Chapter 8 Metabolism Flashcards

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1
Q

Metabolism- Catabolism

A
  • breaking down large molecules into smaller molecules
  • releasing energy (making ATP)
  • Hydrolysis (digestion) reactions
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2
Q

Metabolism-Anabolism

A
  • building large molecules from smaller molecules
  • requires energy (using ATP)
  • Dehydration (condensation) reactions
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3
Q

Coupling of Catabolism and. Anabolism

A
  • Catabolic and Anabolic reactions are coupled (connected) by ATP and NADH
  • ATP stores energy from the catabolic reactions
  • ATP used later in anabolic reactions. •ATP is the cell’s main energy currency
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4
Q

Metabolic Pathways

A
  • Series of chemical reactions
  • Each step is controlled by an enzyme
  • Information to build enzymes is encoded in the cell’s genetic makeup
  • Start with substrate, end with product
  • Intermediates are short-lived
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5
Q

Enzymes: Biological Catalysts

A
  • Catalyst: increases the rate of a reaction
  • Enzymes: catalyst made of protein
  • Converts substrates (reactants) to products
  • Can carry out the reaction repeatedly •Enzyme is not altered as a result of the reaction
  • Action of the enzyme is based on shape/structure
  • Lower the activation energy of a reaction
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6
Q

Activation Energy

A
  • The amount by which the energy of reactants must be raised for reaction to take place
  • Energy added at the beginning de-stabilizes the substrates/reactants
  • Energy required to form unstable transition state
  • Enzymes LOWER the activation energy
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7
Q

Apoenzyme

A

Protein part of the enzyme

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8
Q

Cofactors

A

inorganic part of some enzymes (ions such as calcium, iron or magnesium), can act as electron carriers or participate in ionic bonding
Not all enzymes have cofactors (but if they do, the cofactor is required for the enzyme to function)

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9
Q

Coenzymes

A

organic part of some enzymes (vitamins), act as atom acceptor, sometimes electron carrier (ex: NADH)

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10
Q

Holoenzymes

A
  • Holoenzyme is the Apoenzyme + cofactor and/or coenzyme

* Cofactors/coenzymes can be in the active site or away from the active site

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11
Q

Active Site

A
  • A region on the enzyme that interacts with the substrate

* Where the reaction occurs

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12
Q

Induced fit

A
  • When the substrate arrives to the active site, the enzyme changes shape
  • Slight change in shape allows the enzyme to stress bonds, or bring substrates close together, etc.
  • Product is formed and released
  • Enzyme returns to original conformation
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13
Q

Location of Enzyme Action

A
Endoenzymes: 
stay inside the cell
Exoenzymes: 
•secreted outside of the cell wall
•break down large food molecules or harmful chemicals
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14
Q

Regularity of Enzyme Action: Constitutive enzymes

A
  • always produced in equal amounts or at equal rates

* regardless of the amount of substrate

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15
Q

Regularity of Enzyme Action: Regulated enzymes

A
  • not constantly present

* production is turned on (induced) or turned off (repressed) in response to changes in the substrate concentration

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16
Q

Control of Enzyme Activity

A

Pathways usually have a point of control - single enzyme affects whole process

17
Q

Types of enzyme control: Competitive Inhibition

A

•Substrate mimic (inhibitor) binds to active site- fake-out!•Competes for location (active site!)

18
Q

Types of enzyme control: Noncompetitive Inhibition

A
  • Inhibitor doesn’t resemble the substrate
  • binds to enzyme at a site different from its active site
  • substrate can still bind to the active site, however, the enzyme’s ability to catalyze is significantly slowed down
  • no product made while inhibitor is bound
19
Q

Types of enzyme control: Allosteric Control

A

Allosteric enzymes are: •Large enzymes
•Usually the first reactionin the pathway.

These enzymes are controlled by:
•activators -further in the pathway (B activates E4)
•inhibitors

The activator and inhibitor binding sites are called allosteric (other) sites

20
Q

Types of enzyme control: Feedback Inhibition (example of allosteric inhibition)

A
  • The end-product of the pathway serves as the inhibitor for the allosteric enzyme that catalyzes the reaction at the beginning of the pathway.
  • P inactivates E1
  • Most efficient stopping point
21
Q

Enzyme Poisons

A

Permanently inactivate enzymes
•May be competitive or noncompetitive inhibitor that binds irreversibly to the enzyme
•Or may destroy the enzyme chemically

22
Q

Metabolism

A

All chemical reactions in a living organism

23
Q

Amphibolic pathways

A
  • Metabolic pathways that have both catabolic and anabolic functions
  • Can run forwards or backwards
  • Link pathways together