Energy, Enzymes, & Cellular Work (Ch.5 Pt.2)
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Kinetic energy is the energy of motion, including thermal energy which is the random movement of atoms or molecules.
Potential energy is stored energy based on location or structure. Chemical energy is potential energy available for release in chemical reactions.
Energy can change form but cannot be created or destroyed; it is conserved.
Energy transfers increase disorder (entropy), and some energy is lost as heat.
Exergonic reactions release energy; endergonic reactions require energy input.
ATP stores and releases energy by hydrolyzing its phosphate bonds, coupling exergonic and endergonic reactions.
Activation energy is the energy barrier that must be overcome for a reaction to proceed.
Enzymes lower the activation energy, speeding up chemical reactions without being consumed.
The active site is the specific region on an enzyme where the substrate binds.
The active site changes shape slightly to better fit the substrate, stressing bonds and lowering activation energy.
Temperature, pH, substrate concentration, and presence of cofactors or inhibitors affect enzyme effectiveness.
High temperatures can denature enzymes, changing their 3D shape and rendering them inactive.
Competitive inhibitors block the active site; non-competitive inhibitors bind elsewhere, changing enzyme shape.
Feedback inhibition occurs when the product of a metabolic pathway inhibits an enzyme to regulate the pathway.
Because of the activation energy barrier that prevents spontaneous reactions without enzymes.
Increasing substrate concentration increases reaction rate until enzymes become saturated.
Cofactors are inorganic ions; coenzymes are organic molecules that assist enzyme function.
Penicillin blocks the active site of bacterial enzymes needed for cell wall synthesis, killing bacteria.
Energy from glucose is converted into ATP, which powers cellular work, with some energy lost as heat.
ATP hydrolysis releases energy by breaking phosphate bonds, driving endergonic cellular processes.