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Literature summary for 4.2.99.18 extracted from

  • Timofeyeva, N.A.; Koval, V.V.; Knorre, D.G.; Zharkov, D.O.; Saparbaev, M.K.; Ishchenko, A.A.; Fedorova, O.S.
    Conformational dynamics of human AP endonuclease in base excision and nucleotide incision repair pathways (2009), J. Biomol. Struct. Dyn., 26, 637-652.
    View publication on PubMed
Search for more literature for 4.2.99.18

General Stability

General Stability Organism
under base excision repair conditions, the REF1 domain of APE1 influences the stability of both the enzyme-substrate and enzyme-product complexes, as well as the isomerization rate, but does not affect the rates of initial complex formation or catalysis Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
DNA Homo sapiens
-
 fragments of DNA
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA
-
 Homo sapiens fragments of DNA
-
 ?

Synonyms

Synonyms Comment Organism
APE1
-
 Homo sapiens
apurinic-apyrimidinic endonuclease 1
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function APE1 is a multifunctional enzyme that plays a central role in base excision repair of DNA and is also involved in the alternative nucleotide incision repair pathway Homo sapiens