Chapter 5: Microbial Metabolism Flashcards
Metabolism:
o The sum of all chemical reactions.
• Catabolism – BREAK down.
• Anabolism – BUILD up.
Catabolism:
o Breakdown of complex molecules into simpler molecules.
o Provides energy and building blocks for anabolism.
o ATP turns into ADP and P and Energy.
Anabolism:
o Build complex molecules out of simpler molecules.
o Uses energy and building blocks from catabolic reactions.
o ADP and P and Energy turn into ATP.
Microbial Metabolism:
o Although microbial metabolism can cause disease and food spoilage, many pathways are beneficial rather than pathogenic.
• Enzymes facilitate metabolic reactions.
• ATP is used by microbes and other cells to manage energy needs.
• Catabbolic reactions couple with ATP synthesis.
• Anabolic reactions couple with ATP breakdown.
Metabolic Pathways:
o A METABOLIC PATHWAY is a sequence of enzymatically catalyzed chemical reactions in a cell.
• They are determined by enzymes.
• Enzymes are encoded by genes.
Enzymes:
o Proteins.
o Catalyze chemical reactions.
o 3D globular shape.
Catalysts:
o Speed up a chemical reaction.
• Not permanently altered themselves.
Substrate:
o The substance that the enzyme acts on.
Active Site:
o The location upon the cell in which the substrate would act upon.
Coenzymes and Cofactors:
o Important Coenzymes:
• NAD, NADP, FAD, Coenzyme A.
o Cofacters can be metal ions:
• Zinc, copper, magnesium, manganese, calcium, cobalt.
Six Enzyme Classes Based on Type of Reaction they Catalyze:
o Oxidoreductase. o Transferase. o Hydrolase. o Lyase. o Isomerase. o Ligase.
Factors Influencing Enzyme Activity:
o Temperature (denature proteins when high).
• If temperature increases, rate of reaction increases until the enzyme (protein) id denatured by heat and inactivated.
• This causes the reaction rate to fall steeply.
o pH (denature proteins when high).
o Substrate Concentration.
• Increasing concentration of substrate molecule causes rate of reaction to increase until the active sites on all the enzyme molecules are filled.
• At this point the max rate of reaction is reached.
o Inhibitors.
• Competitive Inhibition: substrate and and competitive inhibitors compete for the active site of an enzyme.
• Noncompetitive inhibition: act on other parts of the apoenzymes or on the cofactor and decrease the enzymes ability to combine with the normal substrate.
Steps of Feedback Inhibition:
o 1. Substrate Binds.
o 2. Product Produced.
o 3. End-product binds to enzyme.
o 4. Pathway shuts down.
Testing for an Enzyme:
o Control:
• Urease Negative.
o Test:
• Bacterial urease hydrolyzes urea, producing ammonia.
• Raises the pH and indicator in medium turns fuchsia.
Ribozymes:
o RNA that function as catalysts by cutting and splicing RNA.
What is a coenzyme?
o Many Coenzymes are derived from B vitamins – nonprotein – associated with and activates an enzyme.
Why is enzyme specificity important?
o Allows the enzyme to find the correct substrate in a vast sea of molecules.
What happens to an enzyme below its optimal temperature?
Slow Reaction