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enzymes Flashcards

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1
Q

what are the sequences reactions occur in called

A

metabolic pathways

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2
Q

name 2 steps of metabolic pathways

A

-anabolic reactions
-catabolic reactions

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3
Q

what are anabolic reactions

A

the building up of molecules

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4
Q

example of an anabolic reaction

A

protein synthesis

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5
Q

what are catabolic creations

A

the breaking down of molecules

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6
Q

example of a catabolic reaction

A

digestion

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7
Q

what are metabolic pathways controlled by

A

enzymes

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8
Q

what are enzymes and what type of protein are they

A

enzymes are catalysts and they are a globular protein

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9
Q

why are enzymes called biological catalysts

A

as they are made by living cells

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10
Q

what properties do enzymes have in the reactions they catalyse

A

-tehy speed up reactions
-aren’t used up
-are not changed
-have high turn over numbers (catalyse many reactions per second)

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11
Q

what does high turn over numbers mean

A

they catalyse many reactions per second

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12
Q

what level of protein structure are enzymes

A

tertiary structure

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13
Q

what does the protein chain of an enzyme fold into and what does it have

A

folds into a spherical or globular shape with hydrophilic R groups on the outside of the molecule which makes the soluble

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14
Q

what structure of an enzyme makes it soluble

A

have hydrophilic R groups on the outside of the molecule

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15
Q

what bonds hold enzymes tertiary structure

A

hydrogen bonds, ionic bonds and disulphide bridges

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16
Q

what is activation energy

A

the amount energy required for a chemical reaction to occur

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17
Q

why is the active site specific and unique in shape

A

due to the specific folding and bonding in the tertiary structure of a protein

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18
Q

how to enzymes catalyse a reaction

A

by lowering the amount of energy needed for the reaction to occur

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19
Q

why are enzymes specific

A

as they only catalyse one particular reaction

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20
Q

what happens when you add an enzyme to a reaction

A

it lowers the activation energy which therefore speeds up the reaction

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21
Q

what happens to the activation energy when enzymes attach to a substrate

A

when enzymes attach to a substrate they can lower the activation energy needed and therefore speed up the reaction

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22
Q

what does the lock and key mechanise suggest

A

it suggests that the enzymes active site is a fixed shape and that due to random collisions between the enzyme and the substrate that they can collide and then combine as they are complementary in shape and then an enzyme substrate complex is formed

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23
Q

once the enzyme substrate complex has formed what does it cause the substrate to do

A

it will slightly distort in shape and the distortion can lower the activation energy

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24
Q

what happens after the enzyme substrate complex has formed

A

after the enzyme substrate compex is formed the substrate slightly distorts in shape which cause the activation energy to lower and then the products are released and the enzyme can be reused

