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Article

Pre-steady state kinetics of DNA binding and abasic site hydrolysis by tyrosyl-DNA phosphodiesterase 1.

Journal of biomolecular structure & dynamics - 1 Aug 2017

Kuznetsov Nikita A, Lebedeva Natalia A, Kuznetsova Alexandra A, Rechkunova Nadejda I, Dyrkheeva Nadezhda S, Kupryushkin Maxim S, Stetsenko Dmitry A, Pyshnyi Dmitrii V, Fedorova Olga S, Lavrik Olga I

Abstract excerpt

Tyrosyl-DNA phosphodiesterase 1 (Tdp1) processes DNA 3'-end-blocking modifications, possesses DNA and RNA 3'-nucleosidase activity and is also able to hydrolyze an internal apurinic/apyrimidinic (AP) site and its synthetic analogs. The mechanism of Tdp1 interaction with DNA was analyzed using pre-steady state stopped-flow kinetics with tryptophan, 2-aminopurine and Förster resonance energy transfer fluorescence...

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Identifiers

PMID: 27687298
DOI: 10.1080/07391102.2016.1220331

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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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