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Results 1 - 10 of 15 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 1.5.1.7Display the reaction diagram Show all sequences 1.5.1.7C205S the Km for N6-(L-1,3-dicarboxypropyl)-L-lysine decreases by more than 30fold for the C205S mutant 724117
Show all pathways known for 1.5.1.7Display the reaction diagram Show all sequences 1.5.1.7C205V the Km for N6-(L-1,3-dicarboxypropyl)-L-lysine decreases by 5fold for the C205V mutant 724117
Show all pathways known for 1.5.1.7Display the reaction diagram Show all sequences 1.5.1.7E122A mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type 712442
Show all pathways known for 1.5.1.7Display the reaction diagram Show all sequences 1.5.1.7E122Q mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type 712442
Show all pathways known for 1.5.1.7Display the reaction diagram Show all sequences 1.5.1.7E16Q/C205S the mutation decreases the turnover number by about 15fold 724121
Show all pathways known for 1.5.1.7Display the reaction diagram Show all sequences 1.5.1.7E78A mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism differs from wild-type, 2-oxoglutarate binds to enzyme and enzyme-NADH 712442
Show all pathways known for 1.5.1.7Display the reaction diagram Show all sequences 1.5.1.7E78A/E122A mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type 712442
Show all pathways known for 1.5.1.7Display the reaction diagram Show all sequences 1.5.1.7E78Q mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type 712442
Show all pathways known for 1.5.1.7Display the reaction diagram Show all sequences 1.5.1.7E78Q/E122Q mutation increases the positive charge of the active site and affects the pKa value of the catalytic group. Kinetic mechanism similar to wild-type 712442
Show all pathways known for 1.5.1.7Display the reaction diagram Show all sequences 1.5.1.7H96Q the mutation results in 100 and more than 1000fold increases in Km values for L-lysine and 2-oxoglutarate, respectively 724358
Results 1 - 10 of 15 > >>