Table 1 Kinetic data obtained for LkcE and its mutants
From: Insights into a dual function amide oxidase/macrocyclase from lankacidin biosynthesis
Enzyme | Substrate(s) | kcat (s−1) | KM (μM) |
|---|---|---|---|
LkcE wt | LC-KA05 (1)/elimination derivative (7) mixture | 3.4 ± 0.2 | 5 ± 2 |
LkcE wt | Deacetylated derivative (6) | 2.4 ± 0.1 | 5 ± 1 |
LkcE wt | Deacetylated derivative (6) complemented with DMSO | 2.2 | 3 |
LkcE wt | EMAA (4) | X | X |
LkcE wt | DATD (5) | X | X |
LkcE wt | EMAA (4)/DATD (5) | X | X |
LkcE E64A | LC-KA05 (1)/elimination derivative (7) mixture | X | X |
LkcE E64Q | LC-KA05 (1)/elimination derivative (7) mixture | X | X |
LkcE R326L | LC-KA05 (1)/elimination derivative (7) mixture | X | X |
LkcE R326Q | Deacetylated derivative (6) | 0.88 | 4 |
LkcE Y182F | Deacetylated derivative (6) | 1.5 | 4 |
