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Literature summary for 4.2.99.18 extracted from

  • Ilina, E.S.; Khodyreva, S.N.; Lavrik, O.I.
    Unusual interaction of human apurinic/apyrimidinic endonuclease 1 (APE1) with abasic sites via the Schiff-base-dependent mechanism (2018), Biochimie, 150, 88-99 .
    View publication on PubMed
Search for more literature for 4.2.99.18

Protein Variants

Protein Variants Comment Organism
additional information APE1 lacking the first 34 amino acids at the Nterminus, unlike wild-type enzyme, is unable to form cross-links with BS-AP DNAs that testifies to the involvement of disordered N-terminal extension, which is enriched in lysine residues, in the interaction with AP sites. Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens The enzyme cleaves an AP site in DNA via Mg2+-dependent hydrolytic mechanism producing a 5'-deoxyribose phosphate and 3'-hydroxyl and, therefore, the interaction with AP sites via the Schiff base formation, which is characteristic of the beta-elimination mechanism, is not required for APE1 catalytic activity ?
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 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P27695
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-

Source Tissue

Source Tissue Comment Organism Textmining
cell culture
-
 Homo sapiens
-
HeLa cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information The enzyme cleaves an AP site in DNA via Mg2+-dependent hydrolytic mechanism producing a 5'-deoxyribose phosphate and 3'-hydroxyl and, therefore, the interaction with AP sites via the Schiff base formation, which is characteristic of the beta-elimination mechanism, is not required for APE1 catalytic activity Homo sapiens ?
-
 ?
additional information diverse BS-AP DNA duplexes as substrates. Purified recombinant human APE1 is capable of forming the 50 kDa-adducts with efficiency of BS-AP DNAs cross-linking to APE1 being dependent on the mutual orientation of AP sites. Identification of APE1 as a target of cross-linking to BS-AP DNA, and cross-linking of cell extract proteins from HeLa cell cell extract to AP DNA with bistranded AP sites, and AP endonuclease activity of APE1 on BS-AP DNAs, detailed overview Homo sapiens ?
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 ?

Subunits

Subunits Comment Organism
? x * 35500, about, SDS-PAGE Homo sapiens

Synonyms

Synonyms Comment Organism
APE1
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 Homo sapiens
apurinic/apyrimidinic endonuclease 1
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 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Homo sapiens

General Information

General Information Comment Organism
malfunction APE1 lacking the first 34 amino acids at the Nterminus, unlike wild-type enzyme, is unable to form cross-links with BS-AP DNAs that testifies to the involvement of disordered N-terminal extension, which is enriched in lysine residues, in the interaction with AP sites. Homo sapiens
additional information a set of AP DNA duplexes containing AP sites in both strands in different mutual orientation (BS-AP DNAs) is used for search in the extracts of human cells proteins specifically recognizing clustered AP sites Homo sapiens
physiological function APE1 is unable to cleave apurinic/apyrimidinic (AP) sites in spite of formation of the Schiff-base-dependent intermediate, which is prerequisite for the beta-elimination mechanism. Clustered AP sites are more cytotoxic than isolated AP lesions because double strand breaks (DSB) can be formed during repair of closely positioned bistranded AP sites. Formation of DSB due to simultaneous cleavage of bistranded AP sites may be regulated by proteins specifically interacting with this complex lesion Homo sapiens