Studying the phosphoryl transfer mechanism of the
Journal
Chemical science
ISSN: 2041-6520
Titre abrégé: Chem Sci
Pays: England
ID NLM: 101545951
Informations de publication
Date de publication:
14 Mar 2019
14 Mar 2019
Historique:
received:
07
01
2019
accepted:
24
01
2019
entrez:
19
4
2019
pubmed:
19
4
2019
medline:
19
4
2019
Statut:
epublish
Résumé
Phosphofructokinases (Pfks) catalyze the ATP-dependent phosphorylation of fructose-6-phosphate (F6P) and they are regulated in a wide variety of organisms. Although numerous aspects of the kinetics and regulation have been characterized for Pfks, the knowledge about the mechanism of the phosphoryl transfer reaction and the transition state lags behind. In this work, we describe the X-ray crystal structure of the homodimeric Pfk-2 from
Identifiants
pubmed: 30996866
doi: 10.1039/c9sc00094a
pii: c9sc00094a
pmc: PMC6429617
doi:
Types de publication
Journal Article
Langues
eng
Pagination
2882-2892Références
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