In vitro characterization of an enzymatic redox cascade composed of an alcohol dehydrogenase, an enoate reductases and a Baeyer–Villiger monooxygenase
نویسندگان
چکیده
An artificial enzyme cascade composed of an alcohol dehydrogenase, an enoate reductase and a Baeyer-Villiger monooxygenase was investigated in vitro to gain deeper mechanistic insights and understand the assets and drawbacks of this multi-step biocatalysis. Several substrates composed of different structural motifs were examined and provided access to functionalized chiral compounds in high yields (up to >99%) and optical purities (up to >99%). Hence, the applicability of the presented enzymatic cascade was exploited for the synthesis of biorenewable polyesters.
منابع مشابه
A biocatalytic redox isomerisation.
A bi-enzymatic cascade for the redox-isomerisation of allylic alcohol is presented. Coupling of an alcohol dehydrogenase to an enoate reductase has been successfully applied in one pot for the isomerisation of an allylic alcohol to the corresponding ketone. Critical parameters for yield and selectivity have been investigated.
متن کاملMultistep Enzyme Catalyzed Processes 2014
An artificial ‘minipathway’ starting with oxyfunctionalization of readily available limonene to carveol followed by oxidation to the corresponding α,β-unsaturated ketone via an alcohol dehydrogenase, an enoate reductase for the subsequent reduction of the double bond and concluded by a Baeyer-Villiger monooxygenase for the formation of the corresponding lactone is presented. This extension of t...
متن کاملThe prodrug activator EtaA from Mycobacterium tuberculosis is a Baeyer-Villiger monooxygenase.
EtaA is a newly identified FAD-containing monooxygenase that is responsible for activation of several thioamide prodrugs in Mycobacterium tuberculosis. It was found that purified EtaA displays a remarkably low activity with the antitubercular prodrug ethionamide. Hinted by the presence of a Baeyer-Villiger monooxygenase sequence motif in the EtaA sequence, we have been able to identify a large ...
متن کاملEngineering of Baeyer-Villiger monooxygenase-based Escherichia coli biocatalyst for large scale biotransformation of ricinoleic acid into (Z)-11-(heptanoyloxy)undec-9-enoic acid
Baeyer-Villiger monooxygenases (BVMOs) are able to catalyze regiospecific Baeyer-Villiger oxygenation of a variety of cyclic and linear ketones to generate the corresponding lactones and esters, respectively. However, the enzymes are usually difficult to express in a functional form in microbial cells and are rather unstable under process conditions hindering their large-scale applications. The...
متن کاملIdentification of a novel Baeyer‐Villiger monooxygenase from Acinetobacter radioresistens: close relationship to the Mycobacterium tuberculosis prodrug activator EtaA
This work demonstrates that Acinetobacter radioresistens strain S13 during the growth on medium supplemented with long-chain alkanes as the sole energy source expresses almA gene coding for a Baeyer-Villiger monooxygenase (BVMO) involved in alkanes subterminal oxidation. Phylogenetic analysis placed the sequence of this novel BVMO in the same clade of the prodrug activator ethionamide monooxyge...
متن کامل