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Results 1 - 10 of 13 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.11F94L single point mutant with improved enzymatic activity 764603
Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.11H312A the activity of the mutant enzyme toward L-glutamate is significantly reduced, however it exhibits catalytic activity toward various L-amino acids 724186
Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.11H533R single point mutant with improved enzymatic activity 764603
Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.11I282M single point mutant with improved enzymatic activity 764603
Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.11more construction of a highly sensitive and selective glutamate microbiosensor based on polypyrrole, multiwalled carbon nanotubes, and glutamate oxidase deposited on the transducer platinum electrode, i.e. Pt/PPy/MWCNT/GluOx electrodes, overview. The biosensor has a high sensitivity, low response to interferences such as ascorbic acid, uric acid and acetaminophen, a fast response time, low detection limit, a linear range of 0.14 mM, and a satisfactory stability, mass transfer-limiting outer membrane of polyurethane, optimization, overview 711530
Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.11R305A the activity of the mutant enzyme toward L-glutamate is significantly reduced, however it exhibits catalytic activity toward various L-amino acids (best substrate is L-histidine) 724186
Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.11R305D the activity of the mutant enzyme toward L-glutamate is significantly reduced, however it exhibits catalytic activity toward various L-amino acids (best substrate is L-arginine) 724186
Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.11R305E wild-type enzyme shows strict substrate specificity for L-glutamate. The mutant variant of L-glutamate oxidase exhibits strict specificity for L-arginine. R305E is a thermostable and pH stable enzyme 765731
Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.11R305K the activity of the mutant enzyme toward L-glutamate is significantly reduced, however it exhibits catalytic activity toward various L-amino acids (best substrate is L-histidine) 724186
Display the word mapDisplay the reaction diagram Show all sequences 1.4.3.11R305L the activity of the mutant enzyme toward L-glutamate is significantly reduced, however it exhibits catalytic activity toward various L-amino acids (best substrate is L-histidine) 724186
Results 1 - 10 of 13 > >>