The Enigma of Substrate Recognition and Catalytic Efficiency of APE1-Like Enzymes.

ABSTRACT: Despite significant achievements in the elucidation of the nature of protein-DNA contacts that control the specificity of nucleotide incision repair (NIR) by apurinic/apyrimidinic (AP) endonucleases, the question on how a given nucleotide is accommodated by the active site of the enzyme remains unanswered. Therefore, the main purpose of our study was to compare kinetics of conformational changes of three homologous APE1-like endonucleases (insect Drosophila melanogaster Rrp1, amphibian Xenopus laevis xAPE1, and fish Danio rerio zAPE1) during their interaction with various damaged DNA substrates, i.e., DNA containing an F-site (an uncleavable by DNA-glycosylases analog of an AP-site), 1,N ⁶-ethenoadenosine (εA), 5,6-dihydrouridine (DHU), uridine (U), o

SUBMITTER: Davletgildeeva AT 

PROVIDER: S-EPMC8033172 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature