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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Homo sapiens |
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 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P27695 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
cell culture | - |
Homo sapiens | - |
HeLa cell | - |
Homo sapiens | - |
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 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 35500, about, SDS-PAGE | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
APE1 | - |
Homo sapiens |
apurinic/apyrimidinic endonuclease 1 | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Homo sapiens |
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 |