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The DNase enzyme relies on the presence of a divalent cation, which is usually Ca 2+, for proper function. The active site of DNase I includes two histidine residues (His134 and His252) and two acidic residues (Glu78 and Asp 212), all of which are critical for the general acid-base catalysis of phosphodiester bonds. [10]
Deoxyribonuclease II (EC 3.1.22.1, DNase II, pancreatic DNase II, deoxyribonucleate 3'-nucleotidohydrolase, pancreatic DNase II, acid deoxyribonuclease, acid DNase) is an endonuclease that hydrolyzes phosphodiester linkages of deoxyribonucleotide in native and denatured DNA, yielding products with 3'-phosphates and 5'-hydroxyl ends, which occurs as a result of single-strand cleaving mechanism. [1]
Depiction of the restriction enzyme (endonuclease) HindIII cleaving a double-stranded DNA molecule at a valid restriction site (5'–A|AGCTT–3').. In biochemistry, a nuclease (also archaically known as nucleodepolymerase or polynucleotidase) is an enzyme capable of cleaving the phosphodiester bonds that link nucleotides together to form nucleic acids.
13423 Ensembl ENSG00000105612 ENSMUSG00000003812 UniProt O00115 P56542 RefSeq (mRNA) NM_001375 NM_010062 NM_001368295 NM_001368296 RefSeq (protein) NP_001366 NP_001366.1 NP_034192 NP_001355224 NP_001355225 Location (UCSC) Chr 19: 12.88 – 12.88 Mb n/a PubMed search Wikidata View/Edit Human View/Edit Mouse Deoxyribonuclease II, lysosomal is a protein that in humans is encoded by the DNASE2 ...
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