The role of His-83 of yeast apurinic/apyrimidinic endonuclease Apn1 in catalytic incision of abasic sites in DNA.

doi:10.1016/j.bbagen.2015.03.001

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Article

The role of His-83 of yeast apurinic/apyrimidinic endonuclease Apn1 in catalytic incision of abasic sites in DNA.

Biochimica et biophysica acta - 1 Jun 2015

Dyakonova Elena S, Koval Vladimir V, Lomzov Alexander A, Ishchenko Alexander A, Fedorova Olga S

Abstract excerpt

BACKGROUND: The apurinic/apyrimidinic (AP) endonuclease Apn1 from Saccharomyces cerevisiae is a key enzyme involved in the base excision repair (BER) at the cleavage stage of abasic sites (AP sites) in DNA. The crystal structure of Apn1 from S. cerevisiae is unresolved. Based on its high amino acid homology to Escherichia coli Endo IV, His-83 is believed to coordinate one of three Zn2+ ions in Apn1's active site...

Topics

Amino Acid Sequence
Catalysis
Catalytic Domain
DNA Repair
DNA Repair Enzymes
DNA, Fungal
Endodeoxyribonucleases
Histidine
Kinetics
Molecular Dynamics Simulation
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Nucleic Acid Conformation

Protein Conformation

Saccharomyces cerevisiae

Saccharomyces cerevisiae Proteins

Zinc

Source

Open in PubMed

Identifiers

PMID: 25766873
DOI: 10.1016/j.bbagen.2015.03.001

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