Crystal structure of an (R)-selective ω-transaminase from Aspergillus terreus.

Chiral amines are important building blocks for the synthesis of pharmaceutical products, fine chemicals, and agrochemicals. ω-Transaminases are able to directly synthesize enantiopure chiral amines by catalysing the transfer of an amino group from a primary amino donor to a carbonyl acceptor with p...

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Autores principales:	Andrzej Łyskowski, Christian Gruber, Georg Steinkellner, Martin Schürmann, Helmut Schwab, Karl Gruber, Kerstin Steiner
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d97d7bbb595e42e8a46ceea7ad294efa
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spelling	oai:doaj.org-article:d97d7bbb595e42e8a46ceea7ad294efa2021-11-18T08:34:48ZCrystal structure of an (R)-selective ω-transaminase from Aspergillus terreus.1932-620310.1371/journal.pone.0087350https://doaj.org/article/d97d7bbb595e42e8a46ceea7ad294efa2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24498081/?tool=EBIhttps://doaj.org/toc/1932-6203Chiral amines are important building blocks for the synthesis of pharmaceutical products, fine chemicals, and agrochemicals. ω-Transaminases are able to directly synthesize enantiopure chiral amines by catalysing the transfer of an amino group from a primary amino donor to a carbonyl acceptor with pyridoxal 5'-phosphate (PLP) as cofactor. In nature, (S)-selective amine transaminases are more abundant than the (R)-selective enzymes, and therefore more information concerning their structures is available. Here, we present the crystal structure of an (R)-ω-transaminase from Aspergillus terreus determined by X-ray crystallography at a resolution of 1.6 Å. The structure of the protein is a homodimer that displays the typical class IV fold of PLP-dependent aminotransferases. The PLP-cofactor observed in the structure is present in two states (i) covalently bound to the active site lysine (the internal aldimine form) and (ii) as substrate/product adduct (the external aldimine form) and free lysine. Docking studies revealed that (R)-transaminases follow a dual binding mode, in which the large binding pocket can harbour the bulky substituent of the amine or ketone substrate and the α-carboxylate of pyruvate or amino acids, and the small binding pocket accommodates the smaller substituent.Andrzej ŁyskowskiChristian GruberGeorg SteinkellnerMartin SchürmannHelmut SchwabKarl GruberKerstin SteinerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 1, p e87350 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Andrzej Łyskowski Christian Gruber Georg Steinkellner Martin Schürmann Helmut Schwab Karl Gruber Kerstin Steiner Crystal structure of an (R)-selective ω-transaminase from Aspergillus terreus.
description	Chiral amines are important building blocks for the synthesis of pharmaceutical products, fine chemicals, and agrochemicals. ω-Transaminases are able to directly synthesize enantiopure chiral amines by catalysing the transfer of an amino group from a primary amino donor to a carbonyl acceptor with pyridoxal 5'-phosphate (PLP) as cofactor. In nature, (S)-selective amine transaminases are more abundant than the (R)-selective enzymes, and therefore more information concerning their structures is available. Here, we present the crystal structure of an (R)-ω-transaminase from Aspergillus terreus determined by X-ray crystallography at a resolution of 1.6 Å. The structure of the protein is a homodimer that displays the typical class IV fold of PLP-dependent aminotransferases. The PLP-cofactor observed in the structure is present in two states (i) covalently bound to the active site lysine (the internal aldimine form) and (ii) as substrate/product adduct (the external aldimine form) and free lysine. Docking studies revealed that (R)-transaminases follow a dual binding mode, in which the large binding pocket can harbour the bulky substituent of the amine or ketone substrate and the α-carboxylate of pyruvate or amino acids, and the small binding pocket accommodates the smaller substituent.
format	article
author	Andrzej Łyskowski Christian Gruber Georg Steinkellner Martin Schürmann Helmut Schwab Karl Gruber Kerstin Steiner
author_facet	Andrzej Łyskowski Christian Gruber Georg Steinkellner Martin Schürmann Helmut Schwab Karl Gruber Kerstin Steiner
author_sort	Andrzej Łyskowski
title	Crystal structure of an (R)-selective ω-transaminase from Aspergillus terreus.
title_short	Crystal structure of an (R)-selective ω-transaminase from Aspergillus terreus.
title_full	Crystal structure of an (R)-selective ω-transaminase from Aspergillus terreus.
title_fullStr	Crystal structure of an (R)-selective ω-transaminase from Aspergillus terreus.
title_full_unstemmed	Crystal structure of an (R)-selective ω-transaminase from Aspergillus terreus.
title_sort	crystal structure of an (r)-selective ω-transaminase from aspergillus terreus.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/d97d7bbb595e42e8a46ceea7ad294efa
work_keys_str_mv	AT andrzejłyskowski crystalstructureofanrselectiveōtransaminasefromaspergillusterreus AT christiangruber crystalstructureofanrselectiveōtransaminasefromaspergillusterreus AT georgsteinkellner crystalstructureofanrselectiveōtransaminasefromaspergillusterreus AT martinschurmann crystalstructureofanrselectiveōtransaminasefromaspergillusterreus AT helmutschwab crystalstructureofanrselectiveōtransaminasefromaspergillusterreus AT karlgruber crystalstructureofanrselectiveōtransaminasefromaspergillusterreus AT kerstinsteiner crystalstructureofanrselectiveōtransaminasefromaspergillusterreus
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Crystal structure of an (R)-selective ω-transaminase from Aspergillus terreus.

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