- per page
APE 1, also known as HAP 1 or Ref-1, acts as an AP lyase by hydrolyzing the phosphodiester backbone at the 5′ end of an apurinic (AP) site, generating a 1 base gap in the DNA duplex and leaving 3′-hydroxyl and 5′-deoxyribose phosphate termini.
a class II apurinic/apyrimidic (AP) enzyme that cleaves 5’ to an AP site by hydrolysis leaving a hydroxyl group at the 3´ terminus and a deoxyribose 5´-phosphate at the 5´ terminus
E.coli Endonuclease VIII functions as both an N-glycosylase (by excising oxidative base lesions) and an AP lyase (by subsequently cleaving the phosphodiester backbone), leaving terminal phosphates at the 5′ and 3′ ends.
The enzyme has DNA glycosylase and apurinic/apyrimidinic lyase (AP lyase) activity.
Modified Enzyme. Ideal for cleaving DNA heteroduplexes on one strand.
Topoisomerase I, derived from Vaccinia virus, is a type I eukaryotic topoisomerase that removes both positive and negative superhelical turns (also called right- and left-handed supercoils) from covalently closed DNA. The product of the reaction is a covalently closed, circular DNA with fewer positive or negative superhelical turns. DNA Topoisomerase I does not absolutely require Mg2+ to function, although low concentrations of Mg2+ may increase activity. Ideal for relax positively and negatively supercoiled DNA in presence of EDTA.
- per page
