EC Number   |
Reaction |
Reference |
|---|
   4.2.99.B1 | 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 |
concerted reaction of dRP lyase and DNA polymerization of Li Polbeta on a uracil-containing DNA participating in single-nucleotide base excision repair (BER), beta-elimination reaction |
692012 |
| 4.2.99.B1 | 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 |
DNA polymerase beta (Pol beta) catalyzes both DNA synthesis at the 3'-hydroxyl terminus and esxcision of 5'-dRP moiety prior to completion of the base excsion repair (BER) by DNA ligase |
692974 |
| 4.2.99.B1 | 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 |
DNA polymerase beta as the major polymerase involved in repair of oxidative base lesions, in single nucleotide replacement mechanisms. The 5'-deoxyribosephosphate lyase activity of Pol beta is essential for repair |
692064 |
| 4.2.99.B1 | 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 |
enzyme cleaves 3' to apurinic/apyrimidinic sites and is capable of removing 5' dRP residues at sites that mimic preincision with AP endonuclease. The activity of UL30 on the preincised and nicked substrates ist significantly greater than observed on apurinic/apyrimidinic DNA. These activities are integral to base excision repair and lead to DNA cleavage on 3' side on abasic sites and 5'-dRP residues that remain after cleavage by 5'-AP endonuclease, via beta-elimination forming a Schiff base intermediate |
694866 |
| 4.2.99.B1 | 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 |
enzyme is involved in single-nucleotide base excision DNA repair, SN-BER |
694467 |
| 4.2.99.B1 | 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 |
homologous to the dRP lyase activity of polymerase beta, pol beta. Proposed to participate in single-nucleotide base excision repair in mammalian cells, which is the major repair pathway in eukaryotic cells responsible for repair of lesions that give rise to abasic siles in DNA |
692957 |
| 4.2.99.B1 | 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 |
695130 |
| 4.2.99.B1 | 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 |
NEIL1 and NEIL2 are capable of removing 2-deoxyribose 5-phosphate from DNA with the effiency comparable to that of Polbeta, and they can substitute for Polbeta dRPase activity in a reconstituted base excision repair (BER) system |
692334 |
| 4.2.99.B1 | 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 |
reaction is part of the DNA base excision repair BER, enzyme releases 5'-terminal deoxyribose phosphate from preincised apurinic/apyrimidinic site DNA by beta-elimination |
692941 |
| 4.2.99.B1 | 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 |
removal of the 5'-deoxyribose phosphate group is a pivotal step in the base excision repair (BER) pathway in vivo.Two important enzymatic steps in mammalian single-nucleotide base excision repair are contributed by beta-pol: DNA resynthesis of the repair patch und lyase removal of 5'-deoxyribose phosphate |
694332 |
