Visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase

Mevalonate diphosphate decarboxylase (MDD) is a key enzyme in the mevalonate pathway and catalyses the decarboxylation of mevalonate-5-diphosphate to isopentenyl diphosphate. Here, the authors provide insights into the conformational changes that occur during substrate binding of MDD and the subsequ...

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Autores principales:	Chun-Liang Chen, Lake N. Paul, James C. Mermoud, Calvin Nicklaus Steussy, Cynthia V. Stauffacher
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b0d17fe2854d4bb9a893293053f08b6e
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spelling	oai:doaj.org-article:b0d17fe2854d4bb9a893293053f08b6e2021-12-02T16:35:19ZVisualizing the enzyme mechanism of mevalonate diphosphate decarboxylase10.1038/s41467-020-17733-02041-1723https://doaj.org/article/b0d17fe2854d4bb9a893293053f08b6e2020-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-17733-0https://doaj.org/toc/2041-1723Mevalonate diphosphate decarboxylase (MDD) is a key enzyme in the mevalonate pathway and catalyses the decarboxylation of mevalonate-5-diphosphate to isopentenyl diphosphate. Here, the authors provide insights into the conformational changes that occur during substrate binding of MDD and the subsequent enzymatic reaction steps by determining the substrate and intermediate bound crystal structures of Enterococcus faecalis MDD.Chun-Liang ChenLake N. PaulJames C. MermoudCalvin Nicklaus SteussyCynthia V. StauffacherNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Chun-Liang Chen Lake N. Paul James C. Mermoud Calvin Nicklaus Steussy Cynthia V. Stauffacher Visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase
description	Mevalonate diphosphate decarboxylase (MDD) is a key enzyme in the mevalonate pathway and catalyses the decarboxylation of mevalonate-5-diphosphate to isopentenyl diphosphate. Here, the authors provide insights into the conformational changes that occur during substrate binding of MDD and the subsequent enzymatic reaction steps by determining the substrate and intermediate bound crystal structures of Enterococcus faecalis MDD.
format	article
author	Chun-Liang Chen Lake N. Paul James C. Mermoud Calvin Nicklaus Steussy Cynthia V. Stauffacher
author_facet	Chun-Liang Chen Lake N. Paul James C. Mermoud Calvin Nicklaus Steussy Cynthia V. Stauffacher
author_sort	Chun-Liang Chen
title	Visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase
title_short	Visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase
title_full	Visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase
title_fullStr	Visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase
title_full_unstemmed	Visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase
title_sort	visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/b0d17fe2854d4bb9a893293053f08b6e
work_keys_str_mv	AT chunliangchen visualizingtheenzymemechanismofmevalonatediphosphatedecarboxylase AT lakenpaul visualizingtheenzymemechanismofmevalonatediphosphatedecarboxylase AT jamescmermoud visualizingtheenzymemechanismofmevalonatediphosphatedecarboxylase AT calvinnicklaussteussy visualizingtheenzymemechanismofmevalonatediphosphatedecarboxylase AT cynthiavstauffacher visualizingtheenzymemechanismofmevalonatediphosphatedecarboxylase
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Visualizing the enzyme mechanism of mevalonate diphosphate decarboxylase

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