Engineered variants of phenylalanine ammonia lyase from Planctomyces brasiliensis were developed through rational design efforts focusing on the aryl binding pocket of the active site, guided by structural and phylogenetic inference. Inherent problems traditionally associated with the biocatalytic hydroamination of acrylic acids, such as low conversion and poor regioselectivity with alkyl and methoxy derivatives, could be overcome. The PbPAL variants described here represent a valuable addition to the biocatalytic toolbox, allowing previously inaccessible amino acid building blocks to be obtained regio- and enantioselectively on preparative scale.

Engineered ammonia lyases for the production of challenging electron-rich L-phenylalanines

Parmeggiani F.;
2018-01-01

Abstract

Engineered variants of phenylalanine ammonia lyase from Planctomyces brasiliensis were developed through rational design efforts focusing on the aryl binding pocket of the active site, guided by structural and phylogenetic inference. Inherent problems traditionally associated with the biocatalytic hydroamination of acrylic acids, such as low conversion and poor regioselectivity with alkyl and methoxy derivatives, could be overcome. The PbPAL variants described here represent a valuable addition to the biocatalytic toolbox, allowing previously inaccessible amino acid building blocks to be obtained regio- and enantioselectively on preparative scale.
2018
biocatalysis; protein engineering; amino acids; ammonia lyases; industrial biotechnology
File in questo prodotto:
File Dimensione Formato  
PbPAL engineering ACS REVISED.pdf

Open Access dal 05/01/2021

: Post-Print (DRAFT o Author’s Accepted Manuscript-AAM)
Dimensione 379.31 kB
Formato Adobe PDF
379.31 kB Adobe PDF Visualizza/Apri

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11311/1126301
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 27
  • ???jsp.display-item.citation.isi??? 24
social impact