3.1.1.78	C132A	755% lower activity than wild-type	638948	
3.1.1.78	C170A	80% lower activity than wild-type	638948	
3.1.1.78	C213S/G152Q	35% lower activity than wild-type	638948	
3.1.1.78	C257A	35% lower activity than wild-type	638948	
3.1.1.78	H17A	97% lower activity than wild-type	638948	
3.1.1.78	H244A	mutant shows extremely reduced hydrolase activity. Crystal structure of His244Ala in complex with the enzyme product: the indolic part in the molecule interacts with Met113, Phe125, Tyr128, and Lys187. This arrangement enables the alkaloid to be fixed by hydrophobic, sandwichlike interactions providing optimal structural accommodation for catalysis	701693	
3.1.1.78	H86A	mutant shows extremely reduced hydrolase activity. Like Met245, His86 is far from the water molecules in the active center. It might therefore be of structural rather than of catalytic significance	701693	
3.1.1.78	M245A	mutant shows extremely reduced hydrolase activity. Met245 is far from the water molecules in the active center and as the neighbor residue of the catalytic His244, it might therefore be of structural rather than of catalytic significance	701693