1.2.7.11	C12/15A	loss of iron–sulfur cluster	724470	
1.2.7.11	C12A	loss of iron–sulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA	724470	
1.2.7.11	C15A	loss of iron–sulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA	724470	
1.2.7.11	C197A	the enzyme retains an unidentified type of iron–sulfur cluster	724470	
1.2.7.11	C46A	loss of iron–sulfur cluster. The mutant enzyme does not show formation of any radical intermediate or production of acetyl-CoA	724470	
1.2.7.11	D468A	inactive with 2-oxoglutarate and pyruvate as substrate	-, 739701	
1.2.7.11	D468A	mutant enzyme StOFOR1 with mutation D468A in alpha-subunit. Vmax with pyruvate as substrate is 1.3% compared to wild-type enzyme. No activity is detected with 2-oxoglutarate	-, 739701	
1.2.7.11	I255L	kcat/Km for pyruvate is 11% of wild-type value, kcat/KM for 2-oxoglutarate is 21% of wild-type value	719399	
1.2.7.11	I255M	kcat/Km for pyruvate is 13% of wild-type value, kcat/KM for 2-oxoglutarate is 2% of wild-type value	719399	
1.2.7.11	I255S	kcat/Km for pyruvate is 23% of wild-type value, kcat/KM for 2-oxoglutarate is 35% of wild-type value	719399	
1.2.7.11	I255V	kcat/Km for pyruvate is 14% of wild-type value, kcat/KM for 2-oxoglutarate is 38% of wild-type value	719399	
1.2.7.11	K125A	the mutant enzyme shows a large increase in the Km-value for CoA and shows poor inactivation by 4-fluoro-7-nitrobenzofurazan, compared with K173A and wild type enzyme	718962	
1.2.7.11	K173A	the mutant enzyme shows a large increase in the Km-value for CoA and shows poor inactivation by 4-fluoro-7-nitrobenzofurazan, compared with K173A and wild type enzyme	718962	
1.2.7.11	K49I	inactive with 2-oxoglutarate as substrate	-, 739701	
1.2.7.11	K49I	mutant enzyme StOFOR1 with mutation K49I in alpha-subunit. Vmax with pyruvate as substrate is 28% compared to wild-type enzyme, Km with pyruvate as substrate is 2.8fold higher as compared to wild-type enzyme. No activity is detected with 2-oxoglutarate	-, 739701	
1.2.7.11	P254G	kcat/Km for pyruvate is 12% of wild-type value, kcat/KM for 2-oxoglutarate is 20% of wild-type value	719399	
1.2.7.11	P257A	no enzyme activity at either 50 or 80°C	719399	
1.2.7.11	P257G	no enzyme activity at either 50 or 80°C	719399	
1.2.7.11	P257V	no enzyme activity at either 50 or 80°C	719399	
1.2.7.11	S41A	mutant enzyme StOFOR1 with mutation S41A in alpha-subunit. Vmax with pyruvate as substrate is 29% compared to wild-type enzyme, Vmax with 2-oxoglutarate as substrate is 40% compared to wild-type enzyme, Km with pyruvate as substrate is 1.5fold higher as compared to wild-type enzyme, Km with 2-oxoglutarate as substrate is 1.5fold higher as compared to wild-type enzyme	-, 739701	
1.2.7.11	S41A	the mutant shows reduced activity compared to the wild type enzyme	-, 739701	
1.2.7.11	T256A	kcat and Km for 2-oxoglutarate are 33% and 51%, respectively, as compared with that of the wild-type enzyme	-, 719399	
1.2.7.11	T256A	kcat/Km for pyruvate is 21% of wild-type value, kcat/KM for 2-oxoglutarate is 15% of wild-type value	-, 719399	
1.2.7.11	T256S	kcat/Km for pyruvate is 15% of wild-type value, kcat/KM for 2-oxoglutarate is 92% of wild-type value	-, 719399	
1.2.7.11	T256V	kcat/Km for pyruvate is 17% of wild-type value, kcat/KM for 2-oxoglutarate is 68% of wild-type value	-, 719399	
1.2.7.11	T349L	mutant enzyme StOFOR1 with mutation T349L in alpha-subunit. Vmax with pyruvate as substrate is 43% compared to wild-type enzyme, Vmax with 2-oxoglutarate as substrate is 74% compared to wild-type enzyme, Km with pyruvate as substrate is 1.6fold higher as compared to wild-type enzyme, Km with 2-oxoglutarate as substrate is 1.1fold higher as compared to wild-type enzyme	-, 739701	
1.2.7.11	T349L	the mutant shows reduced activity compared to the wild type enzyme	-, 739701	
1.2.7.11	Y253A	no enzyme activity at either 50 or 80°C	719399	
1.2.7.11	Y253F	kcat/Km for pyruvate is 3.9% of wild-type value, kcat/KM for 2-oxoglutarate is 16% of wild-type value	-, 719399	
1.2.7.11	Y253W	no enzyme activity at either 50 or 80°C	719399