Different ways to transport ammonia in human and Mycobacterium tuberculosis NAD+ synthetases

M. tuberculosis NAD+ synthetase (tbNadE) is of interest as a drug target. Here the authors present the actively trapped Homo sapiens NAD+ synthetase (hsNadE) and tbNadE structures and show key differences in the synthetase active site and in structural elements possibly involved in the allosteric re...

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Autores principales:	Watchalee Chuenchor, Tzanko I. Doukov, Kai-Ti Chang, Melissa Resto, Chang-Soo Yun, Barbara Gerratana
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/9040fcaf75534cfa8218a7838eb8215a
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spelling	oai:doaj.org-article:9040fcaf75534cfa8218a7838eb8215a2021-12-02T14:40:28ZDifferent ways to transport ammonia in human and Mycobacterium tuberculosis NAD+ synthetases10.1038/s41467-019-13845-42041-1723https://doaj.org/article/9040fcaf75534cfa8218a7838eb8215a2020-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-13845-4https://doaj.org/toc/2041-1723M. tuberculosis NAD+ synthetase (tbNadE) is of interest as a drug target. Here the authors present the actively trapped Homo sapiens NAD+ synthetase (hsNadE) and tbNadE structures and show key differences in the synthetase active site and in structural elements possibly involved in the allosteric regulation of catalysis to be leveraged for the development of M. tuberculosis selective inhibitors.Watchalee ChuenchorTzanko I. DoukovKai-Ti ChangMelissa RestoChang-Soo YunBarbara GerratanaNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Watchalee Chuenchor Tzanko I. Doukov Kai-Ti Chang Melissa Resto Chang-Soo Yun Barbara Gerratana Different ways to transport ammonia in human and Mycobacterium tuberculosis NAD+ synthetases
description	M. tuberculosis NAD+ synthetase (tbNadE) is of interest as a drug target. Here the authors present the actively trapped Homo sapiens NAD+ synthetase (hsNadE) and tbNadE structures and show key differences in the synthetase active site and in structural elements possibly involved in the allosteric regulation of catalysis to be leveraged for the development of M. tuberculosis selective inhibitors.
format	article
author	Watchalee Chuenchor Tzanko I. Doukov Kai-Ti Chang Melissa Resto Chang-Soo Yun Barbara Gerratana
author_facet	Watchalee Chuenchor Tzanko I. Doukov Kai-Ti Chang Melissa Resto Chang-Soo Yun Barbara Gerratana
author_sort	Watchalee Chuenchor
title	Different ways to transport ammonia in human and Mycobacterium tuberculosis NAD+ synthetases
title_short	Different ways to transport ammonia in human and Mycobacterium tuberculosis NAD+ synthetases
title_full	Different ways to transport ammonia in human and Mycobacterium tuberculosis NAD+ synthetases
title_fullStr	Different ways to transport ammonia in human and Mycobacterium tuberculosis NAD+ synthetases
title_full_unstemmed	Different ways to transport ammonia in human and Mycobacterium tuberculosis NAD+ synthetases
title_sort	different ways to transport ammonia in human and mycobacterium tuberculosis nad+ synthetases
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/9040fcaf75534cfa8218a7838eb8215a
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Different ways to transport ammonia in human and Mycobacterium tuberculosis NAD+ synthetases

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