EC Number |
Protein Variants |
Reference |
---|
2.4.1.87 | D102A |
inactive |
721667 |
2.4.1.87 | D104A |
inactive |
721667 |
2.4.1.87 | D116A |
the mutant remains active |
721667 |
2.4.1.87 | D118A |
the mutant remains active |
721667 |
2.4.1.87 | D28A |
the mutant remains active |
721667 |
2.4.1.87 | D30A |
the mutant remains active |
721667 |
2.4.1.87 | D316E |
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 |
2.4.1.87 | D316E |
site-directed mutagenesis, a catalytic domain mutant, crystal structure determination with bound UDP-Gal and Mn2+ |
690994 |
2.4.1.87 | D316N |
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 |
2.4.1.87 | D316N |
site-directed mutagenesis, a catalytic domain mutant, crystal structure determination with bound UDP-Gal and Mn2+ |
690994 |