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