Deoxyribonuclease endonucleolytic

Deoxyribonuclease I [EC 3.1.21.1], also known as pancreatic DNase and thymonuclease, catalyzes the endonucleolytic cleavage of DNA, preferring dsDNA, to a 5 -phosphodinucleotide and 5 -phosphooligonucleotide end products. 

Type II site-specific deoxyribonuclease [EC 3.1.21.4], also referred to as type II restriction enzyme, catalyzes the endonucleolytic cleavage of DNA to give specific, double-stranded fragments with terminal 5 -phosphates. Magnesium ions are required as cofactors. 

Deoxyribonuclease II [EC 3.1.22.1], also referred to as pancreatic DNase II, catalyzes the endonucleolytic hydrolysis of DNA (preferring double-stranded DNA) to produce 3 -phosphomononucleotide and 3 -phos-phooligonucleotide end products. 

Deoxyribonuclease X [EC 3.1.22.5] catalyzes the endonucleolytic cleavage of supercoiled plasma DNA to linear DNA duplexes. The enzyme exhibits a preference for supercoiled DNA. 

Deoxyribonuclease (pyrimidine dimer) [EC 3.1.25.1] catalyzes the endonucleolytic hydrolysis of a bond in DNA near pyrimidine dimers to generate products with 5 -phosphates. The enzyme acts on damaged strands of DNA, 5 from the damaged site. 

Deoxyribonuclease I, DNase I (EC 3.1.21.1) an enzyme (normally obtained from bovine pancreas and therefore also known as pancreatic deoxyribonuclease) which catalyses random endonucleolytic cleavage of intemucleotide bonds of double-stranded DNA, preferentially but not exclusively between adjacent purines and pyrimidines, producing S -phos-phodi- and -oligonucleotides. 

Deoxyribonuclease II, DNase H, pancreatic DNase II, acid DNase, calf thymus attid DNase, spleen acid DNase (EC 3.1.22.1) a monomeric enzyme (M, 31,(XK>) which catalyses the endonucleolytic cleavage of double stranded DNA to 3 -phosphomononu-cleotides and 3 -phosphooligonucleotides The earliest definitive studies were performed on the enzyme from hog spleen, which became known simply as hog-spleen enzyme . But the enzyme (or enzymes with extremely amilar properties) is widely distributed in animal cells, including, e.g. human pancreas, thymus, liver, gastric mucosa and cervix, as well as crab testis, snails and salmon testis. Although optimal activity occurs at pH 4-S, this optimum is not sharply defined, and considerable activity is retained even at neutral pH. 

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