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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.4A170V/Q353L random mutagenesis, the mutant shows 3.5fold increased thermostabilty at 50°C compared to the wild-type enzyme 689922
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.4D144A site-directed mutagenesis 737204
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.4D144E site-directed mutagenesis 737204
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.4D144I site-directed mutagenesis 737204
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.4D394A 23.5% of the wild-type activity, according to the initial rate of sucrose consumption, very poor ativation by glycogen 659439
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.4D507A site-directed mutagenesis 737204
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.4D507I site-directed mutagenesis 737204
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.4E227G mutant enzyme is a highly efficient polymerase that produces a longer polymer than the wild-type enzyme. Decreased stability and the temperature optimum compared to wild-type enzyme 673575
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.4E328Q inactive mutant 720052
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.4E328Q inactive mutant, sucrose binding structure analysis using the crystal structure, PDB ID 1JGI 737204
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