EC Number |
Protein Variants |
Reference |
---|
1.5.1.7 | C205S |
the Km for N6-(L-1,3-dicarboxypropyl)-L-lysine decreases by more than 30fold for the C205S mutant |
724117 |
1.5.1.7 | C205V |
the Km for N6-(L-1,3-dicarboxypropyl)-L-lysine decreases by 5fold for the C205V mutant |
724117 |
1.5.1.7 | 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 |
1.5.1.7 | 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 |
1.5.1.7 | E16Q/C205S |
the mutation decreases the turnover number by about 15fold |
724121 |
1.5.1.7 | E78A |
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 |
1.5.1.7 | E78A/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 |
1.5.1.7 | E78Q |
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 |
1.5.1.7 | E78Q/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 |
1.5.1.7 | H96Q |
the mutation results in 100 and more than 1000fold increases in Km values for L-lysine and 2-oxoglutarate, respectively |
724358 |