EC Number |
Protein Variants |
Reference |
---|
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 | more |
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 | more |
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 |