Biocatalytic Transamination of Aldolase-Derived 3-Hydroxy Ketones

Although optical pure amino alcohols are in high demand due to their widespread applicability, they still remain challenging to synthesize, since commonly elaborated protection strategies are required. Here, a multi-enzymatic methodology is presented that circumvents this obstacle furnishing enantio...

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Detalhes bibliográficos
Autores: Pickl, Mathias, Ebner, Markus, Gittings, Samantha, Clapés Saborit, Pere, Kroutil, Wolfgang
Tipo de documento: artigo
Estado:Versão publicada
Data de publicação:2023
País:España
Recursos:Consejo Superior de Investigaciones Científicas (CSIC)
Repositório:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/307832
Acesso em linha:http://hdl.handle.net/10261/307832
https://api.elsevier.com/content/abstract/scopus_id/85153407068
Access Level:Acceso aberto
Palavra-chave:Transaminase
Aldolase
Biocatalysis
http://metadata.un.org/sdg/3
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Descrição
Resumo:Although optical pure amino alcohols are in high demand due to their widespread applicability, they still remain challenging to synthesize, since commonly elaborated protection strategies are required. Here, a multi-enzymatic methodology is presented that circumvents this obstacle furnishing enantioenriched 1,3-amino alcohols out of commodity chemicals. A Type I aldolase forged the carbon backbone with an enantioenriched aldol motif, which was subsequently subjected to enzymatic transamination. A panel of 194 TAs was tested on diverse nine aldol products prepared through different nucleophiles and electrophiles. Due to the availability of (R)- and (S)-selective TAs, both diastereomers of the 1,3-amino alcohol motif were accessible. A two-step process enabled the synthesis of the desired amino alcohols with up to three chiral centers with de up to >97 in the final products. (Figure presented.).