Carboxypeptidase

Definition

Carboxypeptidase is an enzyme that plays a crucial role in the digestion of proteins by breaking down peptides into individual amino acids. This enzyme is secreted by the pancreas into the small intestine, where it acts on the carboxyl end of peptides to release free amino acids, facilitating their absorption into the bloodstream. Carboxypeptidase is essential for ensuring that proteins consumed in the diet are effectively broken down into their building blocks for use by the body.

5 Must Know Facts For Your Next Test

1. Carboxypeptidase is produced in an inactive form called procarboxypeptidase, which is activated by trypsin in the small intestine.
2. The enzyme specifically cleaves off amino acids from the carboxyl terminal end of peptides, which is crucial for protein digestion.
3. Carboxypeptidase can act on both dietary proteins and endogenous proteins, helping to regulate protein turnover in the body.
4. It works alongside other digestive enzymes, such as trypsin and chymotrypsin, to ensure complete protein digestion in the small intestine.
5. Deficiency or dysfunction of carboxypeptidase can lead to malabsorption issues and nutrient deficiencies due to inadequate protein digestion.

Review Questions

• How does carboxypeptidase contribute to protein digestion, and what would be the consequence of its absence in the digestive process?
  • Carboxypeptidase contributes to protein digestion by cleaving amino acids from the carboxyl end of peptides, allowing for their absorption into the bloodstream. Without this enzyme, protein digestion would be incomplete, leading to larger peptides remaining undigested. This could cause malabsorption issues as the body would not be able to effectively utilize dietary proteins, resulting in potential nutrient deficiencies and impaired physiological functions.
• Discuss the activation process of carboxypeptidase and how it fits into the overall digestive enzyme cascade.
  • Carboxypeptidase is initially produced as an inactive precursor called procarboxypeptidase. This precursor is activated in the small intestine by trypsin, another pancreatic enzyme. Once activated, carboxypeptidase works synergistically with other proteases like trypsin and chymotrypsin in a cascade of enzyme activity that efficiently breaks down proteins into absorbable amino acids. This process is crucial for effective digestion and nutrient absorption.
• Evaluate the role of carboxypeptidase within the broader context of nutrient absorption and its impact on metabolic health.
  • Carboxypeptidase plays a vital role in nutrient absorption by ensuring that proteins are broken down into free amino acids that can be easily absorbed by the intestines. This process directly influences metabolic health because amino acids are essential for various bodily functions, including tissue repair, hormone production, and immune function. A deficiency or impairment in carboxypeptidase activity can lead to incomplete protein digestion, resulting in malnutrition or compromised health status due to inadequate supply of these critical building blocks for biological processes.

Related terms

Protease: An enzyme that breaks down proteins into smaller peptides or amino acids through hydrolysis.

Peptidase: An enzyme that specifically catalyzes the hydrolysis of peptide bonds in proteins and peptides.

Amino Acids: The organic compounds that serve as the building blocks of proteins, essential for various biological functions.