1.4 enzymes Flashcards

1
Q

explain how substrate concentration affects enzyme activity?

A

if enzyme concentration stays constant, then as substrate concentration increases so does rate of reaction.

this is until the reaction plateaus as all the active sites are occupied and therefore at this point enzyme concentration/active sites becomes the limiting factor

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2
Q

define a catabolic enzyme?

A

an enzyme that breaks larger substrate into smaller products

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3
Q

define an anabolic reaction?

A

an enzyme that breaks larger product into smaller substrate

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4
Q

define turnover number?

A

the number of substrate molecule turned into product per unit of time

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5
Q

describe (in terms of bonds) how active sites denature?

A

vibrations break apart the hydrogen bonds in the active site

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6
Q

describe how enzyme concentration affects enzyme concentration graph?

A

as enzyme concentration increases, so does the rate of reaction.
they are directly proportional until it (plataeus??)

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7
Q

describe how substrate concentration affects an enzyme activity graph?

A

as substrate concentration increases, so does the rate of reaction until a certain point where the graph plateau’s.

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8
Q

describe the activity of an enzyme bound on a membrane surface on a temperature graph? explain why this is?

A

the enzymes now make direct contact with the substrate and product is formed faster. - higher total product and same higher optimum as alginate beads.

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9
Q

describe the activity of immobilised enzymes in alginate beads on a temperature graph? and explain why this is?

A

the enzyme activity will continue to increase beyond the optimum, due to the alginate gel fills/supports the active site (stoping it from denaturing) and allowing for more ESC.

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10
Q

describe the effect pH has on an enzyme activity graph?

A

enzymes have a narrow optimum pH range, and the graph increases and decreases at the same rate either side of the optimum, leaving a ’n’ shaped graph.

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11
Q

describe the general graph of temperature affecting enzyme activity?

A

increased temperature gives the molecules more kinetic energy, and therefore the enzymes and substrate move around quicker and have a higher chance of colliding and forming enzyme substrate complexes.
higher temperature = higher rate of reaction (steepness)

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12
Q

describe the process by which lactose get removed from milk?(alginate beads)

A

as milk flows through the column, the substrate (lactose) diffuses into the alginate matrix and forms ESC with lactase, then glucose and galactose diffuses out of the membrane and leave the column with milk.

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13
Q

describe the process of a biosensor?

A

detects molecules

transducer detects the chemical change, amplifier amplifies it, and display.

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14
Q

describe what a biosensor is? give an example

A

a biosensor detects biologically important molecules at low concentrations (blood glucose levels in a diabetic person)

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15
Q

describe what occurs at 25 degrees on an enzyme activity graph?

A

as time increases so does the amount of product formed, there is a lower degree of steepness but they are directly proportional until denaturing temperature

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16
Q

describe what occurs at 37 degrees on an enzyme activity graph?

A

as time increases, so does product formed, there is a steep curve at the beginning until is reaches a peak and then starts to plateau at the highest amount of product formed

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17
Q

describe what occurs at 60 degrees on an enzyme activity graph?

A

as time increases so does product formed, at the beginning there is the steepest curve/rate of reaction until it begins to plateau at a lower amount of product formed

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18
Q

do enzymes have a high or low turnover number?

A

enzymes have a high turnover number

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19
Q

explain how an enzyme substrate complex occurs in relation to the charges? how does the pH affect this?

A

the charges on an amino acid must attract the charges on the substrate molecule
the charges on an enzymes active site are affected by free h+ ions and OH- ions therefore if there is too many of one or the other, the enzyme and substrate would repel one another.

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20
Q

explain how enzyme concentration effects the enzyme activity graph?

A

once product leaves active site, enzymes reused and therefore a low number of enzymes are needed to catalyse a lot of reactions (high turnover number)
this is because there are more active sites available to catalyse more reactions.

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21
Q

explain the effect pH has on the rate of an enzymes reaction inside of the optimum?

A

due to the narrow optimum pH:
small changes can cause reversible changes in structure and possible inactivation
large changes can cause the enzyme to denature

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22
Q

explain the effect pH has on the rate of an enzymes reaction outside of the optimum?

A

due to the narrow optimum pH:
small changes outside of the optimum alters the rate of reaction but not the structure of the enzyme
large changes denatured the enzyme

23
Q

explain what occurs at 25 degrees on an enzyme activity graph?

A

kinetic energy is low, substrate and enzyme collide less often therefore resulting in less enzyme substrate complexes and product is produces slower

24
Q

explain what occurs at 37 degrees on an enzyme activity graph/product formed?

