluc shows markedly greater retention of activity in lysates following incubation at 37°C 727290
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.13A4E/Q11R/Q18L/L27V/A33N/K43R/V44I/A54I/F68D/L72Q/M75K/I90V/P115E/Q124K/Y138I/N166R construction of mutant nanoKAZ, a mutant with 16 amino acid substitutions of the catalytic subunit, by site-directed mutagenesis, the mutant nanoKAZ lacks the amino-terminal signal peptide, crystal structure determination and analysis, structure-function relationship in nanoKAZ, overview. The truncation of 10 amino acid residues at N- and C-terminal regions of nanoKAZ causes a complete loss of luminescence activity. Both the alpha1-helix and beta11-strand in the nanoKAZ molecule might serve to stabilize the molecule, which is essential in catalyzing the luminescence reaction 744231
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.13A54I site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type 744220
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.13A54I/Y138I site-directed mutagenesis, mutation of the catalytic subunit, the mutant shows increased bioluminesce intensity compared to the wild-type 744220
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.13C164A mutation does not significantly affect catalytic activity of subunit kOLase 689868
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.13C164G mutation does not significantly affect catalytic activity of subunit kOLase 689868
Display the word mapDisplay the reaction diagram Show all sequences 1.13.12.13C164S mutation does not significantly affect catalytic activity of subunit kOLase 689868
Results 1 - 10 of 29 > >>