- DNA endonuclease
- Catalyzes the cleavage of the second DNA phosphodiester backbone 3' to deoxyinosine, leaving a 3'-OH and 5' - phosphate
- Endonuclease V activity, to a lesser extent, is also reported on AP site, urea, mismatches, hairpins, loops, and pseudo-Y structures
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 phosphodiester bonds 3´ to the mismatch of deoxyinosine (2), leaving a nick with 3´-hydroxyl and 5´-phosphate (4).
Product SourceAn 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:
Store at (°C) Concentration NEBuffer™ 4 -20 10 X
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