Literature summary for 4.2.99.18 extracted from

Kuznetsova, A.A.; Matveeva, A.G.; Milov, A.D.; Vorobjev, Y.N.; Dzuba, S.A.; Fedorova, O.S.; Kuznetsov, N.A.
Substrate specificity of human apurinic/apyrimidinic endonuclease APE1 in the nucleotide incision repair pathway (2018), Nucleic Acids Res., 46, 11454-11465 .

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

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	pre-steady-state kinetic analysis, kinetic analysis of DNA binding, stopped flow measurements, overview	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P27695	-	-

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	human apurinic/apyrimidinic (AP) endonuclease APE1 catalyses the hydrolysis of phosphodiester bonds on the 5'-side of an AP-site (in the base excision repair pathway) and of some damaged nucleotides (in the nucleotide incision repair pathway). The range of substrate specificity includes structurally unrelated damaged nucleotides. Analysis of the mechanism of broad substrate specificity of APE1, overview. Substrate specificity and substrate binding, molecular dynamics simulations. The damaged nucleotide is everted from the DNA helix and placed into the enzyme's binding pocket, which is formed by Asn174, Asn212, Asn229, Ala230, Phe266, and Trp280. Nevertheless, no damage-specific contacts are detected between these amino acid residues in the active site of the enzyme and model damaged substrates containing 1,N6-ethenoadenosine, alpha-adenosine, 5,6-dihydrouridine, or F-site. The substrate specificity of APE1 is controlled by the ability of a damaged nucleotide to flip out from the DNA duplex in response to an enzyme-induced DNA distortion	Homo sapiens	?	-	?

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	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
additional information	substrate specificity and substrate binding, molecular dynamics simulations. Molecular modelling of the APE1 complex with 13 ntDNA duplexes containing 1,N6-ethenoadenosine, alpha-adenosine, 5,6-dihydrouridine or F-site. Model structures of APE1-DNA complexes show that the pocket of the active site is formed by amino acid residues Asn174, Asn212, Asn229, Ala230, Phe266 and Trp280	Homo sapiens
physiological function	most of the biological importance of APE1 in the DNA repair pathways is associated with the high affinity for the abasic nucleotide and nicking of DNA hydrolytically 5' to the AP-site. APE1 has the ability to incise the DNA sugar-phosphate backbone 5' to structurally unrelated lesions such as alpha-anomeric 2'-deoxynucleosides, various red/ox-modified pyrimidines and etheno-adducts	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)