Endonuclease V is a repair enzyme found in E. coli that recognizes deoxyinosine, a deamination product of deoxyadenosine in DNA. Endonuclease V, often called deoxyinosine 3´ endonuclease, recognizes DNA containing deoxyinosines (paired or not) on double-stranded DNA, single-stranded DNA with deoxyinosines and to a lesser degree, DNA containing abasic sites (ap) or urea, base mismatches, insertion/deletion mismatches, hairpin or unpaired loops, flaps and pseudo-Y structures. It is believed that Endonuclease V needs another protein to repair the DNA, as it does not remove the deoxyinsoine or the damaged bases (1,2,3).
Endonuclease V cleaves the second and third phosphodiester bonds 3´ to the mismatch of deoxyinosine with a 95% efficiency for the second bond and a 5% efficiency for the third bond (2), leaving a nick with 3´-hydroxyl and 5´-phosphate (4).
- Isolated from a recombinant source
- Supplied with 10X Reaction Buffer
An E. coli strain containing a gene fusion of the Endo V gene and the gene coding for the maltose binding protein (MBP). The fusion protein is purified to near homogeneity and is active as a fusion. The protein contains 223 amino acids and has a molecular weight of 24.9 kDa (5).
The following reagents are supplied with this product:
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