Carboxypeptidase

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Carboxypeptidase

Carboxypeptidase (pronounced: kar-bok-see-PEP-ti-days) is a type of enzyme that catalyzes the hydrolytic removal of amino acid residues from the carboxyl end of proteins or peptides.

Etymology

The term "Carboxypeptidase" is derived from the words "carboxyl", referring to the carboxyl group (-COOH) in organic chemistry, and "peptidase", which is a type of enzyme that breaks down peptides.

Function

Carboxypeptidases function in the digestion of proteins and peptides in the gastrointestinal tract, where they are secreted as zymogens by the pancreas. They are also involved in the process of protein catabolism in the cytosol.

Types

There are several types of carboxypeptidases, including:

  • Carboxypeptidase A: This enzyme specifically removes aromatic or aliphatic amino acids from proteins and peptides.
  • Carboxypeptidase B: This enzyme specifically removes basic amino acids from proteins and peptides.
  • Carboxypeptidase N: This enzyme is a regulatory enzyme that modulates the activity of peptide hormones and growth factors.

Related Terms

  • Enzyme: A protein that acts as a biological catalyst to speed up a chemical reaction.
  • Amino Acid: The building blocks of proteins.
  • Protein: A large molecule composed of one or more chains of amino acids in a specific order.
  • Peptide: A short chain of amino acids.
  • Pancreas: A glandular organ in the digestive system and endocrine system of vertebrates.
  • Protein Catabolism: The breakdown of proteins into amino acids and simple derivative compounds.

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