1.7.1.17	F117A	the mutant shows 208% activity with Methyl Red and 176% activity with NADH compared to the wild type enzyme	765245	
1.7.1.17	F161A	inactive	765245	
1.7.1.17	F162A	site-directed mutagenesis	742834	
1.7.1.17	G140F	inactive	765245	
1.7.1.17	G141F	inactive	765245	
1.7.1.17	H143A	the mutant shows 19% activity with Methyl Red and 76% activity with NADH compared to the wild type enzyme	765245	
1.7.1.17	additional information	deletion of the azoR gene in Escherichia coli strain MG1655 has no strong influence on the 7NCCA reduction of the cells even though the pure enzyme displays a clear nitroreductase activity with this compound	743185	
1.7.1.17	N121Q	115% of wild-type activity	-, 744201	
1.7.1.17	N96A	the mutant shows 9% activity with Methyl Red and 37% activity with NADH compared to the wild type enzyme	765245	
1.7.1.17	R139A	the mutant shows 63% activity with Methyl Red and 78% activity with NADH compared to the wild type enzyme	765245	
1.7.1.17	R21G/N121A	136% of wild-type activity	-, 744201	
1.7.1.17	R21G/N121Q	171% of wild-type activity	-, 744201	
1.7.1.17	R21K	80% of wild-type activity	-, 744201	
1.7.1.17	R21K/N121A	41% of wild-type activity	-, 744201	
1.7.1.17	R21K/N121Q	40% of wild-type activity	744201	
1.7.1.17	R59A	site-directed mutagenesis, the mutation enhances the Vmax value for p-methyl red 27fold with a 3.8fold increase of the Km value, residue Arg59 decides the substrate specificity of AzoR	742834	
1.7.1.17	R59A	the mutant shows 70% activity with Methyl Red and 83% activity with NADH compared to the wild type enzyme	765245	
1.7.1.17	R59G	mutation influences the formation of dilution-induced intermediates. Mutant R59G contains only two types of FMN, emitting at 530 nm and 600 nm	744730	
1.7.1.17	S16A	the mutant shows 29% activity with Methyl Red and 49% activity with NADH compared to the wild type enzyme	765245	
1.7.1.17	W105A	complete loss of both affinity for FMN and enzyme activity	-, 745718	
1.7.1.17	W105F	31fold decrease in vmax value, Km value similar to wild-type	-, 745718	
1.7.1.17	W105G	complete loss of both affinity for FMN and enzyme activity	745718	
1.7.1.17	W105H	8fold decrease in vmax value, Km value similar to wild-type	-, 745718	
1.7.1.17	W105Q	68fold decrease in vmax value, Km value similar to wild-type	-, 745718	
1.7.1.17	W105Y	22% reduction in vmax value	-, 745718	
1.7.1.17	W60D	the mutant retains more than 10% of wild type activity	-, 763801	
1.7.1.17	Y119A	the mutant shows 59% activity with Methyl Red and 44% activity with NADH compared to the wild type enzyme	765245	
1.7.1.17	Y120A	site-directed mutagenesis	742834	
1.7.1.17	Y127F	site-directed mutagenesis, Diffraction-quality crystals for the Y127F mutant cannot be obtained	-, 763965	
1.7.1.17	Y151F	site-directed mutagenesis, structure comparison with the wild-type enzyme	-, 763965