Cysteïnproteaser

Cysteïnproteaser, also known as thiolproteases, are a class of enzymes that catalyze the breakdown of proteins by cleaving peptide bonds. Their defining characteristic is the presence of a cysteine residue in their active site, which plays a crucial role in the catalytic mechanism. This cysteine nucleophile attacks the carbonyl carbon of a peptide bond, forming a temporary covalent intermediate.

These enzymes are found in virtually all organisms, from bacteria and viruses to plants and animals, and are involved in a wide array of biological processes. In the human body, cysteïnproteases are essential for protein turnover, cellular debris removal, programmed cell death (apoptosis), and immune system function. They are also implicated in the activation and processing of various proteins, including hormones and signaling molecules.

Dysregulation of cysteïnprotease activity has been linked to numerous diseases. For instance, their overactivity can contribute to the progression of cancer, neurodegenerative disorders like Alzheimer's and Parkinson's disease, and inflammatory conditions. Conversely, a deficiency in certain cysteïnproteases can lead to lysosomal storage diseases.

Due to their critical roles and involvement in disease, cysteïnproteases are important targets for drug development. Inhibitors of specific cysteïnproteases are being investigated and used as therapeutic agents for conditions such as viral infections (e.g., HIV protease inhibitors), cancer, and osteoporosis. The diverse functions and medical relevance of cysteïnproteases make them a subject of ongoing scientific research.