2.8.3.18	E294A	complete loss of activity	721675	
2.8.3.18	E294A	site-directed mutagenesis, the mutant specific catalytic activity is 10000fold reduced compared to the wild-type enzyme, ligand bound crystal structure modeling	721675	
2.8.3.18	E435A	mutant protein is completely insoluble	721675	
2.8.3.18	E435A	site-directed mutagenesis, the mutant is completely insoluble, ligand bound crystal structure determination and analysis, the mutant crystallizes in a closed complex containing dethiaacetyl-CoA, which adopts an unusual curled conformation	721675	
2.8.3.18	E435D	activity similar to wild-type	721675	
2.8.3.18	E435D	site-directed mutagenesis, the mutant catalytic properties are nearly equivalent to those of the His6-tagged wild-type enzyme, ligand bound crystal structure modeling	721675	
2.8.3.18	E435Q	mutant protein is completely insoluble	721675	
2.8.3.18	E435Q	site-directed mutagenesis, the mutant is completely insoluble, ligand bound crystal structure modeling	721675	
2.8.3.18	N347A	large decrease in catalytic activity	721675	
2.8.3.18	N347A	site-directed mutagenesis, the mutant shows impaired catalytic activity, but the apparent affinities for all four substrates are largely unaffected, ligand bound crystal structure modeling	721675	
2.8.3.18	R228E	large decrease in catalytic activity	721675	
2.8.3.18	R228E	site-directed mutagenesis, the mutant has a specific defect in its ability to bind both carboxylate substrates, ligand bound crystal structure modeling	721675	
2.8.3.18	S71A	large decrease in catalytic activity	721675	
2.8.3.18	S71A	site-directed mutagenesis, the mutant shows impaired catalytic activity associated with lower kcat values, ligand bound crystal structure modeling	721675	
2.8.3.18	N347A	the mutant retains about 15% of wild type specific activity	-, 738287