EC Number   |
General Information |
Reference |
|---|
   1.14.13.92 | evolution |
phenylacetone monooxygenase from Thermobifida fusca (TfPAMO) is a thermostable Baeyer-Villiger monooxygenase from the NAD(P)H/FAD-dependent oxidoreductase family |
763827 |
| 1.14.13.92 | evolution |
phenylacetone monooxygenase is the most stable and thermo-tolerant member of the Baeyer-Villiger monooxygenase family |
745991 |
| 1.14.13.92 | evolution |
phenylacetone monooxygenase, PAMO, is a NADPH-dependent Baeyer-Villiger monooxygenase |
764264 |
| 1.14.13.92 | evolution |
the enzyme belongs to the group II of Baeyer-Villiger monooxygenases (BMVOs) |
764409 |
| 1.14.13.92 | evolution |
the enzyme belongs to the group II of Baeyer-Villiger monooxygenases (BMVOs). The prototype of the BVMO enzyme family is the Thermobifida fusca phenylacetone monooxygenase (PAMO). Phenylacetone monooxygenase is the most stable and thermo-tolerant member of the Baeyer-Villiger monooxygenases family, but it has very limited substrate scope compared with other BVMOs such as CPMO in group I or CHMO in group III |
765535 |
| 1.14.13.92 | more |
construction of an enzyme structure model exhibiting most of the conserved motifs of the BVMOs, including the FAD binding domain, the NADP(H) binding domain, the flexible linkers, and the signature motif, overview |
763862 |
| 1.14.13.92 | more |
enzyme molecular docking and molecular dynamics, computational modeling, overview |
765535 |
| 1.14.13.92 | more |
molecular dynamics simulations and induced fit docking of wild-type and mutant enzymes with cyclohexanone |
744548 |
| 1.14.13.92 | physiological function |
phenylacetone monooxygenase (PAMO) catalyzes oxidation of ketones with molecular oxygen and NADPH with the formation of esters |
764116 |
