2.8.3.16	D169A	mutant enzyme is correctly folded and forms interlocked dimers, 1300fold decrease in activity	662253	
2.8.3.16	D169E	mutant enzyme is correctly folded and forms interlocked dimers, inactive mutant enzyme	662253	
2.8.3.16	D169S	mutant enzyme is correctly folded and forms interlocked dimers, inactive mutant enzyme	662253	
2.8.3.16	additional information	construction of a frc deletion mutant, frc expression specifically improves survival in the presence of oxalic acid at pH 3.5, the frc mutant is unable to degrade oxalate, phenotype, overview	-, 671452	
2.8.3.16	W48F	FRC variant	692851	
2.8.3.16	W48Q	FRC variant	692851	
2.8.3.16	G259A	site-directed mutagenesis	693216	
2.8.3.16	G260A	site-directed mutagenesis	693216	
2.8.3.16	Q17A	site-directed mutagenesis	693216