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  3. Mining for Novel Tryptophanase A: Extremophilic Organisms Ardenticatena maritima and Haloarcula japonica as Alternatives to E. coli in the Synthesis of Tryptophan Analogues

Mining for Novel Tryptophanase A: Extremophilic Organisms Ardenticatena maritima and Haloarcula japonica as Alternatives to E. coli in the Synthesis of Tryptophan Analogues

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DOI
10.48620/99706
Publisher DOI
10.1002/cctc.70908
Abstract
Tryptophan (Trp) analogues are a subgroup of noncanonical amino acids (ncAAs), which are increasingly valued in the chemical and pharmaceutical industries. Biocatalytic approaches to the preparation of enantiopure Trp analogues offer highly sustainable pathways with unrivalled stereoselectivity and efficiency. In this study, we characterized two novel TnaA enzymes from the extremophilic bacterium Ardenticatena maritima and archaeon Haloarcula japonica which, in comparison to the well-established Escherichia colitryptophanase (EcTnaA), exhibited enhanced stability under extreme physicochemical conditions, making them promising candidates for biocatalytic synthesis of indole-containing amino acids.
Date Issued
2026-07
Publication Type
Article
Language(s)
en
Author(s)
Aziziyan, Fatemeh  
DCBP Gruppe Prof. Paradisi (Pharmazie)  
Sgroi, Evelyn  
DCBP Gruppe Prof. Paradisi (Pharmazie)  
Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP)  
Frati, Giulia  
Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP)  
Mariem, Omar Ben
Eberini, Ivano
Tolomelli, Alessandra
Paradisi, Francesca  
DCBP Gruppe Prof. Paradisi  
Additional Credits
DCBP Gruppe Prof. Paradisi (Pharmazie)  
Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP)  
DCBP Gruppe Prof. Paradisi  
Journal
ChemCatChem
Publisher
Wiley
ISSN
1867-3880
1867-3899
Access(Rights)
open.access
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