Shifting the Hydrolysis Equilibrium of Substrate Loaded Acyl Carrier Proteins.
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
27 08 2019
27 08 2019
Historique:
pubmed:
10
8
2019
medline:
26
6
2020
entrez:
10
8
2019
Statut:
ppublish
Résumé
Acyl carrier proteins (ACP)s transport intermediates through many primary and secondary metabolic pathways. Studying the effect of substrate identity on ACP structure has been hindered by the lability of the thioester bond that attaches acyl substrates to the 4'-phosphopantetheine cofactor of ACP. Here we show that an acyl acyl-carrier protein synthetase (AasS) can be used in real time to shift the hydrolysis equilibrium toward favoring acyl-ACP during solution NMR spectroscopy. Only 0.005 molar equivalents of AasS enables 1 week of stability to palmitoyl-AcpP from
Identifiants
pubmed: 31397556
doi: 10.1021/acs.biochem.9b00612
pmc: PMC7605104
mid: NIHMS1637729
doi:
Substances chimiques
Acyl Carrier Protein
0
Pantetheine
496-65-1
4'-phosphopantetheine
NM39WU8OFM
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
3557-3560Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM031749
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM095970
Pays : United States
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