Rational engineering of Luminiphilus syltensis(R)-selective amine transaminase for the acceptance of bulky substrates
Konia, Eleni ; Chatzicharalampous, Constantinos LU
; Drakonaki, Athina
; Muenke, Cornelia
; Ermler, Ulrich
; Tsiotis, Georgios
and Pavlidis, Ioannis V.
(2021)
In Chemical Communications
57(96).
p.12948-12951
- 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 ofLuminiphilus 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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/42308441-2649-4e90-9ffd-2acacd902e8d
- author
- Konia, Eleni
; Chatzicharalampous, Constantinos
LU
; Drakonaki, Athina
; Muenke, Cornelia
; Ermler, Ulrich
; Tsiotis, Georgios
and Pavlidis, Ioannis V.
- organization
- publishing date
- 2021-12-14
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Chemical Communications
- volume
- 57
- issue
- 96
- pages
- 4 pages
- publisher
- Royal Society of Chemistry
- external identifiers
-
- pmid:34806715
- scopus:85120548758
- ISSN
- 1359-7345
- DOI
- 10.1039/d1cc04664k
- language
- English
- LU publication?
- yes
- id
- 42308441-2649-4e90-9ffd-2acacd902e8d
- date added to LUP
- 2023-12-19 13:21:07
- date last changed
- 2024-04-03 21:35:40
@article{42308441-2649-4e90-9ffd-2acacd902e8d,
abstract = {{<p>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 ofLuminiphilus 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.</p>}},
author = {{Konia, Eleni and Chatzicharalampous, Constantinos and Drakonaki, Athina and Muenke, Cornelia and Ermler, Ulrich and Tsiotis, Georgios and Pavlidis, Ioannis V.}},
issn = {{1359-7345}},
language = {{eng}},
month = {{12}},
number = {{96}},
pages = {{12948--12951}},
publisher = {{Royal Society of Chemistry}},
series = {{Chemical Communications}},
title = {{Rational engineering of <i>Luminiphilus syltensis(R)</i>-selective amine transaminase for the acceptance of bulky substrates}},
url = {{http://dx.doi.org/10.1039/d1cc04664k}},
doi = {{10.1039/d1cc04664k}},
volume = {{57}},
year = {{2021}},
}