Types of Protease
Amino acids are the building blocks of proteins. Amino acids join together by a link, called a peptide bond, to form chains of polypeptides. Proteins consist countless of peptide bonds.
Various proteases, which are types of enzymes, are needed in the peptide bond formation.
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How It Works
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Our body generates peptide bonds of proteins through a process called hydrolysis (removal of a water molecule). This process usually takes place very slowly, so to make it faster, proteases are added. Proteases act as catalysts to allow cleavage (cutting in specific parts) of proteins in well-defined ways. Note that the residues (R) indicated are those next to where cleavage is most likely to occur.
Trypsin
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These are proteases found in digestive systems of animals. They only cut the protein amino acids lysine and arginine on the R1 site (as shown in the image).
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Thrombin
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This protease is found in the blood. It is an enzyme involved in the coagulation process. Its preferred site to cleave is R1 of the amino acid arginine.
V-8 Protease
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This is an enzyme from Staphylococcus aureus, and its preferred sites to cleave are R1 of aspartic acid and R1 of glutamic acid.
Carboxpeptidase A
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This is another protease found in digestive systems of animals, and it only cleaves R2 of C-terminal amino acid sites.
Thermolysin
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Thermolysin is a protease found in Bacillus thermoprotelyticus, and its preferred site to cleave is R2 leucine, valine, isoleucine and methionine.
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