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A protein engineering approach for expanding the substrate scope of the (S)-selective Chromobacterium violaceum amine transaminase is presented. Amino acid residues in the small binding pocket of the active site were targeted in order to increase the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::186a1c6d1c28353780690231518897dc
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-408218
http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-408218
Autor:
Jonatan C. Campillo-Brocal, Björn Walse, Maria Svedendahl Humble, Federica Ruggieri, Derek T. Logan, Shan Chen, Per Berglund
Publikováno v:
Scientific Reports, Vol 9, Iss 1, Pp 1-15 (2019)
Scientific Reports
Scientific Reports
One of the main factors hampering the implementation in industry of transaminase-based processes for the synthesis of enantiopure amines is their often low storage and operational stability. Our still limited understanding of the inactivation process
Publikováno v:
ChemCatChem
Chemcatchem
Chemcatchem
Dynamic kinetic resolution (DKR) reactions in which a stereoselective enzyme and a racemization step are coupled in one pot would represent powerful tools for the production of enantiopure amines through enantioconvergence of racemates. The exploitat