deoxyribonuclease I activity

Definition

Target type: molecularfunction

Catalysis of the endonucleolytic cleavage of DNA to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end products. [EC:3.1.21.1]

Deoxyribonuclease I (DNase I) activity is a critical molecular function that involves the hydrolysis of phosphodiester bonds within DNA molecules. This enzymatic activity plays a crucial role in various cellular processes, including DNA repair, recombination, and apoptosis. Specifically, DNase I cleaves DNA at specific sites, generating double-stranded breaks with 5'-phosphorylated and 3'-hydroxyl termini. Its preference for cleaving DNA at the phosphodiester bond between a purine base and a pyrimidine base, particularly at the 5'-end of a pyrimidine, contributes to its specificity. The enzyme can act on both single-stranded and double-stranded DNA, although its activity is generally higher on single-stranded DNA. The catalytic mechanism involves the coordination of a divalent metal ion, typically magnesium, by the active site of the enzyme. This metal ion facilitates the nucleophilic attack of a water molecule on the phosphodiester bond, leading to hydrolysis and the breakage of the DNA strand. DNase I activity is tightly regulated within cells, ensuring that DNA degradation occurs in a controlled manner and only when necessary. This regulation is achieved through various factors, including the availability of substrate, the presence of cofactors, and the activity of regulatory proteins. Dysregulation of DNase I activity can have significant implications for cellular function, potentially contributing to various diseases. For example, mutations in the DNase I gene have been linked to immunodeficiency disorders, while aberrant DNase I activity has been implicated in cancer development and autoimmune diseases.'
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Proteins (1)

Compounds (2)