2.3.3.14	D123N	mutant	704648	
2.3.3.14	E155A	mutant enzyme exhibits 1000fold lower activity than wild-type enzyme. Activity of E155A can be partially rescued by formate	685263	
2.3.3.14	E155Q	mutant enzyme exhibits 1000fold lower activity than wild-type enzyme. The kcat for E155Q decreases at high pH, similar to the wild-type enzyme, but is pH independent at low pH	685263	
2.3.3.14	E167A	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	E167Q	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	E222Q	mutant	704648	
2.3.3.14	E74A	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	E74Q	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	H103A	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	H309A	inactive mutant enzyme. Slight increase in activity is observed for H309A in the presence of 300 mM imidazole, which is still 1000fold lower than that of wild type	685263	
2.3.3.14	H309N	inactive mutant enzyme	685263	
2.3.3.14	H72L	replacement of His72 by leucine makes HCS resistant to lysine inhibition, demonstrating the regulatory role of this conserved residue	704692	
2.3.3.14	additional information	activity and protein level of homocitrate synthase are dramatically reduced upon depletion of CuZn-superoxide dismutase. Overexpression of the lys4 gene increases homocitrate synthase activity and is sufficient to suppress the lysine requirement of CuZn-superoxide dismutase-deficient cells	674553	
2.3.3.14	additional information	the RAM domain is responsible for enzyme inhibition. A mutant enzyme lacking the RAM domain is insensitive to inhibition by lysine	-, 756728	
2.3.3.14	Q364R	mutant	704648	
2.3.3.14	Q47A	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	R163A	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	R163K	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	R163Q	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	R288K	mutant	704648	
2.3.3.14	R43A	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	R43K	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	R43Q	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	S165A	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	T197A	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	T197S	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	T197V	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	Y320F	mutant enzyme loses 25fold activity compared to that of the wild-type enzyme	685263	
2.3.3.14	Y332A	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600	
2.3.3.14	Y332F	mutant, reveals the contribution of this residue to substrate binding and catalysis	704600