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Deoxyribonuclease II (DNase II) is also known as acid deoxyribonuclease because it has optimal activity in the low pH environment of lysosomes where it is typically found in higher eukaryotes. Some forms of recombinant DNase II display a high level of activity in low pH in the absence of divalent metal ions, similar to eukaryotic DNase II. [7]
Type I site-specific deoxyribonuclease (EC 3.1.21.3, type I restriction enzyme, deoxyribonuclease (ATP- and S-adenosyl-L-methionine-dependent), restriction-modification system, deoxyribonuclease (adenosine triphosphate-hydrolyzing), adenosine triphosphate-dependent deoxyribonuclease, ATP-dependent DNase, type 1 site-specific deoxyribonuclease) is an enzyme. [1]
Type II site-specific deoxyribonuclease (EC 3.1.21.4, type II restriction enzyme) is an enzyme. [1] This enzyme catalyses the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'- phosphates .
In biochemistry, an endodeoxyribonuclease is a class of enzyme which is a type of deoxyribonuclease (a DNA cleaver), itself a type of endonuclease (a nucleotide cleaver). They catalyze cleavage of the phosphodiester bonds in DNA. They are classified with EC numbers 3.1.21 through 3.1.25. Examples include: DNA restriction enzymes; micrococcal ...
Type III site-specific deoxyribonuclease (EC 3.1.21.5, type III restriction enzyme, restriction-modification system) is an enzyme. [1] This enzyme catalyses the following chemical reaction Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'- phosphates
New details about a study that warned against black plastic spatulas and other kitchen tools have come out. (Getty Creative) (Анатолий Тушенцов via Getty Images)
Deoxyribonuclease (pyrimidine dimer) (EC 3.1.25.1, endodeoxyribonuclease (pyrimidine dimer), bacteriophage T4 endodeoxyribonuclease V, T4 endonuclease V) is an enzyme. [1] [2] This enzyme catalyses the following chemical reaction: Endonucleolytic cleavage near pyrimidine dimers to products with 5'-phosphate
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