Biochem - Enzymes Flashcards

(39 cards)

1
Q

6 major classes of enzymes:

A
  • Ligases
  • Lyases
  • Hydrolyases
  • Isomerases
  • Oxidoreductase
  • Transferases
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2
Q

What 4 things affect enzyme reactions?

A
  • enzyme
  • substrate
  • effectors
  • temperature
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3
Q

Do enzymes get used up?

A

No; they are catalysts

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4
Q

4 reasons biocatalysts are preferred over inorganic catalysts:

A
  • greater reaction specificity: avoid side products
  • higher reaction rates: biologically useful timeframes
  • milder reaction conditions: conducive to cell conditions
  • capacity for regulation: control biological pathways
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5
Q

What 2 reaction conditions are compatible with life?

A
  • 37 degrees C
  • pH of 7
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6
Q

Ligases (synthetases)

A
  • join 2 molecules at the expense of ATP
  • require energy
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7
Q

Lyases

A

remove atoms to form double bonds or add atoms to double bonds

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8
Q

Hydrolyases

A

cleave bonds with addition of water

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9
Q

Isomerases

A
  • move functional groups within a molecule
  • only one substrate and one product
  • think racemic mixtures or epimers
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10
Q

Oxidoreductases (dehydrogenases)

A

catalyze oxidation-reduction reactions

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11
Q

Transferases (kinases)

A
  • move functional groups between molecules
  • induces kinases
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12
Q

Exergonic

A
  • neg (-) delta G
  • spontaneous
  • favorable
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13
Q

Endergonic

A
  • pos (+) delta G
  • non spontaneous
  • nonfavorable
  • must be coupled to exergonics in order to form a net delta G that is favorable
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14
Q

H:

A
  • amount of heat absorbed or released
  • aka exothermic or endothermic
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15
Q

Exothermic

A

releases heat -> -

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16
Q

Endothermic

A

absorbs heat -> +

17
Q

S:

A
  • entropy
  • state of disorder and randomness
18
Q

What info does delta G provide?

A
  • only spontaneity
  • NOT reaction rate
19
Q

Do enzymes alter delta G?

20
Q

Do catalysts alter reaction equilibria?

21
Q

What do enzymes affect?

A

they decrease the free activation energy (delta G) of a reaction

22
Q

Which model goes through a conformational change? (Lock-and-key OR Induced-fit)

23
Q

What kinase is in all tissues?

23
Q

Which model does hexokinase go through?(Lock-and-key OR Induced-fit)

24
What kinase is in liver cells?
glucokinase
25
Michaelis-Menten equation
26
Km is the substrate concentration that yields what?
1/2 Vmax
27
Kcat:
how many substrate molecules can one enzyme molecule convert per second
28
Km:
measure of a substrates affinity for an enzymes
29
Kcat / Km
measure of catalytic efficiency
30
2 types of kinetic mechanisms
- sequential (random and ordered): requires ternary complex - ping-pong: no ternary complex is required
31
sequential mechanism graph
lines intersect
32
ping pong mechanism graph
lines are parallel
33
What type of inhibitor is used in drugs?
reversible inhibitor
34
What type of in inhibitor is a powerful toxin
irreversible inhibitor
35
competitive inhibition
- competes with substrate for binding; binds active site - no change in Vmax; decrease in Km - lines intersect at y axis
36
uncompetitive inhibition
- only binds to ES complex (does not affect substrate) - decrease in Vmax; decrease in Km - lines are parallel
37
mixed inhibition
- binds enzyme w or wo substrate - decrease in Vmax; change in Km - lines intersect LEFT of y axis - Non-comepetitive inhibitors are mixed inhibitors (no change in Km)
38
Competitive, noncompetitive, and uncompetitive plots