Engineering the Active Site of the Amine Transaminase from Vibrio fluvialis for the Asymmetric Synthesis of Aryl-Alkyl Amines and Amino Alcohols
2015 (English)In: ChemCatChem, ISSN 1867-3880, E-ISSN 1867-3899, Vol. 7, no 5, 757-760 p.Article in journal (Refereed) Published
Although the amine transaminase from Vibrio fluvialis has often been applied as a catalyst for the biocatalytic preparation of various chiral primary amines, it is not suitable for the transamination of a-hydroxy ketones and aryl-alkyl ketones bearing an alkyl substituent larger than a methyl group. We addressed this problem through a systematic mutagenesis study of active site residues to expand its substrate scope towards two bulky ketones. We identified two mutants (F85L/V153A and Y150F/V153A) showing 30-fold increased activity in the conversion of (S)-phenylbutylamine and (R)-phenylglycinol, respectively. Notably, they facilitated asymmetric synthesis of these amines with excellent enantiomeric purities of 98% ee.
Place, publisher, year, edition, pages
2015. Vol. 7, no 5, 757-760 p.
amine transaminase, biocatalysis, protein engineering, substrate scope
IdentifiersURN: urn:nbn:se:kth:diva-163448DOI: 10.1002/cctc.201403010ISI: 000350473500008ScopusID: 2-s2.0-84922517376OAI: oai:DiVA.org:kth-163448DiVA: diva2:801019
FunderEU, FP7, Seventh Framework Programme, KBBE-2011-5 289350
QC 201504082015-04-082015-04-072015-04-08Bibliographically approved