1.14.13.92: phenylacetone monooxygenase
This is an abbreviated version!
For detailed information about phenylacetone monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.92
-
1.14.13.92
-
baeyer-villiger
-
ketone
-
enantioselectivity
-
bvmos
-
thermobifida
-
biocatalytic
-
cyclohexanone
-
fusca
-
synthesis
-
sulfoxidations
-
biocatalyst
-
phosphite
-
cyclopentanone
- 1.14.13.92
-
baeyer-villiger
- ketone
-
enantioselectivity
-
bvmos
-
thermobifida
-
biocatalytic
- cyclohexanone
- fusca
- synthesis
-
sulfoxidations
-
biocatalyst
- phosphite
- cyclopentanone
Reaction
Synonyms
4-hydroxyacetophenone monooxygenase, Baeyer-Villiger monooxygenase, BVMO, EtaA, HAPMO, M-PAMO, More, PAMO, phenylacetone monooxygenase, Tf PAMO
ECTree
Advanced search results
General Information
General Information on EC 1.14.13.92 - phenylacetone monooxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
physiological function
phenylacetone monooxygenase (PAMO) catalyzes oxidation of ketones with molecular oxygen and NADPH with the formation of esters
additional information
phenylacetone monooxygenase is the most stable and thermo-tolerant member of the Baeyer-Villiger monooxygenase family
evolution
phenylacetone monooxygenase from Thermobifida fusca (TfPAMO) is a thermostable Baeyer-Villiger monooxygenase from the NAD(P)H/FAD-dependent oxidoreductase family
evolution
phenylacetone monooxygenase, PAMO, is a NADPH-dependent Baeyer-Villiger monooxygenase
evolution
the enzyme belongs to the group II of Baeyer-Villiger monooxygenases (BMVOs)
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
molecular dynamics simulations and induced fit docking of wild-type and mutant enzymes with cyclohexanone
additional information
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
additional information
enzyme molecular docking and molecular dynamics, computational modeling, overview