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 143 > >>
download as CSV
download all results as CSV
EC Number Protein Variants Commentary Reference
Show all pathways known for 2.7.2.4Display the word mapDisplay the reaction diagram Show all sequences 2.7.2.4A157L site-directed mutagenesis 642333
Show all pathways known for 2.7.2.4Display the word mapDisplay the reaction diagram Show all sequences 2.7.2.4A189L site-directed mutagenesis 642333
Show all pathways known for 2.7.2.4Display the word mapDisplay the reaction diagram Show all sequences 2.7.2.4A23L site-directed mutagenesis 642333
Show all pathways known for 2.7.2.4Display the word mapDisplay the reaction diagram Show all sequences 2.7.2.4A279T isolated from Corynebacterium glutamicum strain IWJ001, aspartate kinase mutant AKA279T is encoded by gene lysC1. The mutant enzymes is completely resistant to feed-back inhibition by L-threonine and L-lysine -, 738802
Show all pathways known for 2.7.2.4Display the word mapDisplay the reaction diagram Show all sequences 2.7.2.4A380I the mutant has 11.32fold higher enzyme activity than the wild type enzyme, enhanced thermal stability and shows weakened inhibition with L-lysine 761955
Show all pathways known for 2.7.2.4Display the word mapDisplay the reaction diagram Show all sequences 2.7.2.4A406T site-directed mutagenesis, 30fold more strongly inhibited by threonine 642332
Show all pathways known for 2.7.2.4Display the word mapDisplay the reaction diagram Show all sequences 2.7.2.4A42S site-directed mutagenesis 642333
Show all pathways known for 2.7.2.4Display the word mapDisplay the reaction diagram Show all sequences 2.7.2.4C428R mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition 722849
Show all pathways known for 2.7.2.4Display the word mapDisplay the reaction diagram Show all sequences 2.7.2.4D154A site-directed mutagenesis 642333
Show all pathways known for 2.7.2.4Display the word mapDisplay the reaction diagram Show all sequences 2.7.2.4D154N site-directed mutagenesis 642333
Results 1 - 10 of 143 > >>
download as CSV
download all results as CSV