EC Number |
Protein Variants |
Reference |
---|
1.4.1.18 | E168A |
site-directed mutagenesis |
-, 712491 |
1.4.1.18 | E168Q |
site-directed mutagenesis |
-, 712491 |
1.4.1.18 | F173A |
mutation creates an additional large hydrophobic binding pocket in the active site, which favours the binding of aromatic substrates |
763495 |
1.4.1.18 | F173G |
very low level of activity towards the tested substrates |
763495 |
1.4.1.18 | R226K |
site-directed mutagenesis |
-, 712491 |
1.4.1.18 | R242M |
residue R242 appears to be involved in the binding of the alpha-carboxylic group of L-lysine and is located at the entrance of the active site |
763495 |
1.4.1.18 | R242M/F173A |
mutant converts substrates 1-phenylethan-1-one (6%) and 1-phenylpropan-1-one (19%, ee > 99% R) |
763495 |
1.4.1.18 | R242M/F173V |
mutant converts substrates 1-phenylethan-1-one, 1-phenylpropan-1-one 1-phenylbutan-1-one and 2,3-dihydro-4H-1-benzopyran-4-one (38%, 41%, 8%, 15% conversions, ee > 99% R) |
763495 |
1.4.1.18 | V130A/F173A |
mutant exhibits a significant level of activity towards 1-phenylethan-1-one (74% conversion) and 1-phenylpropan-1-one (65% conversion), and all amine products are obtained in enantiomerically pure form (ee > 99% R) |
763495 |
1.4.1.18 | V130A/F173V |
inactive |
763495 |