Biochemical cascade

A sequence of linked biochemical reactions in which one reaction’s product or signal activates the next, often amplifying a signal or producing a coordinated response.

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Signal transduction: The process by which cells convert an external or internal signal into a specific cellular response. Biochemical cascades are a common architecture for passing signals from receptors to cellular responses.
Enzyme: A biological catalyst that accelerates a chemical reaction without being consumed by it. Enzymes carry out the successive reactions that give biochemical cascades their structure.
Coagulation: The process by which blood forms a clot through coordinated cellular and protein activity. Clotting factors activate one another in a cascade that rapidly builds a fibrin clot.
Metabolic pathway: A series of enzyme-catalyzed reactions that converts starting compounds into products in a cell. Metabolic pathways often process material, whereas cascades commonly propagate activation or information.
Protein phosphorylation: The addition of a phosphate group to a protein, often changing its activity, location, or interactions. Kinase cascades pass activation by phosphorylating downstream proteins.
Substrate (biochemistry): A molecule on which an enzyme acts to produce one or more products. A cascade links products from one reaction to substrates or activators in the next.
Complement system: A network of blood proteins that enhances immune defense by marking microbes, recruiting inflammation, and disrupting membranes. Complement proteins activate successive components to amplify recognition of pathogens.
Gene regulatory network: A system of molecular interactions that controls when and how strongly genes are expressed. Gene networks regulate expression through interacting controls rather than necessarily sequential reaction activation.
Protein kinase: An enzyme that transfers a phosphate group from ATP to a protein substrate. Kinases often activate the next enzyme in a signaling cascade.
Allosteric regulation: Control of a protein’s activity through a molecule binding at a site distinct from its active site. Allosteric switches can relay activation without changing a downstream protein’s abundance.