Enzymes Flashcards

1.7, 1.8, 1.9

1
Q

enzymes are……

A
  • biological catalysts

- They are substrate specific (complementary)

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2
Q

enzymes are effective in….

A

tiny amounts

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3
Q

enzymes are______ proteins at the _______ structure

A

globular, tertiary

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4
Q

catalyses reactions both ___________ (in cell) and __________ (outside cell) which determines structure/function

A

intracellular, extracellular

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5
Q

enzymes are catabolic what does that mean?

A

active site effects bonds in substrate, substrate breaks (hydrolysis)

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6
Q

what does anabolic mean?

A

bring substrate molecules together (building, condensation)

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7
Q

How should a typical reaction should occur:

  1. ______ collide with enzyme with sufficient ______ energy.
  2. alters arrangement of _____
  3. energy of ______ must be lower than energy of _______
A

substrate, kinetic
atoms
products, substrate

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8
Q

how do enzymes speed up chem reactions?

A

lower activation energy (reactions can occur at lower temps)

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9
Q

what is the area the substrate fits into on a protein called?

A

the 3D active site

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10
Q

what is the name given when a substrate interacts with an enzyme?

A

enzyme-substrate complex

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11
Q

Describe the induced fit model

A
  1. enzyme is flexible + alters shape in presence of substrate (due to change of environment)
  2. enzyme puts strain on substrate
  3. causes distortion in substrate bond(s) = lowers activation energy
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12
Q

Describe the outdated lock + key model

A

the shape of the substrate exactly fits into the active site

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13
Q

name the 5 factors that affect enzyme action

A

pH, temp, substrate conc., enzyme conc., conc. of competitive and non-competitive inhibitors

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14
Q

how is the rate of an enzyme controlled reaction measured?

A
  • rate of formation of products

- rate of disappearance of substrate

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15
Q

Describe an enzyme reaction in 6 steps

A
  1. at first easy for substrate to come into contact with enzyme (lots of empty sites)
  2. substrate rapidly broken down = increase in product
  3. less and less substrate = harder to come into contact with enzyme
  4. takes longer for substrate to be broken down = rate of formation + disappearance decreases
  5. reaction slows
  6. graph flattens = all substrate used up
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16
Q

how to measure rate of change? (graph)

A

measuring gradient at certain point (may need a tangent)

17
Q

How does a rise in temp affect enzyme activity?

A

increases kinetic energy, more collisions = more enzyme-substrate complexes

18
Q

what happens when you exceed optimum temp/pH of the enzyme?

A

denaturation of 3D active site = no enzyme-substrate complexes = decrease in rate

19
Q

how does pH affect how an enzyme works?

A
  • can change amino acids making up active site

- can cause breakage of bonds in enzyme tertiary structure (changes active site)

20
Q

what aids in determining the active site?

A

the ionic bonding between NH2 (amine) and COOH (carboxyl)

21
Q

enzymes work well at low conc. because…

A

are not used up in a reaction

22
Q

what happens when enzyme conc. is low?

A
  • excess substrate molecules
  • not enough active sites
  • rate only half of max for no. of substrate
23
Q

what happens when there’s intermediate enzyme conc.?

A
  • all substrate molecules occupy active sites

- rate at max. as all sites filled

24
Q

what happens when there’s high enzyme conc.?

A
  • already enough enzymes to accommodate substrate

- no increase in rate of reaction

25
if conc. of enzyme is fixed and _________ conc. is slowly increased, ____ increases proportionately to conc. of ________
1. substrate 2. rate 3. substrate
26
what happens when there's low substrate conc.?
- substrate cannot occupy all sites | - rate only half the max. possible
27
what happens when there's intermediate substrate conc.?
- all active sites occupied | - rate doubled to max
28
what happens when there's high substrate conc.?
- has no effect (all sites filled) | - no increase in rate
29
define enzyme inhibition
substances that directly or indirectly interfere with the functioning of the active site = reduces activity
30
T or F: competitive and non-competitive inhibitors are permanent
F: they are temporary (reversible)
31
What are competitive inhibitors?
- inhibitors complementary to enzyme's AS | - block substrate from forming E-SC
32
Competitive inhibitors: if substrate conc. increased = effect of inhibitor _______ if conc. of inhibitor increased = rate of reaction _______
1. reduced | 2. reduced
33
what are non-competitive inhibitors?
- bind to enzyme BUT NOT the active site - change the 3D shape of AS - no E-SC formed
34
T or F: non-competitive inhibitors do not compete with substrates
true
35
define metabolic pathways
series of reactions in which each step is catalysed by an enzyme
36
metabolic pathways are...
highly structured
37
why are enzymes in metabolic pathways attached to membranes of cell organelles in a precise sequence?
- the product of one reaction acts as a substrate for the next reaction (greater chance of substrate in contact with enzyme) - more efficient at producing end product
38
what is end product inhibition?
- used to keep a stable conc. of a specific chem | - (the same chem often inhibits the enzyme at start of reaction)