Enzymes Flashcards

(36 cards)

1
Q

What do anabolic reactions do

A

build up molecules e.g protein synthesis

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2
Q

What do catabolic reactions do

A

break down molecules e.g digestion

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3
Q

What are enzymes

A

globular proteins that act as catalysts

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4
Q

Why are enzymes called biological catalysts

A

Because they are made of living cells

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5
Q

What is the structure of an enzyme

A

Protein with tertiary structure
Hydrophillic R groups on the surface making it soluble
Particular sequence of amino acids
R groups determine shape and bonds that form

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6
Q

What is the active site

A

specific 3D site which substrate binds to by weak chemical bonds

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7
Q

what are the general characteristics of enzymes

A

speed up reactions
not used up
have a high turn over rate
only catalyse reactions that are energetically favourable

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8
Q

what are the 3 sites of enzyme action

A

extracellular
intracellular in solution
intracellular membrane bound

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9
Q

what is an example of an enzyme acting extracellular

A

enzymes secreted from cells in exocytosis

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10
Q

what is an example of an enzyme acting intracellular in a solution

A

in solution inside cells e.g glucose breakdown in glycolysis

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11
Q

what is an example of an enzyme acting intracellular membrane bound

A

attached to membranes e.g mitochondria in ATP formation

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12
Q

what is the lock and key model

A

the active site and substrate are complementary to each other and it is a specific fit

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13
Q

what is the lock and key model

A

the active site shape changes slightly to acomodate the substrate

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14
Q

how do enzymes speed up the rate of reaction

A

they modify the substrate so that the reaction requires a lower activation energy
when substrate enters active site the molecules alters the shape so reactions can occur at lower temp

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15
Q

what is activation energy

A

minimum energy required in a chemical system for a reaction to occur

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16
Q

what is the first limiting factor in a reaction

A

the enzyme conc

17
Q

what is the limiting factor as the reaction carries on

A

the substrate conc

18
Q

how do you calculate rate of production

A

increase in mass divided by time

19
Q

how do you calculate % increase in mass

A

actual increase in mass divided by initial mass X100

20
Q

what is inactivation

A

reversible reduction of enzyme activity at low temp
insufficient energy to form E+S complexes

21
Q

what happens to enzymes over 40 degrees

A

denature due to increasing breaking hydrogen bonds and altering the enzymes tertiary structure

22
Q

what happens to enzymes at low temps

A

they become inactivated

23
Q

what happens to enzymes if PH is too high

A

it becomes neutralised by positive OH- charges

24
Q

what happens to enzymes if the PH is too low

A

the H+ ion attracts negative charges and neutralises them

25
What is enzyme inhibition
the decrease in the rate of an enzyme controlled reaction by an inhibitor
26
What does an inhibitor do
binds with the enzyme and stops it from forming an enzyme substrate complex
27
What is the effect of substrate concentration on enzyme activities
the more substrate the more successful collisions and complexes formed
28
What is the effect of enzyme concentration on activity
as enzyme concentration increases there are more active sites available so more complexes can form
29
What is the effect of pH on enzyme activities
too High Neutralised by excess OH-ions Too low The H+ions neutralise negative charges Both of these disrupt ionic and hydrogen bonds which changes the shape of the active site
30
How are enzymes immobilised
fixed trapped or bound on an inert matrix
31
What materials can be used to immobilise an enzyme
sodium alginate beads or cellulose microfibrils
32
How do immobilised enzymes work at higher temperatures and pH
It creates a microenvironment because trapping the molecule prevents the shape change that would denature the active site
33
what is an example of an inhibitor being used and how does it work
lactose free milk milk passed through a column with immobilised lactase lactose binds to active site and is broken Down
34
what are the advantages of immobilised enzymes
increased stability and function over a wide range of temperatures and pH products not contaminated enzymes easily recovered for reuse
35
why do enzymes trapped in beads have lower rate of reactions
because as is inside bead so substrate has to diffuse readily available to bind on a matrix
36