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The AP endonuclease recognizes this sugar and essentially cuts the DNA at this site and then allows for DNA repair to continue. [10] E. coli cells contain two AP endonucleases: endonuclease IV (endoIV) and exonuclease III (exoIII) while in eukaryotes, there is only one AP endonuclease. [11]
A restriction enzyme, restriction endonuclease, REase, ENase or restrictase is an enzyme that cleaves DNA into fragments at or near specific recognition sites within molecules known as restriction sites.
The protein is a member of the XPG/RAD2 endonuclease family and is one of ten proteins essential for cell-free DNA replication. DNA secondary structure can inhibit flap processing at certain trinucleotide repeats in a length-dependent manner by concealing the 5' end of the flap that is necessary for both binding and cleavage by the protein ...
Nuclease S1 (EC 3.1.30.1) is an endonuclease enzyme that splits single-stranded DNA (ssDNA) and RNA into oligo- or mononucleotides. This enzyme catalyses the following chemical reaction. Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products
A nicking enzyme (or nicking endonuclease) is an enzyme that cuts only one strand of a double-stranded DNA or RNA molecule [1] at a specific recognition nucleotide sequence known as the restriction site. Such enzymes hydrolyze (cut) only one strand of the DNA duplex, to produce DNA molecules that are “nicked”, rather than cleaved. [2] [3]
The endonuclease activity of FENs was initially identified as acting on a DNA duplex which has a single-stranded 5' overhang on one of the strands [4] (termed a "5' flap", hence the name flap endonuclease [5]). FENs catalyse hydrolytic cleavage of the phosphodiester bond at the junction of single- and double-stranded DNA. [6]
In molecular biology, enzymes in the DNA/RNA non-specific endonuclease family of bacterial and eukaryotic endonucleases EC 3.1.30.-share the following characteristics: they act on both DNA and RNA, cleave double-stranded and single-stranded nucleic acids and require a divalent ion such as magnesium for their activity.
Uracil DNA glycosylase flips a uracil residue out of the duplex, shown in yellow. DNA glycosylases are responsible for initial recognition of the lesion. They flip the damaged base out of the double helix, as pictured, and cleave the N-glycosidic bond of the damaged base, leaving an AP site. There are two categories of glycosylases ...