Rational engineering of Luminiphilus syltensis ( R )-selective amine transaminase for the acceptance of bulky substrates
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BiBTeXDespite 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 the day, and their substrate scope is limited, apart from a few stellar works on the field. Herein, Luminiphilus syltensis (R)-selective amine transaminase’s structure was elucidated to facilitate the engineering towards variants active on bulkier substrates. V37A variant led to increased activity towards 1-phenylpropylamine and to activity against 1-butylamine. On the contrary, S248 and T249 positions, located on the β-turn in P-pocket, seem crucial for maintaining enzyme’s activity.
SEEK ID: https://fairdomhub.org/publications/629
DOI: 10.1039/D1CC04664K
Projects: CEPOPA - Development of sustainable chemoenzymatic processes for optical...
Publication type: Journal
Journal: Chemical Communications
Citation: Chem. Commun.,10.1039.D1CC04664K
Date Published: 2021
Registered Mode: by DOI
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Created: 14th Nov 2021 at 13:57
Last updated: 8th Dec 2022 at 17:26
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https://orcid.org/0000-0001-5811-368XAssist. Prof. of Enzyme Technology Laboratory, Department of Chemistry, University of Crete, Greece
The Hellenic Foundation for Research and Innovation is a new institution through which a profound reforming effort is being undertaken in the field of Research and Innovation in the country. The Organization supports unrestricted research (the systematic inquiry born of scientific curiosity) and new researchers by providing scholarships for doctoral candidates, as well as research projects for post-doctoral students, Researchers and Faculty Members. Through H.F.R.I., the research and academic ...
Web page: http://www.elidek.gr/en/homepage/
CEPOPA envisions a sustainable cascade one-pot process for the synthesis of optically pure amines from alcohols and/or alkynes, using enzymes immobilized onto catalytically active nanomaterials. In the framework of the project, efficient chemoenzymatic processes will be developed for the synthesis of a set of amines that can be used as building blocks for pharmaceuticals or biomaterials.
Programme: Hellenic Foundation for Research and Innovation - Supporting academic Staff and Researchers
Public web page: Not specified
Start date: 24th Feb 2020
End date: 23rd Aug 2023
The structure of was Transaminase of gamma-proteobacterium deposited in PDB under the code: 7p3t
Creator: Eleni Konia
Submitter: Ioannis Metaxas
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Data of the activity/pH profile of the under study enzymes
Creator: Eleni Konia
Submitter: Ioannis Metaxas
Data for the photometric determination of the activity for the under study enzymes.
Creator: Eleni Konia
Submitter: Ioannis Metaxas
Data file for the Pyridoxamine phosphate formation assay
Creator: Eleni Konia
Submitter: Ioannis Metaxas
