RESUMO
To expand the available set of Baeyer-Villiger monooxygenases (BVMOs), we have created expression constructs for producing 22 Type I BVMOs that are present in the genome of Rhodococcus jostii RHA1. Each BVMO has been probed with a large panel of potential substrates. Except for testing their substrate acceptance, also the enantioselectivity of some selected BVMOs was studied. The results provide insight into the biocatalytic potential of this collection of BVMOs and expand the biocatalytic repertoire known for BVMOs. This study also sheds light on the catalytic capacity of this large set of BVMOs that is present in this specific actinomycete. Furthermore, a comparative sequence analysis revealed a new BVMO-typifying sequence motif. This motif represents a useful tool for effective future genome mining efforts.
Assuntos
Proteínas de Bactérias/química , Proteínas de Bactérias/genética , Clonagem Molecular , Oxigenases de Função Mista/química , Oxigenases de Função Mista/genética , Rhodococcus/enzimologia , Motivos de Aminoácidos , Sequência de Aminoácidos , Proteínas de Bactérias/metabolismo , Expressão Gênica , Cinética , Oxigenases de Função Mista/metabolismo , Dados de Sequência Molecular , Filogenia , Rhodococcus/química , Rhodococcus/classificação , Rhodococcus/genética , Homologia de Sequência de Aminoácidos , Especificidade por SubstratoRESUMO
Two Candida antarctica lipases catalyze the enantioselective acylation of N-substituted trans-4-(4'-fluorophenyl)-3-hydroxymethylpiperidines in organic solvents. These two lipases show opposite stereochemical preference in these processes. Both enantiomers can be obtained in their optically pure forms. The (3S,4R) isomer, is an intermediate for the synthesis of (-)-Paroxetine.
