Ribonuclease: Difference between revisions
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Latest revision as of 21:04, 23 February 2025
Ribonuclease (RNase) is a type of enzyme that catalyzes the degradation of RNA into smaller components. RNases can be categorized into endoribonucleases and exoribonucleases, and comprise several sub-classes within the EC 2.7 (translocases) and EC 3 (hydrolases) classes of enzymes recognized by the International Union of Biochemistry and Molecular Biology.
Function[edit]
Ribonucleases perform several important roles in RNA metabolism, including the degradation of RNA molecules as part of the cell's metabolism, the generation of nucleotides for the cell, and the regulation of gene expression.
Types[edit]
There are several types of RNases, including:
- Ribonuclease A, a pancreatic RNase that serves to degrade dietary RNA
- Ribonuclease H, an RNase that recognizes and cleaves the RNA in RNA-DNA hybrids
- Ribonuclease III, an RNase that cleaves double-stranded RNA
- Ribonuclease P, an RNase involved in generating tRNA molecules from larger, precursor molecules
- Ribonuclease T1, an RNase that cleaves single-stranded RNA
Inhibitors[edit]
Ribonuclease inhibitors are proteins that bind to ribonucleases and inhibit their activity. They are important for controlling the activity of ribonucleases in the cell and preventing unwanted RNA degradation.
See also[edit]
References[edit]
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