Serine proteases

Serine proteases (pronounced: /ˈsɛriːn ˈproʊtiːˌeɪz/) are a type of protease that cleave peptide bonds in proteins, in which serine serves as the nucleophilic amino acid at the enzyme's active site. They are found ubiquitously in both eukaryotes and prokaryotes. Serine proteases are involved in a variety of physiological processes, including digestion, immune response, blood coagulation and cell cycle progression.

Etymology

The term "serine protease" comes from "serine", a type of amino acid, and "protease", an enzyme that conducts proteolysis. The name "serine" is derived from sericum, the Latin word for silk, due to its smooth texture. The term "protease" is derived from the Greek words "proteios" meaning "primary" and "ase" meaning "enzyme".

Types of Serine Proteases

There are many types of serine proteases, including trypsin, chymotrypsin, and elastase, which are produced in the pancreas and are involved in digestion. Other serine proteases include thrombin and plasmin, which are involved in blood coagulation and fibrinolysis respectively.

Function

Serine proteases function by cleaving the peptide bonds in proteins, which is a critical process in many biological functions. They are involved in digestion, where they break down dietary proteins into amino acids that can be absorbed and used by the body. In the immune system, serine proteases are involved in the activation of zymogens, which are inactive enzymes that are activated in response to specific signals. In blood coagulation, serine proteases such as thrombin and plasmin play key roles in the formation and dissolution of blood clots.

Related Terms

• Protease
• Peptide bond
• Serine
• Nucleophile
• Eukaryote
• Prokaryote
• Trypsin
• Chymotrypsin
• Elastase
• Thrombin
• Plasmin
• Zymogen
• Amino acid
• Proteolysis

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