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Literature summary for 4.2.99.18 extracted from

  • Kuznetsova, A.A.; Fedorova, O.S.; Kuznetsov, N.A.
    Kinetic features of 30-50 exonuclease activity of human AP-endonuclease APE1 (2018), Molecules, 23, E2101 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.2.99.18

Cloned(Commentary)

Cloned (Comment) Organism
recombinant enzyme expression in Escherichia coli strain Rosetta II(DE3) Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information analysis of enzyme activity and kinetics with DNA substrates comprising duplexes of deoxyribonucleotides with one 5'-dangling end that contain a fluorescent 2-aminopurine residue at the 1st, 2nd, 4th, or 6th position from the 3'-end of the short oligonucleotide. The impact of the 3'-end nucleotide, which contains mismatched, undamaged bases or modified bases as well as an abasic site or phosphate group, on the efficiency of 3'-5'-exonuclease activity is determined Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic mechanism of 3'-end nucleotide removal in the 3'-5'-exonuclease process catalyzed by APE1 under pre-steady-state conditions, interaction of enzyme APE1 with DNA containing an abasic site, overview Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P27695
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain Rosetta II(DE3) Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information analysis of enzyme activity and kinetics with DNA substrates comprising duplexes of deoxyribonucleotides with one 5'-dangling end that contain a fluorescent 2-aminopurine residue at the 1st, 2nd, 4th, or 6th position from the 3'-end of the short oligonucleotide. The impact of the 3'-end nucleotide, which contains mismatched, undamaged bases or modified bases as well as an abasic site or phosphate group, on the efficiency of 3'-5'-exonuclease activity is determined. The rate-limiting step of 3'-nucleotide removal by APE1 in the 3'-5'-exonuclease process is the release of the detached nucleotide from the enzyme's active site. Exonuclease activity of APE1 is effective toward duplexes containing gaps or 5'-dangling ends. For the kinetic analysis of the 3'-5'-exonuclease reaction, the duplexes of 15 and 28 nucleotides (nt) with a 5'-dangling end served as model DNA substrates Homo sapiens ?
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 ?

Synonyms

Synonyms Comment Organism
AP-endonuclease
-
 Homo sapiens
APE1
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 Homo sapiens
apurinic/apyrimidinic-endonuclease
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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
7.5
-
 assay at Homo sapiens

General Information

General Information Comment Organism
physiological function APE1 is one of the key enzymes taking part in the repair of damage to DNA. The primary role of APE1 is the initiation of the repair of AP-sites by catalyzing the hydrolytic incision of the phosphodiester bond immediately 5' to the damage. In addition to the AP-endonuclease activity, APE1 possesses 3'-5'-exonuclease activity, which presumably is responsible for cleaning up nonconventional 3'-ends that were generated as a result of DNA damage or as transition intermediates in DNA repair pathways Homo sapiens