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Rational engineering of Luminiphilus syltensis (R)-selective amine transaminase for the acceptance of bulky substrates
- Source :
- Chemical Communications. 57:12948-12951
- Publication Year :
- 2021
- Publisher :
- Royal Society of Chemistry (RSC), 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.
- Subjects :
- chemistry.chemical_classification
Stereochemistry
Metals and Alloys
Rational engineering
Substrate (chemistry)
General Chemistry
Luminiphilus syltensis
Catalysis
Surfaces, Coatings and Films
Electronic, Optical and Magnetic Materials
Transaminase
Enzyme
chemistry
Materials Chemistry
Ceramics and Composites
Amine gas treating
Subjects
Details
- ISSN :
- 1364548X and 13597345
- Volume :
- 57
- Database :
- OpenAIRE
- Journal :
- Chemical Communications
- Accession number :
- edsair.doi...........d8551938ee0eb7e89a291f1e499d7174