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Results 1 - 10 of 30 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 1.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.3G378E feedback resistance of the enzyme 246394
Show all pathways known for 1.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.3G378S construction of a homoserine dehydrogenase mutant HDG378S, encoded by hom1, in Corynebacterium glutamicum strain IWJ001, one of the best L-isoleucine producing strains. Strain HDG378S is partially resistant to L-threonine with the half maximal inhibitory concentration between 12 and 14 mM. Overexpression of lysC1, hom1 and thrB1 increased L-threonine and L-lysine production in Corynebacterium glutamicum ATCC13869 by 96folds and 21.2folds, respectively, overview -, 738802
Show all pathways known for 1.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.3G433R site-directed mutagenesis, strain HS33/pACYC-pycP458S-thrAG433R-lysC shows increased activity (62.4% of the maximum theoretical yield) -, 760402
Show all pathways known for 1.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.3H309A decrease of catalytic activity and elimination of substrate inhibition 246402
Show all pathways known for 1.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.3K105A site-directed double-primer PCR mutagenesis -, 739791
Show all pathways known for 1.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.3K105R site-directed double-primer PCR mutagenesis -, 739791
Show all pathways known for 1.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.3K195A site-directed mutagenesis, inactive mutant. In the crystal structure, the positions of Lys195 and L-Hse are significantly retained with those of the wild-type enzyme, enzyme crystal structure analysis 761404
Show all pathways known for 1.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.3K205A site-directed double-primer PCR mutagenesis -, 739791
Show all pathways known for 1.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.3K57Aa site-directed mutagenesis, in contrast to the wild-type enzyme, the mutant enzyme shows catalytic activity with NADP+, the activity with NAD+ is increased compared to the wild-type enzyme -, 741408
Show all pathways known for 1.1.1.3Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.3K99A site-directed mutagenesis, inactive mutant. In the crystal structure, the productive geometry of the ternary complex is almost preserved with one new water molecule taking over the hydrogen bonds associated with Lys99, mutant enzyme crystal structure analysis 761404
Results 1 - 10 of 30 > >>