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Literature summary for 4.2.99.18 extracted from
- Interaction of APE1 and other repair proteins with DNA duplexes imitating intermediates of DNA repair and replication (2008), Biochemistry (Moscow), 73, 261-272.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| human X-ray repair cross-complementing group 1 protein | stimulates APendonuclease and 3'-phosphodiesterase activities of APE1 and increases efficiency of 3'-5'-exonuclease excision of the match as well as noncanonical pairs by APE1 | Mus musculus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant production of APE1 | Mus musculus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| human X-ray repair cross-complementing group 1 protein (XRCC1) | at high XRCC1 concentrations, inhibition of APE1 exonuclease activity is observed | Mus musculus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| K+ | 25 mM included in assay medium. DNA structures with a nick and DNArec used for photoaffinity modification are substrates for APE1 3'-5'-exonuclease activity, that is more efficient at decreased salt concentrations. | Mus musculus |  |
| Mg2+ | 2 mM included in assay medium | Mus musculus | |
| Mn2+ | In order to cleave phosphodiester bonds in the course of endonuclease and exonuclease reactions catalyzed by APE1, Mg2+ or Mn2+ is needed | Mus musculus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 37000 | - |
calculated and affirmed by immunoprecipitation | Mus musculus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Mus musculus | APE1 binds with the highest efficiency to DNA substrate containing 5'-sugar phosphate group in the nick/gap | ? | - |
? | |
| additional information | Mus musculus | APE1 exhibits 3'-phosphodiesterase, 3'-phosphatase, and 3'-5'-exonuclease activities | ? | - |
? | |
| additional information | Mus musculus | APE1 is one of the candidates for the role of base excision repair (BER) pathway coordinator, which controls the whole process. APE1 participates in stimulation of activity of BER enzymes | ? | - |
? | |
| additional information | Mus musculus | APE1 stimulates DNA synthesis catalyzed by DNA polymerase beta, and a human Xray repair cross-complementing group 1 protein stimulates APE1 3'-5'-exonuclease activity on 3'-recessed DNA duplex | ? | - |
? | |
| additional information | Mus musculus | DNA with the recessed 3'-end (DNArec) is one of the preferential substrates for APE1 3'-5'-exonuclease activity | ? | - |
? | |
| additional information | Mus musculus | enzyme cleaves the DNA sugar phosphate backbone at the 5'-position in relation to the AP site, forming a nick with the hydroxyl group at the 3'-end and deoxyribose phosphate at the 5'-end | ? | - |
? | |
| additional information | Mus musculus | high APE1 affinity to dsDNA | ? | - |
? | |
| additional information | Mus musculus | When APE1 and DNA polymerase beta are both present, a ternary complex APE1-DNA polymerase beta-DNA is formed with the highest efficiency with DNA product of APE1 endonuclease activity and with DNA containing 5'-flap or mononucleotide-gapped DNA with 5'-p group | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| purification of recombinant enzyme | Mus musculus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| MEF cell | embryonic fibroblast cell | Mus musculus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
APE1 exonuclease activity | Mus musculus |
| additional information | - |
APE1 is most efficiently (5% yield) modified by DNA substrate bearing the 5'-pF group (DNAFAP-pF), which flanks a nick. This DNA structure is a model of a short-patch BER intermediate or a long-patch BER product and is an analog of the product of endonuclease or substrate of the exonuclease APE1 activity | Mus musculus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | APE1 binds with the highest efficiency to DNA substrate containing 5'-sugar phosphate group in the nick/gap | Mus musculus | ? | - |
? | |
| additional information | APE1 exhibits 3'-phosphodiesterase, 3'-phosphatase, and 3'-5'-exonuclease activities | Mus musculus | ? | - |
? | |
| additional information | APE1 is one of the candidates for the role of base excision repair (BER) pathway coordinator, which controls the whole process. APE1 participates in stimulation of activity of BER enzymes | Mus musculus | ? | - |
? | |
| additional information | APE1 stimulates DNA synthesis catalyzed by DNA polymerase beta, and a human Xray repair cross-complementing group 1 protein stimulates APE1 3'-5'-exonuclease activity on 3'-recessed DNA duplex | Mus musculus | ? | - |
? | |
| additional information | DNA with the recessed 3'-end (DNArec) is one of the preferential substrates for APE1 3'-5'-exonuclease activity | Mus musculus | ? | - |
? | |
| additional information | enzyme cleaves the DNA sugar phosphate backbone at the 5'-position in relation to the AP site, forming a nick with the hydroxyl group at the 3'-end and deoxyribose phosphate at the 5'-end | Mus musculus | ? | - |
? | |
| additional information | high APE1 affinity to dsDNA | Mus musculus | ? | - |
? | |
| additional information | When APE1 and DNA polymerase beta are both present, a ternary complex APE1-DNA polymerase beta-DNA is formed with the highest efficiency with DNA product of APE1 endonuclease activity and with DNA containing 5'-flap or mononucleotide-gapped DNA with 5'-p group | Mus musculus | ? | - |
? | |
| additional information | APE1 most efficiently binds to DNA substrate bearing tetrahydrofuran in the middle of one of the strands (AP-dsDNA) | Mus musculus | ? | - |
? | |
| additional information | for APE1 in MEF extract, efficiency of formation of protein-DNA crosslinking changes depending on the nature of 5'-group flanking the nick in DNA structure: DNAFAP-pF (100%), DNAFAP-OH (68.2%), DNAFAP-flap (54.6%), DNAFAP-gap (44.2%), DNAFAP-rec (41.3%), DNAFAP-p (41.1%) | Mus musculus | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AP endonuclease 1 | - |
Mus musculus |
| APE1 | - |
Mus musculus |
| human apurinic/apyrimidinic endonuclease 1 | - |
Mus musculus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Mus musculus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Mus musculus |
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