Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17

Abstract Omega (ω)-transaminase catalyzes the transfer of an amino group from a non-α position amino acid, or an amine compound with no carboxylic group, to an amino acceptor, and has been studied intensively because of its high potential utility in industry and pharmatheutics. The ω-transaminase fr...

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Autores principales:	Young-Cheul Shin, Hyungdon Yun, Hyun Ho Park
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ef94aea327e64249bec491cd8d5ea7a6
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spelling	oai:doaj.org-article:ef94aea327e64249bec491cd8d5ea7a62021-12-02T11:40:25ZStructural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS1710.1038/s41598-018-29846-02045-2322https://doaj.org/article/ef94aea327e64249bec491cd8d5ea7a62018-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-29846-0https://doaj.org/toc/2045-2322Abstract Omega (ω)-transaminase catalyzes the transfer of an amino group from a non-α position amino acid, or an amine compound with no carboxylic group, to an amino acceptor, and has been studied intensively because of its high potential utility in industry and pharmatheutics. The ω-transaminase from Vibrio fluvialis JS17 (Vfat) is an amine:pyruvate transaminase capable of the stereo-selective transamination of arylic chiral amines. This enzyme exhibits extraordinary enantio-selectivity, and has a rapid reaction rate for chiral amine substrates. In this study, we report the crystal structure of the apo form of Vfat. The overall structure of Vfat was typical of other class III aminotransferase exhibiting an N-terminal helical domain, a small domain, and a large domain. Interestingly, the two subunits of apo Vfat in the asymmetric unit had different structures. A comparison of the overall structure to other transaminases, revealed that the structures of the N-terminal helical domain and the large domain can be affected by cofactor occupancy, but the structural rearrangement in these regions can occur independently.Young-Cheul ShinHyungdon YunHyun Ho ParkNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-9 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Young-Cheul Shin Hyungdon Yun Hyun Ho Park Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17
description	Abstract Omega (ω)-transaminase catalyzes the transfer of an amino group from a non-α position amino acid, or an amine compound with no carboxylic group, to an amino acceptor, and has been studied intensively because of its high potential utility in industry and pharmatheutics. The ω-transaminase from Vibrio fluvialis JS17 (Vfat) is an amine:pyruvate transaminase capable of the stereo-selective transamination of arylic chiral amines. This enzyme exhibits extraordinary enantio-selectivity, and has a rapid reaction rate for chiral amine substrates. In this study, we report the crystal structure of the apo form of Vfat. The overall structure of Vfat was typical of other class III aminotransferase exhibiting an N-terminal helical domain, a small domain, and a large domain. Interestingly, the two subunits of apo Vfat in the asymmetric unit had different structures. A comparison of the overall structure to other transaminases, revealed that the structures of the N-terminal helical domain and the large domain can be affected by cofactor occupancy, but the structural rearrangement in these regions can occur independently.
format	article
author	Young-Cheul Shin Hyungdon Yun Hyun Ho Park
author_facet	Young-Cheul Shin Hyungdon Yun Hyun Ho Park
author_sort	Young-Cheul Shin
title	Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17
title_short	Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17
title_full	Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17
title_fullStr	Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17
title_full_unstemmed	Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17
title_sort	structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from vibrio fluvialis js17
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/ef94aea327e64249bec491cd8d5ea7a6
work_keys_str_mv	AT youngcheulshin structuraldynamicsofthetransaminaseactivesiterevealedbythecrystalstructureofacofactorfreeomegatransaminasefromvibriofluvialisjs17 AT hyungdonyun structuraldynamicsofthetransaminaseactivesiterevealedbythecrystalstructureofacofactorfreeomegatransaminasefromvibriofluvialisjs17 AT hyunhopark structuraldynamicsofthetransaminaseactivesiterevealedbythecrystalstructureofacofactorfreeomegatransaminasefromvibriofluvialisjs17
_version_	1718395678741233664

Structural dynamics of the transaminase active site revealed by the crystal structure of a co-factor free omega-transaminase from Vibrio fluvialis JS17

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