Enzymes 1 Flashcards

1
Q

how do enzymes act as catalysts

A

lower activation energy by providing alternative transition state

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2
Q

5 key features

A
  1. Globular proteins
  2. Show specificity
  3. Catalysts
  4. Sensitive to changes in physical and chemical environment
  5. Their activity can be controlled
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3
Q

Lysozome

2 points

A
  1. enzyme in tears and secretions on exposed surfaces of body
  2. attacks bacterial cell walls killing the bacteria (natural antibiotic)
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4
Q

Lysozome

shape

A

includes a cleft into which part of the bacterial cell wall (made of peptidoglycan) can fit

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5
Q

Lysozome

which bond does it break

A

bond between sugars 4 and 5 of a hexamer

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6
Q

2 parts of AS

A

Substrate Binding Site

Catalytic Site

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7
Q

lock and key

A

binding site has complementary shape to substrate(s)]

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8
Q

induced fit

A

contact between part of the binding site and the substrate induces a change in shape of the active site to bind to the substrate

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9
Q

4 levels of enzyme specificity

A

absolute

bond

group

stereo

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10
Q

catalysts lower

A

activation energy

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11
Q

catalysis

proximity

A

substrate molecules close together

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12
Q

catalysis

orientation

A

substrates have correct relative orientation

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13
Q

catalysis

Strain/distortion

A

binding puts strain on bond making it easier for reaction to occur

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14
Q

acid-base catalysis

A

protons (H+) donated/accepted

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15
Q

Covalent catalysis

A

temporary covalent bond between enzyme and substrate

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16
Q

effect of time

start of reaction

A

very quick

Maximum ratio of S/E so greatest chance of collision

17
Q

effect of time

middle of reaction

A

amount of S decreases (it is converted to P) less chance of S colliding with E so rate of reaction decreases

18
Q

effect of time

end of reaction

A

Rate decreases until reaction reaches equilibrium (no net change in amount of S or P) when graph reaches plateau. Rate = 0

19
Q

dont understantd inital reaction velocity on graph

A

?

20
Q

IRV

Initial Reaction Velocity (t=0) =

A

x/y

used to compare enzyme activities

21
Q

Katal

A

1 Katal of enzyme activity produces 1 mole of product per second

or utilises one mole of substrate per second

(1 Katal = 1 mole/sec)

22
Q

Unit

A

1 Unit of enzyme activity produces 1 umole of product per minute

or utilises 1 umole of substrate per min

(1 Unit = 1 mmole/min)

23
Q

Turnover number (kcat)

A

the number of substrate molecules that can be converted to product by 1 enzyme molecule in 1 second

24
Q

Changes in pH affect

A

electrostatic bonds

25
Q

pH will decrease enzyme activity if

5 points

A
  1. Overall 3-D structure of active site is altered
  2. Group involved in binding to substrate changes charge
  3. Group involved in the catalytic act changes charge
  4. Group on substrate involved in binding to enzyme changes charge
  5. Group on substrate involved in catalytic act changes charge
26
Q

Optimum pH range not always ~pH 7

e.g.

A

pepsin

27
Q

Two effects of temperature

A

kinetic

denaturing

28
Q

temperature
kinetic effect
3 points

A
  1. Increased motion of molecules
  2. Increased collisions between enzyme/substrate
  3. Increased rate of reaction
29
Q

temperature
denaturing effect
5 points

A
  1. Proteins take on the 3-D structure with lowest potential energy - increases their stability
  2. Increased energy causes increased motion within the molecule as well as between molecules
  3. Weak bonds in the tertiary structure (hydrogen bonds) are broken and new bonds form in different positions
  4. New 3-D structures form
  5. If the change in 3-D structure alters the active site of the enzyme so that it cannot catalyse the reaction it is said to be denatured
30
Q

Denaturing effect is due to both

A

temperature and time of exposure to that temperature

31
Q

Optimum temperature is not always ~37 ºC

A

depends on location and what reaction occurs