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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.87D102A inactive 721667
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.87D104A inactive 721667
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.87D116A the mutant remains active 721667
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.87D118A the mutant remains active 721667
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.87D28A the mutant remains active 721667
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.87D30A the mutant remains active 721667
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.87D316E mutant show modest reduction in kcat and Km for lactose. Strucutural studies with mutant D316E show that the negative charge is crucial for catalytic activity and needed for its interaction with Arg202 for an active site structure that facilitates the binding of UDP-gal in a catalytically competent conformation 690994
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.87D316E site-directed mutagenesis, a catalytic domain mutant, crystal structure determination with bound UDP-Gal and Mn2+ 690994
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.87D316N mutant is inactive. Strucutural studies with mutant D316N show that the negative charge is crucial for catalytic activity and needed for its interaction with Arg202 for an active site structure that facilitates the binding of UDP-gal in a catalytically competent conformation 690994
Display the word mapDisplay the reaction diagram Show all sequences 2.4.1.87D316N site-directed mutagenesis, a catalytic domain mutant, crystal structure determination with bound UDP-Gal and Mn2+ 690994
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