Proteolysis

Proteolysis is the breakdown of proteins into peptides and amino acids by enzymes or microorganisms. It regulates protein turnover and supports digestion, cellular signaling, and nutrient recycling.

Protease: An enzyme that hydrolyzes peptide bonds in proteins or peptides. Proteases catalyze most enzymatic proteolysis by cutting specific peptide bonds.
Protein digestion: The enzymatic breakdown of dietary proteins into absorbable peptides and amino acids. Digestive proteolysis makes food proteins available for absorption.
Protein: A biological macromolecule composed of one or more chains of amino acids. Proteins are the substrates whose chains proteolysis cleaves.
Protein synthesis: The cellular process of assembling proteins from amino acids according to genetic information. It builds protein chains, opposing the degradative direction of proteolysis.
Peptide bond: The covalent bond linking amino acids in peptides and proteins. Proteolysis breaks peptide bonds to fragment protein chains.
Proteasome: A large protein complex that degrades proteins marked for destruction inside cells. The proteasome is a major machine for regulated intracellular proteolysis.
Peptide: A molecule made of a short chain of amino acids linked by peptide bonds. Peptides are common intermediate products of protein breakdown.
Protein denaturation: The loss of a protein's native structure without necessarily breaking its peptide bonds. Denaturation unfolds proteins but is distinct from enzymatic chain cleavage.
Protease catalytic mechanism: The chemical strategies proteases use to cleave peptide bonds, including acid–base catalysis and covalent intermediates. Different catalytic strategies explain how proteases carry out the same bond-breaking reaction.
Apoptosis: A regulated form of cell death involving orderly cellular dismantling. Proteolytic cascades execute and regulate many steps of apoptosis.

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