4.1.1.4	E61Q	the catalytic activity of the mutant shows a decrease in kcat (about 20fold with no change in Km)	705885	
4.1.1.4	E76Q	the catalytic activity of the mutant shows a decrease in kcat, the mutant exhibits a slight downward shift of the pH optimum	705885	
4.1.1.4	E76Q	the catalytic activity of the mutant shows a decrease in kcat, the mutant exhibits aslight downward shift of the pH optimum	705885	
4.1.1.4	E76Q	the mutant shows wild type activity	748436	
4.1.1.4	E76Q	the optimum pH value for the enzymatic activity remains essentially unchanged in the E76Q mutation	715025	
4.1.1.4	K115C	mutant enzymes K115C and K115Q are catalytically inactive at pH 5.95. Mutant enzymes K116C, K116N and K116R have reduced but significant activities	4540	
4.1.1.4	K115Q	mutant enzymes K115C and K115Q are catalytically inactive at pH 5.95. Mutant enzymes K116C, K116N and K116R have reduced but significant activities	4540	
4.1.1.4	additional information	generation of an aadc deletion mutant, the mutant produces a maximum acetone concentration comparable to that produced by wild-type. Non-enzymatic decarboxylation of acetoacetate in vitro, under conditions similar to in vivo acetone-butanol-ethanol fermentation, produces 1.3 to 5.2 g/L acetone between pH 4.0-6.5 and explains why various knock-out and knockdown strategies designed to disrupt aadc in solventogenic Clostridium species do not eliminate acetone production during acetone-butanol-ethanol fermentation	-, 726757	
4.1.1.4	additional information	the butanol ratio increases from 70% to 80.05%, with acetone production reduced to approximately 0.21 g/l in the adc-disrupted mutant 2018adc	-, 705516	
4.1.1.4	R29Q	the catalytic activity of Arg29Gln does not increase at pH values above the wild type optimum for AAD of about 5.4	705885