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Exam 1

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Termini in questo insieme (20)

  • What are oxidation-reduction (redox) reactions in microbial metabolism?

    Redox reactions involve the transfer of electrons from an electron donor to an electron acceptor, where the donor is oxidized and the acceptor is reduced.

  • Name three important electron carriers in microbial metabolism.

    NAD+ (to NADH), NADP+ (to NADPH), and FAD (to FADH2) are key electron carriers.

  • What is phosphorylation in the context of ATP production?

    Phosphorylation is the addition of an inorganic phosphate to a substrate, often to ADP to form ATP.

  • List the three types of phosphorylation used by cells to produce ATP.

    Substrate-level phosphorylation, oxidative phosphorylation, and photophosphorylation.

  • What is substrate-level phosphorylation?

    ATP production by transferring a phosphate group directly from an organic molecule to ADP.

  • What is oxidative phosphorylation?

    ATP production using energy from redox reactions during respiration to create a proton motive force.

  • What is photophosphorylation?

    ATP production using light energy to drive the phosphorylation of ADP.

  • What are enzymes and their role in metabolism?

    Enzymes are organic catalysts that increase the likelihood and rate of biochemical reactions without being consumed.

  • Name the six categories of enzymes based on their mode of action.

    Hydrolases, isomerases, ligases (polymerases), lyases, oxidoreductases, and transferases.

  • What is an apoenzyme and a holoenzyme?

    An apoenzyme is an inactive protein enzyme without its cofactor; binding with a cofactor forms the active holoenzyme.

  • What are cofactors and coenzymes?

    Cofactors are non-protein enzyme helpers; coenzymes are organic cofactors derived from vitamins.

  • How do enzymes affect activation energy in chemical reactions?

    Enzymes lower the activation energy required, speeding up the reaction without changing the overall energy change.

  • What is the induced fit model of enzyme-substrate interaction?

    The enzyme's active site changes shape to more closely fit the substrate upon binding.

  • List factors that influence enzyme activity.

    Temperature, pH, enzyme and substrate concentrations, and presence of inhibitors.

  • What are enzyme inhibitors and their types?

    Substances that block enzyme activity without denaturing the enzyme; types include competitive, noncompetitive, and feedback inhibitors.

  • Describe competitive inhibition of enzymes.

    Inhibitor competes with substrate for the active site; increasing substrate concentration can overcome inhibition.

  • What is allosteric activation?

    Binding of an activator at an allosteric site changes the enzyme's shape to make the active site functional.

  • Explain noncompetitive inhibition at an allosteric site.

    Inhibitor binds to an allosteric site, distorting the active site and reducing or stopping enzyme activity.

  • What is feedback inhibition in metabolic pathways?

    The end-product of a pathway binds allosterically to an enzyme early in the pathway, shutting down further production.

  • Give an example of an enzyme and its reaction type from the six enzyme classes.

    Hydrolase: Lipase breaks down lipids by hydrolysis; Oxidoreductase: Lactic acid dehydrogenase oxidizes lactic acid to pyruvic acid.