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

Autor:	Luisa, Moretto, Steven, Vance, Brennan, Heames, R William, Broadhurst
Rok vydání:	2017
Předmět:	Alcohol Oxidoreductases Chemistry Binding Sites Bacterial Proteins Protein Conformation Acyl Carrier Protein Protein Structure Tertiary Substrate Specificity
Zdroj:	Chemical Communications (Cambridge, England)
ISSN:	1364-548X
Popis:	Interaction studies show that KR domains possess a generic binding site for ACP domains and provide evidence that the 5′-phosphopantetheine prosthetic group plays a key role in delivering acyl substrates to the active site in the correct orientation. 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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::60a58962a6f0cb79d126ee5c4750d315 https://pubmed.ncbi.nlm.nih.gov/28980673 Zobrazit plný text záznamu