DNA Repair Proteins

DNA Repair Proteins

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APE 1
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.
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Endonuclease IV, E. coli
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
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Fpg, E. coli
Fpg (also known as Formamidopyrimidine DNA glycosylase, Mut M, FAPY DNA Glycosylase, and 8-oxoguanine DNA glycosylase) participates in the base-excision (BER) pathway of DNA repair enzymes and acts both as a N-glycosylase and an AP-lyase. The N-glycosylase activity releases damaged purines from double stranded DNA, generating an apurinic/apyrimidinic (AP site). The AP-lyase activity cleaves both the 3′ and 5′ phosphodiester bonds at the AP site, producing a 1 base gap in the DNA and 3′ and 5′ phosphate termini. Bases recognized and removed by Fpg include 7, 8-dihydro-8-oxoguanine (8-oxoguanine), 8-oxoadenine, fapy-guanine, methy-fapy-guanine, fapy-adenine, aflatoxin B1-fapy-guanine, 5-hydroxy-cytosine and 5-hydroxy-uracil (1,2).
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T4 Endonuclease VII
Modified Enzyme. Ideal for cleaving DNA heteroduplexes on one strand.
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Uracil DNA Glycosylase (UDG)
Uracil-DNA Glycosylase catalyzes the hydrolysis of the N-glycosylic bond between the uracil and sugar, leaving an abasic site in uracil-containing single or double-stranded DNA. The enzyme shows no measurable activity on short oligonucleotides (<6 bases), or RNA substrates.
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