Structural Comparison of
Binding Sites
Catalytic Domain
Enterococcus faecalis
/ enzymology
Fluorodeoxyuridylate
/ chemistry
Humans
Models, Molecular
Protein Binding
Protein Conformation
Protein Multimerization
Structure-Activity Relationship
Substrate Specificity
Thymidine Monophosphate
/ chemistry
Thymidylate Synthase
/ chemistry
Enterococcus faecalis
half-site reactivity
selectivity
thymidylate synthase
x-ray structure
Journal
Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009
Informations de publication
Date de publication:
31 Mar 2019
31 Mar 2019
Historique:
received:
11
03
2019
revised:
22
03
2019
accepted:
28
03
2019
entrez:
3
4
2019
pubmed:
3
4
2019
medline:
20
7
2019
Statut:
epublish
Résumé
Thymidylate synthase (TS) is an enzyme of paramount importance as it provides the only de novo source of deoxy-thymidine monophosphate (dTMP). dTMP, essential for DNA synthesis, is produced by the TS-catalyzed reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) using N⁵,N
Identifiants
pubmed: 30935102
pii: molecules24071257
doi: 10.3390/molecules24071257
pmc: PMC6479881
pii:
doi:
Substances chimiques
Fluorodeoxyuridylate
134-46-3
Thymidine Monophosphate
365-07-1
Thymidylate Synthase
EC 2.1.1.45
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
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