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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 this interaction, we studied the K48Q mutant of Escherichia coli TS using structural and biophysical methods. The k(cat)...

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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 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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