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Enzymes : - Coggle Diagram
Enzymes :
Enzyme Regulation
Reversible Inhibition: Inhibitor binds temporarily, doesn't permanently attach.
Competitive inhibition: inhibitor bind to active site, blocking substrate. can be out-competed by high substrate concentration.
Regulatory molecules: Activators (increases energy) and Inhbitors (decrease energy) bind specifically to enzymes
Non competitive inhibition: Inhibitor binds to another site (allosteric site) changing enzyme shape. cannot be outcompeted by substrate.
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Cooperativity: substrate itself acts as allosteric activator; binding at one active site increases activity at others.
Cofactors: Non-protein helper molecules required for enzyme activity: can be organic ions or organic molecules, such as Fe or Mg.
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Compartmentalization: Enzymes stored in specific cell compartments,
Feedback Inhibition: end product of a pathway inhibits an upstream enzyme. (usually the first committed step)
prevents overproduction, saves energy.
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Structure and function
catalysts: A substance that speeds up a reaction without being a reactant (as enzymes are biological catalysts)
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Transition state: unstable high-energy state reactants must pass through (enzymes stabilizes this state)
Substrate: The reactant molecule(s) an enzyme binds with. (example: Lactose, substrate for lactase)
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Active site: Region of enzyme where substrate binds (where catalysis happens, forced by specific amino acids)
