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Article

A remote mutation affects the hydride transfer by disrupting concerted protein motions in thymidylate synthase.

Journal of the American Chemical Society - 24 Oct 2012

Wang Zhen, Abeysinghe Thelma, Finer-Moore Janet S, Stroud Robert M, Kohen Amnon

Abstract excerpt

The role of protein flexibility in enzyme-catalyzed activation of chemical bonds is an evolving perspective in enzymology. Here we examine the role of protein motions in the hydride transfer reaction catalyzed by thymidylate synthase (TSase). Being remote from the chemical reaction site, the Y209W mutation of Escherichia coli TSase significantly reduces the protein activity, despite the remarkable similarity...

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Identifiers

PMID: 23034004
DOI: 10.1021/ja307859m
PMCID: PMC3490427

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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