Inter-Active Site Communication Mediated by the Dimer Interface β-Sheet in the Half-the-Sites Enzyme, Thymidylate Synthase.
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
30 07 2019
30 07 2019
Historique:
pubmed:
10
7
2019
medline:
27
5
2020
entrez:
9
7
2019
Statut:
ppublish
Résumé
Thymidylate synthase (TS) is a dimeric enzyme conserved in all life forms that exhibits the allosteric feature of half-the-sites activity. Neither the reason for nor the mechanism of this phenomenon is understood. We used a combined nuclear magnetic resonance (NMR) and molecular dynamics approach to study a stable intermediate preceding hydride transfer, which is the rate-limiting and half-the-sites step. In NMR titrations with ligands leading to this intermediate, we measured chemical shifts of the apoenzyme (lig
Identifiants
pubmed: 31283187
doi: 10.1021/acs.biochem.9b00486
pmc: PMC7110413
mid: NIHMS1566049
doi:
Substances chimiques
Thymidylate Synthase
EC 2.1.1.45
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
3302-3313Subventions
Organisme : NCI NIH HHS
ID : P30 CA016086
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM083059
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM123247
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM127698
Pays : United States
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