EC Number   |
Reaction |
Reference |
|---|
   1.14.13.92 | phenylacetone + NADPH + H+ + O2 = benzyl acetate + NADP+ + H2O |
- |
- |
| 1.14.13.92 | phenylacetone + NADPH + H+ + O2 = benzyl acetate + NADP+ + H2O |
catalytic mechanism, via C4a-peroxyflavin and Criegee intermediates, of phenylacetone monooxygenases for the native substrate phenylacetone as well as for a linear non-native substrate 2-octanone, using molecular dynamics simulations, quantum mechanics and quantum mechanics/molecular mechanics calculations, and theoretical basis for the preference of the enzyme for the native aromatic substrate over non-native linear substrates, overview |
745991 |
| 1.14.13.92 | phenylacetone + NADPH + H+ + O2 = benzyl acetate + NADP+ + H2O |
reaction mechanism |
671189 |
| 1.14.13.92 | phenylacetone + NADPH + H+ + O2 = benzyl acetate + NADP+ + H2O |
reaction mechanism and catalytic cycle, rapid binding of NADPH is followed by a transfer of the (4R)-hydride from NADPH to the FAD cofactor. The reduced PAMO is rapidly oxygenated by molecular oxygen, yielding a C4a-peroxyflavin. The peroxyflavin enzyme intermediate, possibly a Criegee intermediate or a C4a-hydroxyflavin form, reacts with phenylacetone to form benzylacetate, residue R337 is important in catalysis, overview |
684245, 685231, 690110 |
| 1.14.13.92 | phenylacetone + NADPH + H+ + O2 = benzyl acetate + NADP+ + H2O |
the reaction mechanism of BVMO, and particularly PAMO, with native substrate phenylacetone proceeds via the formation of a Criegee intermediate with anionic character, which is subsequently rearranged via the migration of alkyl group to yield the product ester, reaction mechanism, overview. Modeling of the reaction intermediate C4a-peroxyflavin |
765535 |
