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