6.2.1.33	D385A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	D402A	100fold decrease in ratio kcat/Km for CoA	702299	
6.2.1.33	D402P	crystallization data. Mutant adopts the proposed adenylate-forming conformation with very little change to the overall structure.The ability of the mutant to catalyze the adenylate-forming half-reaction is reduced by about 3fold, catalysis of the second half-reaction is reduced by 4 orders of magnitude	702299	
6.2.1.33	E306Q	mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate	-, 776	
6.2.1.33	E410A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	F473A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzymem but increased kcat	690988	
6.2.1.33	G163I	mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate	-, 776	
6.2.1.33	G166I	mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate	-, 776	
6.2.1.33	G408A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	H207A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	H207F	site-directed mutagenesis,the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	H207Q	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	H254A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	K169M	mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate	-, 776	
6.2.1.33	K477A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	K492A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	K492L	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	K492R	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	M203A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	N302A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	P168A	mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate	-, 776	
6.2.1.33	R400A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	R439A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	R475A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	R87A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	S407A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	T161A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	T251A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	T306A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	T307A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988	
6.2.1.33	W440A	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, but increased kcat	690988	
6.2.1.33	Y304F	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	690988