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8.3-8.4

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Termini in questo insieme (20)

  • Energy Coupling

    In cellular metabolism use of energy is released from exergonic reaction to drive an endergonic reaction (ATP)

  • Atp

    Releases free energy when phosphate bonds are hydrolyzed. Energy is used to drive endergonic reactions in cell.

  • How many phosphat groups does atp have

    3

  • Hydrolysis

    When water breaks off the last phosphate group, Atp becomes Adp and releases energy

  • Phosphorylated Intermediate

    A molecule with a phosphate group bound to it. Making it more reactive (less stable) that the UnPhosphorylated Intermediate.

  • Mechanical Work

    Atp binds noncovantly to motor proteins and then is hydrolyzed. Causing shape change that walks the motor protein forward.

  • What do enzymes do in chemical reactions/metabolism

    They make it happen faster by making them easier to start, Without enzyme metabolism would be completely conjested.

  • Activasion Energy

    The amount of energy that reactants must absorb before a chemical reaction can start

  • What happens in chemical reaction

    reactant molecule absorb energy, bonds become unstable , new bonds form, energy released/absorbed

  • Catalysis

    A process by which chemical agent called a catalyst selectively increase the rate of reaction without being consumed by the reaction.

  • Substrat

    The reactant on which enzymes work

  • Enzyme-substract complex

    Temapary complex when enzymes binds to substrate molecules

  • Active site

    Specific Region of an enzyme that binds to the substrat and the pocket in which catalysis occurs.

  • Induced Fit

    Caused by the entry of the substrate, the change in shape of the active site of an enzyme so it binds more better to the substrate

  • Cofactors

    Any Nonprotein molecule on ion that is required for the property function of an enzyme they might be permantly bound to the active site or loosley bound along with a substart durring catalosis.

  • Coenzymes

    Organic molecules serving a cofactor. Most vitamins functions as coenzymes in metabolic reactions.

  • Competitive Inhibitor

    Substance that reduce the activity of an enzynme by entering the active site in place of the substrate, whos structure mimics the substrate

    (allows body to slow down or chill when certain products arent needed)

  • Noncompetitive Inhibitirs

    Attaches somewhere else on enzyme changes the shape so the substate doesnt fit it into it.

    (allows body to slow down or chill when certain products arent needed)

  • PH LEVEL AFEECTS ON ENZYMES

    Too acidic - enzymes shape or chemical properties may change

    Too Base = Enzymes Shape or chemical properties may change

    Optimal Ph- Enzymes work best

  • Temperature effect

    Too. Cold- Molecules move slowly (collide less often) reactions happen slowy

    Optimal temp - Molecules move quickly enough for frequent collisions and enzymes keep working shape

    Too hot- Enzymes can lose its shape, Called denateraction, reaction rates drop .