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