ch 6 - Enzymes Flashcards

1
Q

efficiently and selectively catalzye chemical reactions

A

enzymes

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2
Q

how do enzymes contributes to human health?

A
  • can pathologically impact diseases
  • therapeutic causes (target specific enzymes in body)
  • indicate diseases (biomarkers)
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3
Q

true or false. all enzymes are proteins, and all proteins are enzymes.

A

false. all enzymes are proteins but not all proteins are enzymes

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4
Q

how are enzymes classified?

A

into 6 groups, based on the type of reaction they catalyze

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5
Q

3 characteristics of catalysts

A
  1. lower E needed for rxn to proceed
  2. speed up attainment of equilibrium but dont change equilibrium
  3. unchanged by the rxn
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6
Q

Enzymes ________ increase the rates of reaction.

Enzymes ________ affect the equilibrium of the reaction.

A

Do

Do not

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7
Q

how does substrate binding promote reactions?

A
  • reduces the entropy
  • dissolves the substrate to expose reactive enzymes
  • aligns functional groups of enzyme with substrate
  • distorts substrates
  • induced fit of enzyme in response to substrate binding
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8
Q

explain transition state binding in enzymes

A
  • enzyme distorts the substrate, forcing it toward transition state
  • enzyme must be shape and chemically compatible
  • enzyme changes shape without breaking to fit into a binding site
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9
Q

name the equation:
Vo = Vmax[S]
Km + [S]

A

Michaelis-Menton

- measures relationship between velocity and substrate concentration

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10
Q

what is Km?

A
  • amount of substrate required for enzyme to be functioning at 1/2 maximal velocity
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11
Q

what is a Lineweaver-Burk plot?

A
  • describes relationship b/w [S] and Vo
  • double reciprocal of 1/Vo vs 1/[S]
  • more precise was to analyze kinetic data
  • determines Vmax and Km
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12
Q

what is kcat?

A
  • enzyme turnover number
  • number of molecules of substrate converted to product per unit time under saturated conditions
  • cVmax/[Et]
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13
Q

What reversible enzyme inhibitor is being described and name an example.

  • usually resembles substrate
  • can only bind to free enzymes
  • results in a increase in Km, and a decrease in affinity for substrate molecule
A
  • Competitive inhibitor
  • example: transition state analogue
  • normal crosses y-axis at same point as inhibitor
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14
Q

What reversible enzyme inhibitor is being described?

  • bind only to enzyme substrate
  • vmax and km are both decreased
A
  • Uncompetitive inhibitor

- lines are parallel on graph/plot

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15
Q

Name the enzyme inhibitor.

  • binds both enzyme and enzyme substrate
  • vmax decreases and theres no change in km
A
  • noncompetitive inhibitor

- start at same spot on graph, but the noncompetitve inhibitor crossed the y-axis higher up than the no inhibitor

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16
Q

what type of inhibitor is useful for killing organisms? (herbasides, pestasides, chemical warfare)

A
  • irreversible inhibitors
  • 1 specific type is suicidal inactivators
    - trojan horse
    - very effective drugs, initially unreactive but convert to a reactive species that inactivates the enzyme
17
Q

what are serine proteases and name examples.

A
  • digestive enzymes that cleave peptide bonds in protein substrates
  • mediate turnover of self proteins
  • examples: trypsin, chymotrypsin, elastase
18
Q

what are the general characteristics of allosteric enzymes?

A
  • have activities regulated by interactions with metabolic intermediates
  • bind non-covalently to at sites distinct from active site
  • usually quaternary structure
  • often catalzye branch-point reactions
  • slow
  • dont obey Michaelis-Menten kinetics
  • have sigmoidal curves