4. Energy and Enzymes Definitions Endergonic: +∆G due to adding free energy (anabolic – make bigger e.g. amino to protein) o Products > Reactants o Not spontaneous Exergonic: - ∆G due to release in free energy (catabolic – breakdown of complex to simple) o Reactants > Products o Spontaneous Activated carrier molecule: Activation energy (Eₔ): The required energy to start a reaction. Leads to transition state (bonds are broken and ready to be broken) and products. Active site: The region of an enzyme that recognizes binds to the substrate o Substrate: Molecule that enzyme catalyzes o Catalysis: Introduction of a catalyst (e.g. enzyme) into a reaction Cofactors: atoms/molecules other than proteins. Some enzymes require this to function. May be inorganic metal ions (e.g., iron, copper, zinc), or organic cofactors/coenzymes (e.g., NAD+, NADP+, vitamin C). e.g., catalase – enzyme that detoxifies free radicals; requires iron cofactor. Inhibitors – prevent substrate from binding to enzyme o Competitive: Inhibitor molecule closely resembling substrate, binds to active site to prevent bonding of substrate o Noncompetitive: Binds to enzyme to alter the shape, preventing bonding of substrate. Enzyme becomes inactive (e.g. poisons) Allosteric inhibition – Molecule binds to allosteric site, leading to stabilization of inactive enzyme Feedback inhibition – Product of a reaction acts as a regulator Metabolism The sum of the chemical reactions on the body Energy released by catabolic reactions is used to power anabolic reactions o E.g. ATP => ADP + Pi (catabolic) => ATP (anabolic) ATP 3 phosphate groups, 1 5-C sugar (ribose) molecule, nucleotide base (adenine) Hydrolysis Reactants: ATP and H2O Products: ADP and inorganic phosphate molecule (Pi) ∆G = -7.3 kcal/mol Enzymes Act as catalysts for biological reactions Decrease Activation Energy Bring substrates closer together Conformational changes and Act as ideal environment