Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site

L-asparaginases catalyse the hydrolysis of L-asparagine to L-aspartic acid and ammonia. Here, the authors present high resolution crystal structures of Rhizobium etli L-asparaginase that contains a Zn2+ binding site without a catalytic role and discuss the catalytic mechanism of the enzyme.

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Autores principales:	Joanna I. Loch, Barbara Imiolczyk, Joanna Sliwiak, Anna Wantuch, Magdalena Bejger, Miroslaw Gilski, Mariusz Jaskolski
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c9f06facb4a14c2fae5b9053da75c6f1
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spelling	oai:doaj.org-article:c9f06facb4a14c2fae5b9053da75c6f12021-11-21T12:34:50ZCrystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site10.1038/s41467-021-27105-x2041-1723https://doaj.org/article/c9f06facb4a14c2fae5b9053da75c6f12021-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-27105-xhttps://doaj.org/toc/2041-1723L-asparaginases catalyse the hydrolysis of L-asparagine to L-aspartic acid and ammonia. Here, the authors present high resolution crystal structures of Rhizobium etli L-asparaginase that contains a Zn2+ binding site without a catalytic role and discuss the catalytic mechanism of the enzyme.Joanna I. LochBarbara ImiolczykJoanna SliwiakAnna WantuchMagdalena BejgerMiroslaw GilskiMariusz JaskolskiNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Joanna I. Loch Barbara Imiolczyk Joanna Sliwiak Anna Wantuch Magdalena Bejger Miroslaw Gilski Mariusz Jaskolski Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site
description	L-asparaginases catalyse the hydrolysis of L-asparagine to L-aspartic acid and ammonia. Here, the authors present high resolution crystal structures of Rhizobium etli L-asparaginase that contains a Zn2+ binding site without a catalytic role and discuss the catalytic mechanism of the enzyme.
format	article
author	Joanna I. Loch Barbara Imiolczyk Joanna Sliwiak Anna Wantuch Magdalena Bejger Miroslaw Gilski Mariusz Jaskolski
author_facet	Joanna I. Loch Barbara Imiolczyk Joanna Sliwiak Anna Wantuch Magdalena Bejger Miroslaw Gilski Mariusz Jaskolski
author_sort	Joanna I. Loch
title	Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site
title_short	Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site
title_full	Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site
title_fullStr	Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site
title_full_unstemmed	Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site
title_sort	crystal structures of the elusive rhizobium etli l-asparaginase reveal a peculiar active site
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/c9f06facb4a14c2fae5b9053da75c6f1
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Crystal structures of the elusive Rhizobium etli l-asparaginase reveal a peculiar active site

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