EC Number |
Cofactor |
Reference |
---|
1.14.13.92 | (R)-NADPD |
deuterated cofactor derivative, the overall rate of catalysis is largely determined by the rate of hydride transfer upon replacement of NADPH by (R)-NADPD as the coenzyme, overview |
685231 |
1.14.13.92 | FAD |
- |
657625, 659371, 710979, 726716, 763827, 763862, 764116, 764264, 764409, 765535 |
1.14.13.92 | FAD |
binding structure involving Arg337, overview |
671189 |
1.14.13.92 | FAD |
residue R337, which is conserved in other Baeyer-Villiger monooxygenases, is positioned close to the flavin cofactor |
685231 |
1.14.13.92 | NADH |
poor activity with NADH, kinetics, binding mode, overview |
710979 |
1.14.13.92 | NADPH |
- |
659371, 671189, 671682, 675467, 677171, 678885, 684245, 685231, 690110, 726716, 726793, 727379, 728163, 728164, 744548, 745991, 763827, 763862, 764116, 764264, 764409, 765535 |
1.14.13.92 | NADPH |
can not be replaced by NADH |
657625 |
1.14.13.92 | NADPH |
PAMO is a type I Baeyer-Villiger monooxygenase, that strongly prefers NADPH over NADH as an electron donor, the function of NADPH in catalysis cannot be easily replaced by NADH. The conserved R217 is essential for binding the adenine moiety of the nicotinamide coenzyme while it also contributes to the recognition of the 2'-phosphate moiety of NADPH, binding mode, overview. T218 and K336 do not have a strong effect on the coenzyme specificity |
710979 |