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Literature summary for 4.2.99.18 extracted from

  • Kladova, O.A.; Bazlekowa-Karaban, M.; Baconnais, S.; Pietrement, O.; Ishchenko, A.A.; Matkarimov, B.T.; Iakovlev, D.A.; Vasenko, A.; Fedorova, O.S.; Le Cam, E.; Tudek, B.; Kuznetsov, N.A.; Saparbaev, M.
    The role of the N-terminal domain of human apurinic/apyrimidinic endonuclease 1, APE1, in DNA glycosylase stimulation (2018), DNA Repair, 64, 10-25 .
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
additional information construction of a redox-deficient truncated APE1 protein lacking the first N-terminal 61 amino acid residues (APE1-NDELTA61) the mutant cannot stimulate DNA glycosylase activities of OGG1, MBD4, and ANPG on duplex DNA substrates in contrast to the wild-type enzyme Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information association of APE1 with undamaged DNA reduces effective concentration of the enzyme and subsequently decreases APE1-catalyzed cleavage rates on long DNA substrates Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic analysis of human 8-oxoguanine-DNA glycosylase activation through APE1, overview Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P27695
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information electron microscopy imaging of APE1-DNA complexes reveals oligomerization of APE1 along the DNA duplex and APE1-mediated DNA bridging followed by DNA aggregation. APE1 polymerizes on both undamaged and damaged DNA in cooperative mode. Duplex DNA and diverse oligonucleotides with single base lesion are used as substrates, stopped-flow fluorescence measurements Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
AP endonuclease
-
 Homo sapiens
APE1
-
 Homo sapiens
APEX1
-
 Homo sapiens
apurinic/apyrimidinic endonuclease
-
 Homo sapiens
apurinic/apyrimidinic endonuclease 1
-
 Homo sapiens
HAP-1
-
 Homo sapiens
Ref-1
-
 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
7.6
-
 assay at, endonuclease activity Homo sapiens

General Information

General Information Comment Organism
malfunction the redox-deficient truncated APE1 protein lacking the first N-terminal 61 amino acid residues (APE1-N?61) cannot stimulate DNA glycosylase activities of OGG1, MBD4, and ANPG on duplex DNA substrates Homo sapiens
additional information association of APE1 with undamaged DNA reduces effective concentration of the enzyme and subsequently decreases APE1-catalyzed cleavage rates on long DNA substrates. APE1 oligomers on DNA induce helix distortions thereby enhancing molecular recognition of DNA lesions by DNA glycosylases via a conformational proofreading/selection mechanism. Thus, APE1-mediated structural deformations of the DNA helix stabilize the enzyme-substrate complex and promote dissociation of human DNA glycosylases from the AP site with a subsequent increase in their turnover rate. APE1 shows DNA length dependence with preferential repair of short DNA duplexes. Electron microscopic analysis of DNA complexes with the APE1 protein Homo sapiens
physiological function the base excision repair (BER) pathway consists of sequential action of DNA glycosylase and apurinic/apyrimidinic (AP) endonuclease necessary to remove a damaged base and generate a single-strand break in duplex DNA. Human multifunctional AP endonuclease 1 (APE1) plays essential roles in BER by acting downstream of DNA glycosylases to incise a DNA duplex at AP sites and remove 3'-blocking sugar moieties at DNA strand breaks. Human apurinic/apyrimidinic (AP) endonuclease, APE1, stimulates DNA glycosylases, e.g. human 8-oxoguanine-DNA glycosylase (OGG1), by increasing their turnover rate on duplex DNA substrates, overview. The redox domain of APE1 is necessary for the active mode of stimulation of DNA glycosylases (e.g. of uracil-DNA glycosylase activity of MBD4). Consequently, APE1 shows DNA length dependence with preferential repair of short DNA duplexes. APE1-catalyzed oligomerization along DNA induces helix distortions, which in turn enable conformational selection and stimulation of DNA glycosylases Homo sapiens