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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.38D170A only 50% of the FAD is covalently bound. With vanilly alcohol, eugenol, and 4-(methoxymethyl)phenol the mutant enzyme is more than 1000fold less active than the wild-type enzyme 654161
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.38D170A/T457E produces (S)-1-(4'-hydroxyphenyl)ethanol from 4-ethylphenol. The wild-type enzyme produces (R)-1-(4'-hydroxyphenyl)ethanol 654161
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.38D170E with vanilly alcohol, eugenol, and 4-(methoxymethyl)phenol the mutant enzyme is 5-fold to 100fold less active than the wild-type enzyme 654161
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.38D170N no FAD is covalently bound. With vanilly alcohol, eugenol, and 4-(methoxymethyl)phenol the mutant enzyme is more than 1000fold less active than the wild-type enzyme 654161
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.38D170S with vanilly alcohol, eugenol, and 4-(methoxymethyl)phenol the mutant enzyme is more than 1000fold less active than the wild-type enzyme 654161
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.38D170S/T457E produces (S)-1-(4'-hydroxyphenyl)ethanol from 4-ethylphenol. The wild-type enzyme produces (R)-1-(4'-hydroxyphenyl)ethanol 654161
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.38D170E substrate preference is similar to wild-type enzyme, as the wild-type enzyme the mutant enzyme favors the production of alkenes 655540
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.38D170S most active with branched-chain 4-alkylphenol, mutant enzyme favors the formation of alcohols 655540
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.38H422A mutant enzyme retains activity, turnover rates decrease by 1 order of magnitude. Mutant enzyme is still able to form a stable binary complex of reduced enzyme and a quinone methide product intermediate, a crucial step during vanillyl-alcohol oxidase-mediated catalysis. Although mutation prevents covalent linkage of FAD, mutant enzyme contains tightly bound FAD 655975
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.38H422C mutant enzyme retains activity, turnover rates decrease by 1 order of magnitude. Although mutation prevents covalent linkage of FAD, mutant enzyme contains tightly bound FAD 655975
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