Structural Comparison of <i>Enterococcus faecalis</i> and Human Thymidylate Synthase Complexes with the Substrate dUMP and Its Analogue FdUMP Provides Hints about Enzyme Conformational Variabilities

Structural Comparison of <i>Enterococcus faecalis</i> and Human Thymidylate Synthase Complexes with the Substrate dUMP and Its Analogue FdUMP Provides Hints about Enzyme Conformational Variabilities

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&#8242;-deoxyuridine-5&#8242;-monophosphate (dUMP) using...

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Bibliographic Details
Main Authors: Cecilia Pozzi, Stefania Ferrari, Rosaria Luciani, Giusy Tassone, Maria Paola Costi, Stefano Mangani
Format: Article
Language:English
Published: MDPI AG 2019-03-01
Series:Molecules
Subjects:
thymidylate synthase
<i>Enterococcus faecalis</i>
half-site reactivity
x-ray structure
selectivity
Online Access:https://www.mdpi.com/1420-3049/24/7/1257

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https://www.mdpi.com/1420-3049/24/7/1257

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