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Article

Role of an invariant lysine residue in folate binding on Escherichia coli thymidylate synthase: calorimetric and crystallographic analysis of the K48Q mutant.

The international journal of biochemistry & cell biology - 1 Jan 2008

Arvizu-Flores Aldo A, Sugich-Miranda Rocio, Arreola Rodrigo, Garcia-Orozco Karina D, Velazquez-Contreras Enrique F, Montfort William R, Maley Frank, Sotelo-Mundo Rogerio R

Abstract excerpt

Thymidylate synthase (TS) catalyzes the reductive methylation of deoxyuridine monophosphate (dUMP) using methylene tetrahydrofolate (CH(2)THF) as cofactor, the glutamate tail of which forms a water-mediated hydrogen bond with an invariant lysine residue of this enzyme. To understand the role of t...

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Identifiers

PMID: 18403248
DOI: 10.1016/j.biocel.2008.02.025
PMCID: PMC2533807

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18403248-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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