4.3.1.17	A65G	site-directed mutagenesis of the human liver isozyme cSDH, large structural alterations, serine binding is not affected, overview	691069	
4.3.1.17	A65S	structure of A65S hSDH mutant is determined at 1.3 A resolution. Mutant shows decreased activity (50%) with substrate L-serine compared to wild-type. Mutant shows measurable activity with substrate D-serine	728723	
4.3.1.17	A65S/V225S	double mutant shows only 10% of activity with substrate L-serine compared to wild-type (100%). Double mutant shows very little but measurable activity with substrate D-serine	728723	
4.3.1.17	C183A	135% of wild-type activity. Enzyme retains the positive cooperativity seen in the native enzyme	713970	
4.3.1.17	C221A	70% of wild-type activity. Enzyme retains the positive cooperativity seen in the native enzyme	713970	
4.3.1.17	C226A	100% of wild-type activity. Enzyme retains the positive cooperativity seen in the native enzyme	713970	
4.3.1.17	C303A	site-directed mutagenesis of the human liver isozyme cSDH, structural alterations, overview	691069	
4.3.1.17	C304A	10% of wild-type activity. Mutant displays altered kinetics with a higher Km and a Hill coefficient indicating negative homotropic cooperativity	713970	
4.3.1.17	C309A	site-directed mutagenesis of the cancer cell isozyme cSDH, structural alterations, overview	691069	
4.3.1.17	C343A	inactive, mutants lacks the charge transfer absorbance at 400 nm that is indicative of the 4Fe-4S center	713970