Back to Search
Start Over
Rational engineering of Luminiphilus syltensis (R)-selective amine transaminase for the acceptance of bulky substrates.
- Source :
-
Chemical Communications . 12/14/2021, Vol. 57 Issue 96, p12948-12951. 4p. - Publication Year :
- 2021
-
Abstract
- Despite the plethora of information on (S)-selective amine transaminases, the (R)-selective ones are still not well-studied; only a few structures are known to date, and their substrate scope is limited, apart from a few stellar works in the field. Herein, the structure of Luminiphilus syltensis (R)-selective amine transaminase is elucidated to facilitate engineering towards variants active on bulkier substrates. The V37A variant exhibited increased activity towards 1-phenylpropylamine and to activity against 1-butylamine. In contrast, the S248 and T249 positions, located on the β-turn in the P-pocket, seem crucial for maintaining the activity of the enzyme. [ABSTRACT FROM AUTHOR]
- Subjects :
- *AMINES
*STAR-branched polymers
*AMINOTRANSFERASES
*ENGINEERING
Subjects
Details
- Language :
- English
- ISSN :
- 13597345
- Volume :
- 57
- Issue :
- 96
- Database :
- Academic Search Index
- Journal :
- Chemical Communications
- Publication Type :
- Academic Journal
- Accession number :
- 153948893
- Full Text :
- https://doi.org/10.1039/d1cc04664k