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15.3J3ASerineProteases.pdf
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Summary

Serine proteases are a family of enzymes that cut peptide bonds in proteins, with a serine residue in their active site. They perform important functions in digestion, blood clotting, and the complement system. Examples include chymotrypsin, trypsin, and elastase, which have similar structures but different substrate specificities. Serine proteases are also involved in blood clotting, with factors such as thrombin and plasmin, and in the complement system, with proteins like C1r and C1s. Serpins are inhibitors of serine proteases, and they work by mimicking the substrate and forming a covalent bond with the protease, leading to its destruction. Deficiencies in serpins can lead to diseases such as alpha-1-antitrypsin deficiency, which can cause emphysema and liver damage, and C1INH deficiency, which can cause hereditary angioedema. Other serine proteases and serpin-like molecules are found in nature, including subtilisin, acetylcholinesterase, and angiotensinogen.

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Serine proteases are a family of enzymes that cut peptide bonds in proteins, with a serine residue in their active site.

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  • File Format: PDF
  • File Size: 83 KB
  • Pages: 4
  • Language: EN
  • Total Downloads: 342
  • Last Updated: 12 hours ago

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