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Literature summary for 4.2.99.B1 extracted from

  • Bebenek, K.; Tissier, A.; Frank, E.G.; McDonald, J.P.; Prasad, R.; Wilson, S.H.; Woodgate, R.; Kunkel, T.A.
    5'-Deoxyribose phosphate lyase activity of human DNA polymerase iota in vitro (2001), Science, 291, 2156-2159.
    View publication on PubMed
Search for more literature for 4.2.99.B1

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Reaction

Reaction Comment Organism Reaction ID
catalysis of the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site in DNA where a DNA-(apurinic or apyrimidinic site) lyase has already cleaved the C-O-P bond 3' to the apurinic or apyrimidinic site in reactions reconstituted with uracil-DNA glycosylase, apurinic/apyrimidinic endonuclease and ligase I, pol iota can use its dRP lyase and polymerase activities to repair G-U and A-U pairs in DNA, a specialized form of base excision repair, BER. pol iota has an intrinsic dRP lyase activity and the reactions proceeds via beta-elimination involving an active residue containing a primary amine Homo sapiens
a

Synonyms

Synonyms Comment Organism
dRP lyase
-
 Homo sapiens
pol iota with 5'-deoxyribose phosphate lyase activity Homo sapiens
polymerase iota with 5'-deoxyribose phosphate lyase activity Homo sapiens