6.4.1.3	A431C	kcat (propionyl-CoA) decreased compared to wild-type, Km (propionyl-CoA) increased compared to wild-type. kcat (acetyl-CoA) increased compared to wild-type, Km (propionyl-CoA) similar to wild-type	726557	
6.4.1.3	A431D	mutant enzyme shows no activity	726557	
6.4.1.3	A431I	kcat (propionyl-CoA) decreased compared to wild-type, Km (propionyl-CoA) increased compared to wild-type. kcat (acetyl-CoA) increased compared to wild-type, Km (propionyl-CoA) similar to wild-type	726557	
6.4.1.3	A431L	mutant enzyme shows no activity	726557	
6.4.1.3	A487V	no effect on activity	652691	
6.4.1.3	A497V	beta subunit, no effect on subunit interactions and activity	653247	
6.4.1.3	A497V	polymorphism, 30% higher specific activity than wild-type enzyme	662392	
6.4.1.3	A497V	significantly increased activity	651459	
6.4.1.3	A513_R514insP	insertion between residues 513 and 514 of the beta subunit, leads to partial degradation of the subunit, strongly reduced activity	653246	
6.4.1.3	A513_R514insP	insertion, severe degradation of the subunit	651459