karboxypeptidase

Carboxypeptidase is a class of enzymes that play a crucial role in protein digestion. These enzymes, also known as exopeptidases, function by cleaving amino acids from the carboxyl terminal end of a polypeptide chain. This process liberates individual amino acids, which can then be absorbed and utilized by the body. Carboxypeptidases are synthesized in the pancreas and secreted into the small intestine.

There are several types of carboxypeptidases, broadly categorized into two main groups: carboxypeptidase A and carboxypeptidase B. Carboxypeptidase A primarily cleaves hydrophobic and aromatic amino acids, such as phenylalanine, tyrosine, and tryptophan. Carboxypeptidase B, on the other hand, specifically removes basic amino acids, like arginine and lysine. This specificity ensures that various types of amino acids are released efficiently during digestion.

The activity of carboxypeptidases is essential for obtaining a full complement of amino acids from dietary proteins. Without these enzymes, the body would struggle to break down larger protein molecules into their absorbable building blocks. This can lead to protein malnutrition and other health issues. In addition to their digestive function, some carboxypeptidases are involved in other physiological processes, such as blood coagulation and hormone regulation. The study of carboxypeptidases continues to reveal their diverse roles in biological systems.