Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates

Interaction studies using fragments excised from the modular mycolactone polyketide synthase show that ketoreductase domains possess a generic binding site for acyl carrier protein domains and provide evidence that the pendant 5′-phosphopantetheine prosthetic group plays a key role in delivering acy...

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Detalles Bibliográficos
Autores principales: Moretto, Luisa, Vance, Steven, Heames, Brennan, Broadhurst, R. William
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2017
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6038798/
https://www.ncbi.nlm.nih.gov/pubmed/28980673
http://dx.doi.org/10.1039/c7cc04625a
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author Moretto, Luisa
Vance, Steven
Heames, Brennan
Broadhurst, R. William
author_facet Moretto, Luisa
Vance, Steven
Heames, Brennan
Broadhurst, R. William
author_sort Moretto, Luisa
collection PubMed
description Interaction studies using fragments excised from the modular mycolactone polyketide synthase show that ketoreductase domains possess a generic binding site for acyl carrier protein domains and provide evidence that the pendant 5′-phosphopantetheine prosthetic group plays a key role in delivering acyl substrates to the active site in the correct orientation.
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spelling pubmed-60387982018-07-26 Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates Moretto, Luisa Vance, Steven Heames, Brennan Broadhurst, R. William Chem Commun (Camb) Chemistry Interaction studies using fragments excised from the modular mycolactone polyketide synthase show that ketoreductase domains possess a generic binding site for acyl carrier protein domains and provide evidence that the pendant 5′-phosphopantetheine prosthetic group plays a key role in delivering acyl substrates to the active site in the correct orientation. Royal Society of Chemistry 2017-10-25 2017-10-05 /pmc/articles/PMC6038798/ /pubmed/28980673 http://dx.doi.org/10.1039/c7cc04625a Text en This journal is © The Royal Society of Chemistry 2017 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0)
spellingShingle Chemistry
Moretto, Luisa
Vance, Steven
Heames, Brennan
Broadhurst, R. William
Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates
title Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates
title_full Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates
title_fullStr Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates
title_full_unstemmed Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates
title_short Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates
title_sort dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6038798/
https://www.ncbi.nlm.nih.gov/pubmed/28980673
http://dx.doi.org/10.1039/c7cc04625a
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