cysteine-type endopeptidase inhibitor activity

Definition

Target type: molecularfunction

Binds to and stops, prevents or reduces the activity of a cysteine-type endopeptidase. [GOC:dph, GOC:tb]

Cysteine-type endopeptidase inhibitor activity is a molecular function that describes the ability of a molecule to inhibit the activity of cysteine-type endopeptidases. These enzymes are a class of proteases that utilize a cysteine residue in their active site to catalyze the hydrolysis of peptide bonds. Cysteine-type endopeptidases are involved in a wide range of biological processes, including protein degradation, signal transduction, and inflammation. Inhibitors of these enzymes can be used to study their function and to develop drugs for the treatment of various diseases.

The mechanism of inhibition of cysteine-type endopeptidases varies depending on the inhibitor. Some inhibitors bind to the active site of the enzyme and block the access of the substrate. Other inhibitors modify the active site of the enzyme, rendering it inactive. Still others inhibit the enzyme by interacting with its regulatory domains.

Examples of cysteine-type endopeptidase inhibitors include:

- E-64: A potent inhibitor of papain, a cysteine-type endopeptidase that is found in plants.
- Pepstatin A: An inhibitor of aspartic proteases, a class of enzymes that includes pepsin and renin.
- Cysteine protease inhibitors (CPIs): A family of proteins that are found in plants, animals, and fungi. CPIs inhibit the activity of cysteine-type endopeptidases by binding to their active site.

Inhibitors of cysteine-type endopeptidases are being investigated as potential therapeutic agents for a variety of diseases, including cancer, inflammatory diseases, and infectious diseases. For example, inhibitors of cathepsins, a family of cysteine-type endopeptidases that are involved in tumor growth and metastasis, are being studied as potential anticancer drugs.'
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Proteins (4)

Compounds (16)