Inner Amino Acid Contacts Are Key Factors of Multistage Structural Rearrangements of DNA and Affect Substrate Specificity of Apurinic/Apyrimidinic Endonuclease APE1.
active-site plasticity
apurinic/apyrimidinic endonuclease
base excision repair
conformational dynamics
damaged nucleotide
nucleotide eversion
nucleotide incision repair
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
14 Jul 2023
14 Jul 2023
Historique:
received:
27
06
2023
revised:
10
07
2023
accepted:
13
07
2023
medline:
31
7
2023
pubmed:
29
7
2023
entrez:
29
7
2023
Statut:
epublish
Résumé
Apurinic/apyrimidinic endonuclease 1 (APE1) is one of the most important enzymes in base excision repair. Studies on this enzyme have been conducted for a long time, but some aspects of its activity remain poorly understood. One such question concerns the mechanism of damaged-nucleotide recognition by the enzyme, and the answer could shed light on substrate specificity control in all enzymes of this class. In the present study, by pulsed electron-electron double resonance (DEER, also known as PELDOR) spectroscopy and pre-steady-state kinetic analysis along with wild-type (WT) APE1 from
Identifiants
pubmed: 37511233
pii: ijms241411474
doi: 10.3390/ijms241411474
pmc: PMC10380840
pii:
doi:
Substances chimiques
DNA-(Apurinic or Apyrimidinic Site) Lyase
EC 4.2.99.18
Amino Acids
0
DNA
9007-49-2
Endonucleases
EC 3.1.-
Nucleotides
0
Deoxyuridine
W78I7AY22C
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Russian Ministry of Science and Higher Education
ID : FWGF-FWGF-2021-0003
Organisme : Russian Ministry of Science and Higher Education
ID : 121031300041-4
Organisme : Russian Science Foundation
ID : 23-44-00064
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