Sökning: onr:"swepub:oai:DiVA.org:kth-163448" >
Engineering the Act...
Engineering the Active Site of the Amine Transaminase from Vibrio fluvialis for the Asymmetric Synthesis of Aryl-Alkyl Amines and Amino Alcohols
-
Nobili, Alberto (författare)
-
- Steffen-Munsberg, Fabian (författare)
- KTH,Industriell bioteknologi,University of Greifswald, Germany
-
Kohls, Hannes (författare)
-
visa fler...
-
Trentin, Ivan (författare)
-
Schulzke, Carola (författare)
-
Höhne, Matthias (författare)
-
Bornscheuer, Uwe T. (författare)
-
visa färre...
-
(creator_code:org_t)
- 2015-02-02
- 2015
- Engelska.
-
Ingår i: ChemCatChem. - : Wiley. - 1867-3880 .- 1867-3899. ; 7:5, s. 757-760
- Relaterad länk:
-
https://urn.kb.se/re...
-
visa fler...
-
https://doi.org/10.1...
-
visa färre...
Abstract
Ämnesord
Stäng
- 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.
Ämnesord
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Nyckelord
- amine transaminase
- biocatalysis
- protein engineering
- substrate scope
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
Hitta via bibliotek
Till lärosätets databas