A

there is higher kinetic energy, therefore enzyme and substrate collide more often resulting in more successful enzyme substrate complexes and product is formed quicker

as it levels off, there is no more substrate left to convert, and substrate concentration is now the limiting factor

25
explain what occurs at 60 degrees on an enzyme activity graph?
product is initially formed very quickly due to higher kinetic energy levels, after this the enzymes denature and as the active sites shape has changed less product is formed due to no more ESC unconverted substrate remains
26
how do biosensors work?
they use immobilised enzymes on a gel membrane, the biosensor detects when substrate turns into product (chemical change)
27
how does a competitive enzyme inhibitors work?
the inhibitor is structurally similar to substrate molecule and therefore can fit in the active site instead of the substrate this prevents enzyme-substrate complexes.
28
how does lysozyme enzyme destroy pathogenic bacteria?
the lysozyme enzyme breaks down the cell wall of pathogenic bacteria (the glycosidic bonds between its amino sugars)
29
what are enzymes?
enzymes are biological catalysts that have tertiary structure
30
what are some advantages of immobilised enzymes?
enzyme does not contaminate the product, they can be reused, only a small quantity of enzyme needed, they have greater stability/denature at higher temperatures, more control over the process.
31
what are some uses of industrial enzymes?
used in food, pharmaceutical, agrochemical
32
what are the factors affecting enzyme activity?
temperature, pH, substrate concentration, enzyme concentration,
33
what do enzymes do to the activation energy? and therefore temperature?
enzymes lower the activation energy and therefore reactions can occur at lower temperatures
34
what does an enzyme inhibitor graph look like? (substrate conc. against rate of reaction)
non-competitive inhibitors plateau, as the rate of reaction stays the same, this is because there is a lower amount of available enzymes to perform enzyme substrate complexes and so it becomes the limiting factor. competitive inhibitors increase more-so (rate of reaction increases) as there’s a higher chance of more ESC with the more substrate concentration.
35
what does catalase enzyme break down?
catalase breaks down hydrogen peroxide into water and oxygen.
36
what does decreased flow rate do to the rate of removal of lactose from milk in a column?
decreased flow rate allows for more contact time between the enzyme and substrate.
37
what does lactose get turned into by lactase?
glucose and galactose
38
what does the lock and key-hypothesis suggest?
that the substrate and enzyme have an exact fit
39
what is a non-competitive inhibitor?
a non-competitive inhibitor binds to any other part of the enzyme and alters the overall shape of the enzyme/active sit, this therefore means that the substrate can no longer fit into the active site.
40
what is activation energy?
the energy to break existing chemical bonds inside molecules and begin a chemical reaction.
41
what is an immobilised enzyme?
an immobilised enzyme is fixed, bound or trapped in an inert matrix.
42
what is enzyme inhibition?
a substance that decreases the rate of an enzyme catalysed reaction or stops it.
43
what is the induced fit hypothesis?
that the substrate molecule changes the shape of the of the active site to fit perfectly (think glove on a hand)
44
what occurs if you increase substrate concentration on a competitive inhibitor?
increasing substrate concentration, decreases the effect of a competitive inhibitor as the enzyme is now more likely to collide with the substrate and not the inhibitor. these keep increasing on a graph
45
what occurs if you increase substrate concentration to a non-competitive inhibitor?
increasing substrate concentration will not increase rate of reaction as the substrate no longer fits in the enzymes active site therefore successful enzyme substrate complexes cannot form. graph plateaus lower than I would without an inhibitor
46
what occurs in the enzyme-substrate complex?
enzymes combine with substrate molecules at the active site following a successful collision to produce a product, hence catalysing the reaction.
47
what shape does an ezyme’s active site have?
Its active site has a specific shape, which is complimentary to the particular substrate
48
where would you find the lysozyme enzyme?
in tears and other secretions
49
which is quicker, free enzymes or immobilised enzymes?
free enzymes are quicker, as both the substrate and enzyme are moving, whereas in immobilised only the substrate is moving.
50
why is a immobilised enzyme bound on a membrane (any membrane) better than immobilised enzymes enzymes within alginate beads?
immobilised enzymes bound on a membrane allow for a quicker reaction as they do not need to diffuse into the bead/jellly to perform enzyme substrate compelxes.
51
why is diffusion quicker in the smaller alginate beads when removing lactose from milk?
the smaller beads have a smaller surface area, which means there is more space for the molecules to diffuse, enabling quicker diffusion.
52
why is the induced fit hypothesis advantageous to the amount of product being formed?
several substrate can react with the same enzyme
53
What has x-ray diffraction shown in lysozyme?
a groove in the side of it (active site)
54
what is a buffer?
stabilise pH level/consistent