1.4.1.18 E168A site-directed mutagenesis 1.4.1.18 E168Q site-directed mutagenesis 1.4.1.18 F173A mutation creates an additional large hydrophobic binding pocket in the active site, which favours the binding of aromatic substrates 1.4.1.18 F173G very low level of activity towards the tested substrates 1.4.1.18 R226K site-directed mutagenesis 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 1.4.1.18 R242M/F173A mutant converts substrates 1-phenylethan-1-one (6%) and 1-phenylpropan-1-one (19%, ee > 99% R) 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) 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) 1.4.1.18 V130A/F173V inactive 1.4.1.18 V130G/F173A mutant is stereospecific (ee > 99% R) for the amination of 1-phenylpropan-1-one (78% conversion) and other ketones 1.4.1.18 V130G/F173V inactive 1.4.1.18 V172A/F173A dramatic reduction of catalytic activity 1.4.1.18 V172A/F173G very low level of activity towards the tested substrates 1.4.1.18 V172G/F173A dramatic reduction of catalytic activity 1.4.1.18 V172G/F173G very low level of activity towards the tested substrates 1.4.1.18 Y156F site-directed mutagenesis