Thiocysteine lyases as polyketide synthase domains installing hydropersulfide into natural products and a hydropersulfide methyltransferase

Enzymes installing an intact hydropersulfide (-SSH) group into natural products have so far not been identified. Here, the authors report the characterization of an S-adenosyl methionine-dependent hydropersulfide methyltransferase (GnmP) for guangnanmycin biosynthesis, and identification of three SH...

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Autores principales:	Song Meng, Andrew D. Steele, Wei Yan, Guohui Pan, Edward Kalkreuter, Yu-Chen Liu, Zhengren Xu, Ben Shen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/7e54d45513a14124aa34574274bcc283
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spelling	oai:doaj.org-article:7e54d45513a14124aa34574274bcc2832021-12-02T18:51:16ZThiocysteine lyases as polyketide synthase domains installing hydropersulfide into natural products and a hydropersulfide methyltransferase10.1038/s41467-021-25798-82041-1723https://doaj.org/article/7e54d45513a14124aa34574274bcc2832021-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25798-8https://doaj.org/toc/2041-1723Enzymes installing an intact hydropersulfide (-SSH) group into natural products have so far not been identified. Here, the authors report the characterization of an S-adenosyl methionine-dependent hydropersulfide methyltransferase (GnmP) for guangnanmycin biosynthesis, and identification of three SH domains within several NRPS-PKS assembly lines as thiocysteine lyases.Song MengAndrew D. SteeleWei YanGuohui PanEdward KalkreuterYu-Chen LiuZhengren XuBen ShenNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Song Meng Andrew D. Steele Wei Yan Guohui Pan Edward Kalkreuter Yu-Chen Liu Zhengren Xu Ben Shen Thiocysteine lyases as polyketide synthase domains installing hydropersulfide into natural products and a hydropersulfide methyltransferase
description	Enzymes installing an intact hydropersulfide (-SSH) group into natural products have so far not been identified. Here, the authors report the characterization of an S-adenosyl methionine-dependent hydropersulfide methyltransferase (GnmP) for guangnanmycin biosynthesis, and identification of three SH domains within several NRPS-PKS assembly lines as thiocysteine lyases.
format	article
author	Song Meng Andrew D. Steele Wei Yan Guohui Pan Edward Kalkreuter Yu-Chen Liu Zhengren Xu Ben Shen
author_facet	Song Meng Andrew D. Steele Wei Yan Guohui Pan Edward Kalkreuter Yu-Chen Liu Zhengren Xu Ben Shen
author_sort	Song Meng
title	Thiocysteine lyases as polyketide synthase domains installing hydropersulfide into natural products and a hydropersulfide methyltransferase
title_short	Thiocysteine lyases as polyketide synthase domains installing hydropersulfide into natural products and a hydropersulfide methyltransferase
title_full	Thiocysteine lyases as polyketide synthase domains installing hydropersulfide into natural products and a hydropersulfide methyltransferase
title_fullStr	Thiocysteine lyases as polyketide synthase domains installing hydropersulfide into natural products and a hydropersulfide methyltransferase
title_full_unstemmed	Thiocysteine lyases as polyketide synthase domains installing hydropersulfide into natural products and a hydropersulfide methyltransferase
title_sort	thiocysteine lyases as polyketide synthase domains installing hydropersulfide into natural products and a hydropersulfide methyltransferase
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/7e54d45513a14124aa34574274bcc283
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Thiocysteine lyases as polyketide synthase domains installing hydropersulfide into natural products and a hydropersulfide methyltransferase

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