English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/159783
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:


Nucleophile Promiscuity of Engineered Class II Pyruvate Aldolase from E. Coli, YfaU

AuthorsHernández Sánchez, Karel ; Joglar Tamargo, Jesús ; Bujons, Jordi; Parella, Teodor; Clapés Saborit, Pere
KeywordsMBP-YfaU W23V/L216A
Pyruvate aldolases
E. Coli
Issue Date24-Jan-2018
CitationAngewandte Chemie - International Edition
AbstractPyruvate-dependent aldolases exhibit a stringent selectivity for pyruvate, limiting their synthetic potential application, a drawback shared with other existing aldolases. Structure-guided rational protein engineering rendered a 2-keto-3-deoxy-L-rhamnonate aldolase variant, fused with maltose binding protein (MBP-YfaU W23V/L216A), capable to efficiently convert larger pyruvate analogs, e.g. having linear and branched aliphatic chains, in aldol addition reactions. Combination of these nucleophiles with N-Cbz-alaninal and N-Cbz-prolinal electrophiles gave access to chiral building blocks, e.g. derivatives of (2S,3S,4R)-4-amino-3-hydroxy-2-methylpentanoic acid (68%, dr 90:10) and the enantiomer of Dolaproine (33%, dr 94:6) as well as a collection of unprecedented α-amino acid derivatives of the proline and pyrrolizidine type, with conversions varying between 6-93% and diasteromeric ratios from 50:50 to 95:5 depending on the nucleophilic and electrophilic components
Publisher version (URL)10.1002/ange.201711289
Appears in Collections:(IQAC) Artículos
Files in This Item:
File Description SizeFormat 
Nucleophile Promiscuity of Engineered Class II Pyruvate Aldolase from E. Coli, YfaU.pdf226,81 kBAdobe PDFThumbnail
Show full item record
Review this work

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.