Deoxyribonuclease ii, lysosomal
Deoxyribonuclease II, Lysosomal (also known as DNase II) is an enzyme that catalyzes the hydrolytic cleavage of phosphodiester bonds in DNA molecules, leading to the degradation of DNA. This enzyme is found in the lysosome, a specialized compartment within cells that is involved in the breakdown and recycling of cellular components.
Structure[edit | edit source]
DNase II is a glycoprotein with a molecular weight of approximately 45 kDa. It is composed of two identical subunits, each of which contains a single active site. The active site of DNase II contains two zinc ions, which are essential for its catalytic activity.
Function[edit | edit source]
The primary function of DNase II is to degrade DNA. This enzyme is particularly important in cells that are undergoing apoptosis, a process of programmed cell death. During apoptosis, the DNA in the cell's nucleus is fragmented, and DNase II is one of the enzymes responsible for this fragmentation.
In addition to its role in apoptosis, DNase II is also involved in the immune response. It has been shown to degrade the DNA of invading pathogens, thereby preventing their replication within the cell.
Clinical significance[edit | edit source]
Mutations in the gene encoding DNase II can lead to a number of diseases, including retinitis pigmentosa, a genetic disorder that causes progressive vision loss. In addition, alterations in the activity of this enzyme have been implicated in the development of certain types of cancer.
See also[edit | edit source]
References[edit | edit source]
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Contributors: Prab R. Tumpati, MD