Enzymes Flashcards

1.7, 1.8, 1.9

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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Describe the outdated lock + key model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
Q

if conc. of enzyme is fixed and _________ conc. is slowly increased, ____ increases proportionately to conc. of ________

A
  1. substrate
  2. rate
  3. substrate
26
Q

what happens when there’s low substrate conc.?

A
  • substrate cannot occupy all sites

- rate only half the max. possible

27
Q

what happens when there’s intermediate substrate conc.?

A
  • all active sites occupied

- rate doubled to max

28
Q

what happens when there’s high substrate conc.?

A
  • has no effect (all sites filled)

- no increase in rate

29
Q

define enzyme inhibition

A

substances that directly or indirectly interfere with the functioning of the active site = reduces activity

30
Q

T or F: competitive and non-competitive inhibitors are permanent

A

F: they are temporary (reversible)

31
Q

What are competitive inhibitors?

A
  • inhibitors complementary to enzyme’s AS

- block substrate from forming E-SC

32
Q

Competitive inhibitors:
if substrate conc. increased = effect of inhibitor _______
if conc. of inhibitor increased = rate of reaction _______

A
  1. reduced

2. reduced

33
Q

what are non-competitive inhibitors?

A
  • bind to enzyme BUT NOT the active site
  • change the 3D shape of AS
  • no E-SC formed
34
Q

T or F: non-competitive inhibitors do not compete with substrates

A

true

35
Q

define metabolic pathways

A

series of reactions in which each step is catalysed by an enzyme

36
Q

metabolic pathways are…

A

highly structured

37
Q

why are enzymes in metabolic pathways attached to membranes of cell organelles in a precise sequence?

A
  • 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
Q

what is end product inhibition?

A
  • used to keep a stable conc. of a specific chem

- (the same chem often inhibits the enzyme at start of reaction)