Two distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-ACP thioesterase

The substrate specificity of acyl-ACP thioesterase (TE) plays a crucial role in determining the product profile of type II fatty acid synthase. Utilizing two FatB-type acyl-ACP TEs, the authors here define determinants of substrate specificity and create synthetic enzymes with distinct catalytic tra...

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Autores principales:	Fuyuan Jing, Le Zhao, Marna D. Yandeau-Nelson, Basil J. Nikolau
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/17d741f5a0974db283669f98d20cacb7
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id	oai:doaj.org-article:17d741f5a0974db283669f98d20cacb7
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spelling	oai:doaj.org-article:17d741f5a0974db283669f98d20cacb72021-12-02T14:40:44ZTwo distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-ACP thioesterase10.1038/s41467-018-03310-z2041-1723https://doaj.org/article/17d741f5a0974db283669f98d20cacb72018-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-03310-zhttps://doaj.org/toc/2041-1723The substrate specificity of acyl-ACP thioesterase (TE) plays a crucial role in determining the product profile of type II fatty acid synthase. Utilizing two FatB-type acyl-ACP TEs, the authors here define determinants of substrate specificity and create synthetic enzymes with distinct catalytic traits.Fuyuan JingLe ZhaoMarna D. Yandeau-NelsonBasil J. NikolauNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-10 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Fuyuan Jing Le Zhao Marna D. Yandeau-Nelson Basil J. Nikolau Two distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-ACP thioesterase
description	The substrate specificity of acyl-ACP thioesterase (TE) plays a crucial role in determining the product profile of type II fatty acid synthase. Utilizing two FatB-type acyl-ACP TEs, the authors here define determinants of substrate specificity and create synthetic enzymes with distinct catalytic traits.
format	article
author	Fuyuan Jing Le Zhao Marna D. Yandeau-Nelson Basil J. Nikolau
author_facet	Fuyuan Jing Le Zhao Marna D. Yandeau-Nelson Basil J. Nikolau
author_sort	Fuyuan Jing
title	Two distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-ACP thioesterase
title_short	Two distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-ACP thioesterase
title_full	Two distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-ACP thioesterase
title_fullStr	Two distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-ACP thioesterase
title_full_unstemmed	Two distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-ACP thioesterase
title_sort	two distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-acp thioesterase
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/17d741f5a0974db283669f98d20cacb7
work_keys_str_mv	AT fuyuanjing twodistinctdomainscontributetothesubstrateacylchainlengthselectivityofplantacylacpthioesterase AT lezhao twodistinctdomainscontributetothesubstrateacylchainlengthselectivityofplantacylacpthioesterase AT marnadyandeaunelson twodistinctdomainscontributetothesubstrateacylchainlengthselectivityofplantacylacpthioesterase AT basiljnikolau twodistinctdomainscontributetothesubstrateacylchainlengthselectivityofplantacylacpthioesterase
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Two distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-ACP thioesterase

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