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Article

The role of protein dynamics in thymidylate synthase catalysis: variants of conserved 2'-deoxyuridine 5'-monophosphate (dUMP)-binding Tyr-261.

Biochemistry - 20 Jun 2006

Newby Zachary, Lee Tom T, Morse Richard J, Liu Yaoquan, Liu Lu, Venkatraman Prasanna, Santi Daniel V, Finer-Moore Janet S, Stroud Robert M

Abstract excerpt

The enzyme thymidylate synthase (TS) catalyzes the reductive methylation of 2'-deoxyuridine 5'-monophosphate (dUMP) to 2'-deoxythymidine 5'-monophosphate. Using kinetic and X-ray crystallography experiments, we have examined the role of the highly conserved Tyr-261 in the catalytic mechanism of TS. While Tyr-261 is distant from the site of methyl transfer, mutants at this position show a marked decrease in...

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Identifiers

PMID: 16768437
DOI: 10.1021/bi060152s
PMCID: PMC2556892

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Source receipt: pubmed, retrieved 7 Sept 2026.

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