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25
what is the induced fit model
the induced fit is when the enzymes slightly changes shape to mould around the substrate
26
why in the induced fit model does the activation energy lower when an enzyme substrate complex is formed
as due to the enzyme moulding around the substrate it puts a strain on the bonds which weakens the bonds and therefore lowers the activation energy
27
what causes the activation energy to lower in the induced fit model
the strain on the bonds due to the enzyme moulding around the substrate
28
what happens after the enzyme substrate complex has formed in the induced fit model
the products are then removed and the enzyme active site returns to its original shape
29
what factors affect the rate of enzyme controlled reactions
-temperature -PH -substarte concentration -enzyme concentarion -inhibitors
30
what happens in enzyme controlled reactions if the temperature is too low
if the temperature is too low then there isn't going to be enough kinetic energy for enzymes and substrates to be moving fast enough for them to have successful collisions between the enzyme active site and the substrate - therefore there is fewer enzyme substrate complexes
31
what happens in enzyme controlled reactions if the temperature is too high
if the temperature is too high there is too much kinetic energy which causes the enzyme to denature, so the active site has changed shape so enzyme substrate complexes can't form
32
why does an enzyme denature if there is too much kinetic energy
as the bonds holding the amino acids in there tertiary structure in the active site are going to break due to the increase in temperature
33
what happens to the enzyme if the PH it too high or too low
the enzyme will denature
34
what happens in enzyme controlled reactions if the PH it too high
if the PH is too high there are too many hydrogen ions
35
what happens in enzyme controlled reactions if the PH it too low
if the PH it too low there are too many OH- ions
36
what do both the hydrogen ions or OH- ions cause in enzyme control reactions if they are too many of them
as they have a positive or negative charge they interfere with the charges in the amino acids in the active site, so the bonds holding the amino acids together in their 3D shape will break which means the active site will slightly change shape so therefore the enzyme has denatured so fewer enzyme substrate complexes form so rate of reaction is lower
37
what happens when the bonds holding the amino acids together in their 3D shape break
the active sire will slight change shape so therefore the enzyme has denatured so fewer enzyme substrate complexes form so rate of reaction is lower
38
what bonds holding the amino acids together in their 3D normally break
hydrogen and ionic bonds
39
How does substrate concentration affect the rate of an enzyme controlled reaction
at low substrate concentrations there is a lower rate of reaction as if there isn't enough substrate the reaction is slower as there are fewer substrate molecules available to collide with the enzyme so fewer enzyme substrate complexes form so the rate of reaction is slower
40
what happens when there is a low substrate concentration in an enzyme controlled reaction and why
there is a lower rate of reaction as their isnt enough substrate so the reaction is slower as there are fewer substrate molecules to collide with so fewer enzyme substrate complexes form
41
How does enzyme concentration affect the rate of an enzyme controlled reaction
if there isnt enough enzymes then the enzyme active sites will become saturated with small amount of substrate so therefore there is a slower rate of reaction as there are no more active sites available for enzyme substrate complexes to form
42
why after a certain point when you continue to increase substrate concentration does the rate of reaction stay constant
as there is a new limiting factor which is the enzyme concentration
43
what happens if you add more substrate but don't keep adding more enzymes
if you keeping adding more and more substrates eventually if you aren't also adding more enzyme the active sites will become fully saturated - so every active site is in use so the reaction can't occur any faster
44
when you get to a higher enzyme concentration why does the rate of reaction level off
as there is a new limiting factor which is empty active sites due to not enough substrate - so there is more enzymes than substrates so some of the enzymes aren't in use
45
what is an inhibitor
an enzyme that binds somewhere on an enzyme and prevents the enzyme from functioning
46
whats a competitive inhibitor
a non competitive inhibior is the same shape as substrate or is very similar so it can bind to active site as its also complementary to the active site
47
how is the competitive inhibitor able to bind to the active sire
as it has the same shape as the substrate or a similar shape so it is complementary
48
what forms when the competitive inhibitor binds with the active site
an enzyme Inhibitor complex
49
what does the competitive inhibitor prevent
it prevents the substrate from being able to bind so no enzyme substrate complexes can form
50
if you add high concentrations of substrate what can this do to the inhibitor
it will flood or outcompete the inhibitor knocking them out of the active site
51
what is a non competitive inhibitor
a non competitive inhibitor binds away from the active site on the allosteric site
52
what happens to the structure of an enzyme when a non competitive inhibitors binds to the allosteric site
the tertiary structure of the protein slight changes which therefore causes the active site to slightly change shape, as the active site is has changed shape the substrate is no longer complementary to active site so it can't bind to form an enzyme substrate complex
53
why can't a substrate bind to the active site of an enzyme when there's a non competitive inhibitor
as a non competitive inhibits binds to allosteric site which slightly changes shape of the tertiary structure so active site changes shape so the substrate isn't complementary to active site
54
what is an immobilised enzyme
an enzyme that is attached to an inert or insoluble material
55
what are the 4 ways in which enzymes can attach to an inert or insoluble molecules
-absorption -covalent bonding -encapsulation -cross linking
56
how do you encapsulate enzymes in alginate beads to form corn syrup
1 - mix enzymes with sodium alginate 2- add drop by drop into calcium chloride 3 - the pack the alginate beads into columns 4 - run substrate through the column 5 - collect products from bottom
57
why do the alginate beads start to form once calcium chloride is added
as sodium alginate and calcium chloride forms a complex which is insoluble which then become the alginate beads
58
why are alginate beads packed Into columns
there is enzymes in the alginate beads and in the column you have glucose solution which is the substrate here, so you run glucose solution through the column and the enzymes would catalyse the reaction and then product will come out from the bottom here the product would be fructose
59
what does the alginate beads acts and and what does the glucose solution act as
the alginate beads act as an enzyme and the glucose solution acts as a substrate
60
what is the product formed in a column of alginate beads and glucose solution
fructose is the product
61
what is the processes of alginate beads and glucose solution forming fructose used for
used in the production of corn syrup
62
in the example on mobilised enzymes and mink using alginate beads what is the enzyme and what is the substrate
the substrate is the lactose in milk and the immobilised enzyme which is found in the alginate beads is lactase
63
describe the process that uses alginate beads and immobilised enzymes to do with milk
1 - lactose can be poured through the channel containing the alginate beads with immobilised enzyme lactase and the product formed is lactose free milk
64
what is the product that's formed when lactose milk is pored through a column contains alginate beads with immobilised enzyme lactase
the product formed is lactose free milk
65
how is lactose free milk formed
as the immobilised enzymes lactose converts lactose into glucose and galactose as the milk flows through
66
what is the only issue with producing lactose free milk this way
as you can't get 100% yield, so you can't get 100% lactose free milk
67
to get a higher yield of lactose free milk what would you do
you would run the products through the column a few more times
68
how are immobilised enzymes used
in alginate beads
69
why can immobilised enzymes be easily reused
as they are separate from the product
70
why would you use immobilised enzymes
-can be reused -easily recover enzymes -longer shelf life of enzyme
71
name an advantage of immobilised enzymes
less purification is needed as it keeps the product enzyme free so it doesn't affect product quality
72
why do immobilised enzymes need less purification
as it keeps the product enzyme free so it doesn't affect product quality
73
name another advantage of immobilised enzymes
it allows for continuous production using the same column
74
why is using immobilised an enzymes an efficient process
as it results in more product per unit time
75
what is the benefit of the immobilised enzyme and product being separate
it reduces end product inhibition
76
what do immobilise enzymes allow the enzymes to become more tolerant too
enzymes become more tolerant to PH changes and is more tolerant of temperature it is thermostable which means its less likely to denature at high temperatures
77
what does immobilised enzymes making enzymes thermostable allow
it allows the temperature to be increase a bit higher to speed up reactions but enzymes won't denature

biol (19 decks)

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