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	
4.3.1.17	C385A	inactive, mutants lacks the charge transfer absorbance at 400 nm that is indicative of the 4Fe-4S center	713970	
4.3.1.17	C396A	inactive, mutants lacks the charge transfer absorbance at 400 nm that is indicative of the 4Fe-4S center	713970	
4.3.1.17	C458A	44% of wild-type activity. Enzyme retains the positive cooperativity seen in the native enzyme	713970	
4.3.1.17	C458A	kcat/Km for L-serine is 2.2fold lower than the wild-type value	746916	
4.3.1.17	cSDH-hSDH	chimeric protein	678411	
4.3.1.17	DELTA(C458)	mutant enzyme has no detectable activity	746916	
4.3.1.17	DELTA(P456,E457,C458)	mutant enzyme has no detectable activity	746916	
4.3.1.17	DELTAP128	hSDH	678411	
4.3.1.17	E445A	mutant enzyme has no detectable activity	746916	
4.3.1.17	E457A	kcat/Km for L-serine is 1.5fold lower than the wild-type value	746916	
4.3.1.17	G72A	site-directed mutagenesis of the cancer cell isozyme cSDH, large structural alterations, serine binding is not affected, changing alanine to glycine at residue 72 in cSDH is responsible for the reduced catalytic activity of cSDH, overview	691069	
4.3.1.17	G72A/S228A	site-directed mutagenesis of the cancer cell isozyme cSDH, catalytic activities for both the substrates are substantially recovered, overview	691069	
4.3.1.17	H124A/N126A	kcat/Km for L-serine is 48.5fold lower than the wild-type value	746916	
4.3.1.17	H152S	ratio of elimination reaction to racemization is 1.4 compared to 3.7 in wild-type	662359	
4.3.1.17	H19A	kcat/Km for L-serine is 127fold lower than the wild-type value	746916	
4.3.1.17	H61A	mutant enzyme has no detectable activity	746916	
4.3.1.17	H61N	mutant enzyme has no detectable activity	746916	
4.3.1.17	H61S	mutant enzyme has no detectable activity	746916	
4.3.1.17	InsP128	cSDH, cSDH lacks a Pro residue corresponding to Pro128 in hSDH	678411	
4.3.1.17	K444A	mutant enzyme has no detectable activity	746916	
4.3.1.17	L287V	cSDH	678411	
4.3.1.17	additional information	construction of a mutant strain devoid of functional genes sdaA, sdaB, tdcG encoding the three isozymes of the organism, the loss of the ability to deaminate L-serine severely impairs growth and cell division in Escherichia coli K-12 leading e.g. to filamentation, phenotype, overview	694235	
4.3.1.17	N154F	ratio of elimination reaction to racemization is 0.33 compared to 3.7 in wild-type	662359	
4.3.1.17	P153S	ratio of elimination reaction to racemization is 0.24 compared to 3.7 in wild-type	662359	
4.3.1.17	Q155D	ratio of elimination reaction to racemization is 0.25 compared to 3.7 in wild-type	662359	
4.3.1.17	S16A	mutant enzyme has no detectable activity	746916	
4.3.1.17	S17A	kcat/Km for L-serine is 4.8fold lower than the wild-type value	746916	
4.3.1.17	S18A	mutant enzyme has no detectable activity	746916	
4.3.1.17	S53A	kcat/Km for L-serine is 2.9fold lower than the wild-type value	746916	
4.3.1.17	T20A	kcat/Km for L-serine is 4.2fold lower than the wild-type value	746916	
4.3.1.17	T290A	kcat/Km for L-serine is 127fold lower than the wild-type value	746916	
4.3.1.17	T446A	kcat/Km for L-serine is 91.7fold lower than the wild-type value	746916	
4.3.1.17	T57A	kcat/Km for L-serine is 31.7fold lower than the wild-type value	746916