Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Protein Variants

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 10
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.4E61Q the catalytic activity of the mutant shows a decrease in kcat (about 20fold with no change in Km) 705885
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.4E76Q the catalytic activity of the mutant shows a decrease in kcat, the mutant exhibits a slight downward shift of the pH optimum 705885
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.4E76Q the catalytic activity of the mutant shows a decrease in kcat, the mutant exhibits aslight downward shift of the pH optimum 705885
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.4E76Q the mutant shows wild type activity 748436
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.4E76Q the optimum pH value for the enzymatic activity remains essentially unchanged in the E76Q mutation 715025
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.4K115C mutant enzymes K115C and K115Q are catalytically inactive at pH 5.95. Mutant enzymes K116C, K116N and K116R have reduced but significant activities 4540
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.4K115Q mutant enzymes K115C and K115Q are catalytically inactive at pH 5.95. Mutant enzymes K116C, K116N and K116R have reduced but significant activities 4540
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.4more 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
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.4more 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
Display the word mapDisplay the reaction diagram Show all sequences 4.1.1.4R29Q the catalytic activity of Arg29Gln does not increase at pH values above the wild type optimum for AAD of about 5.4 705885
Results 1 - 10 of 10