factors affecting enzyme activity Flashcards

1
Q

explain how catabolism and anabolism are related to metabolism

A

catabolism is the breaking down of molecules

anabolism is the building up of molecules

reactions involve both breaking down and building up of molecules and metabolism is the sum of all reactions int he body

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2
Q

describe the flow of the composition of a living organism,what makes what in order to form a whole organism

A

polymers-cells-tissues-organs-organism

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2
Q

why do enzymes only catalyse one reaction

A

enzymes are very specifc.Each nzyme has a different shaped active site which is complementary to one speecidfic substrate molecule,explaining why they usually catalase one reaction

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2
Q

what are the 4 factors affecting enzyme activity

A

-ph
-temperature
-enzyme concentration
-substrate concentration

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2
Q

describe why thee rate of reaction is lower at lower teemperature

A

the lower temp means that molecules have lower kinetic energy thus they mov slower.This results is less frequent successful collision between the active site and the specific subsate so fewer enzyme-substrate complexes are formed thus the rate of reaction is slower

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2
Q

explain why the rate of reeaction is higher at higher temperature

A

at higher temperature the molecules have more kinetic energy so movie faster.This increases the likelihood that active site and substrate will collide and because the collision has higher energy it also means that there is a higher chance that each collision will result in a reaction,so in an ezyme-substarte complex

-in other words the faster movement of molecules results is more frequent successful collision so more enzyme-substate complex formation which increases the rate of a reaction

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3
Q

what is the definition of optimum temperature of an enzyme

A

the temperature at which the reaction catalysed by the enzyme is at its fastest

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4
Q

are the effects of high temperature reversible

A

no they are irreversible

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5
Q

are the effects of low temperature reversible

A

yes they are reversible

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6
Q

describe the process of denaturation of an enzyme

A

-As thee temperature increases so does the vibration of an enzyme molecule.This puts a strain on the hydrogen and ionic bonds which maintain the tertiary structure of the enzyme.At certain temperatures they break,this causes the active site of the enzyme to change shape so its no longer complementary to the specific substrate and as a result the substrate can no longer bond and a reaction cant occur

enzyme is said to have denatured

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7
Q

how do you compare graphs

A

-compare initial rates
-compare when the graph plateaus

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7
Q

describe how a ph above or below the optimum ph will affect enzyme activity

A

when the ph changes above or below the optimum ph of 7 ,the number of H+ ions or OH- ions increase.The ions interact with the charged R groups of main o acids.This in turn decreases the extent to which they interact with each other.This affects the hydrogen and ionic bonds which maintain the tertiary structure of the enzyme.When they break the active site of the enzyme changes shape and becomes denatured

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7
Q

what thee optimum ph of an enzyme

A

7,at the optimum ph the shape of the active site of an enzyme is in correct shape

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8
Q

describee the process of renaturation involving ph

A

when the ph changes slightly from 7 the shape of the active site changes,its no longer complementary to the substrate and the substrate cant bond,however if you return back to optimum ph the active site will restore its original shape ,where its complementary to that specific substrate

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9
Q

what changes to rate of reaction does the increase of enzyme concentration have .Exaplain why

A

when you increase ethe concentration of enzymes ,the rate of reaction will increase.This is because by increasing the concentration of the enzyme there will be a higher number of active sites available which the substrate can bind to

-result in more frequent successful collisions between active site and the substrate so results in more ESC’S

-thus faster rate of reaction

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10
Q

what is the v max of a reaction

A

its when the reaction is proceeding as fast as possible,

the rate of reaction has reached its maximum point

11
Q

describe what is happening at the v max of a reaction involving enzyme concentration and why

A
  • all teh active site of enzymes are occupied by a substrate molecule

-no more ESC’s can be formed as a result , until the products have been released from the active sites of the enzymes

11
Q

how can we further increase the V max of a reaction

A

increase the concentration of enzyme or increase the temperature of the reaction

12
Q

Explain why at some point increase the enzyme concentration does not result in higher V max/rate of reaction

A

at some point increasing the concentration of a reaction no longer affects the rate of the reaction, this is because the concentration of substrate has become a limiting factor.The concentration of enzyme is in excess so adding more of it will not have a further effect

13
Q

describe the effects of increasing substrate concentration on the rate of reaction and explain why that is

A

-increasing the substarte concnetration also increases thee rate of a reaction

-this is because there will be more substrate molecule to fill and bind to the active sites of enzymes

-result in more frequent successful collision,forming more ESCs so increasing the rate of a reaction

14
Q

explain why at some point increasing the concentration of substrate molecules does not increase the rate of a reaction,has no effect

A

at some point a point of ‘saturation’is reached where all the present active sites of enzymes have been occupied by specific substate molecules,so the addition of more substrates will not affect the rate of reaction as the enzyme concentration has become the limiting factor

14
Q

what can we do to increase the rate of the reaction / V max

A

increase the enzyme concentration

15
Q

what is Q 10 also known as

A

temperature coefficient

16
Q

what does Q 10 show

A

It shows how much the rate of a reaction when the temperature
increases by 10 degrees

17
how would you vary the substrate concentration
carry out serial dilutions of an existing stock solution of known concentration to produce different standard solutions of known concentration of substrate -can do the same for the enzyme involved in the reaction to investigate the effect enzyme concentration will have on the rate of a reaction
17
describe a experiment that can measure the rate of breakdown of starch -you can change the experiment to investigate the effect different factors will have on the rate of breakdown of starch
using a pipette add a drop of iodine dissolved in potassium iodide in each well of the spotting tile -get a test tube,in it place set volume of known concentration of amylase together with a buffer solution to maintain the level of pH during the reaction - to another test tube add a known concentration of starch solution -add the starch solution to the amylase and buffer solution -start stopwatch,at regular intervals using a pipette draw up some of the amylase nd starch solution and add it to the first well on the spotting tile -if the colour changes from orange to blue-black then starch is present and the reaction is still taking place -to measure the reaction rate time how long it will take for the drop of iodine in the spotting tile to remain orange and not change colour to blue-black,indicating that starch has ben broken down into maltose by the enzyme amylase -the less time it takes the faster the rate of the reaction
18
how would you control the temperature
use a thermostatically set water bath and a thermometer to check the temperature remains constant
18
what are some variables you need to keep constant during the experiment
so they don't alter your results
18
what is the ph buffer used for
to maintain the level of pH during a reaction
19
what is an independent variable
variable altered during the experiment
19
how would you control the enzyme and substrate concentration
use a set volume of the enzyme and substrate and use standard known concentration of the enzyme and substrate
20
what is a dependent variable
variable you measure
21
describe how the rate if reaction of catalase breaking down hydrogen peroxide can be measured -remember you can alter the experiment to investigate how a particular factor for example enzyme concentration will effect the rate if the reaction
-first, add a set volume of hydrogen peroxide into one test tube and add a set ph buffer into the same test tube to maintain the ph level during the reaction -place a bund onto the test tube and connect it to an inverted measuring cylinder which contains water using delivery tubing -Measure the rate of the reaction by measuring the volume of oxygen produced over a s et period of time -using a pipette add known concentration of catalase to the test tube of hydrogen peroxide and suffer solution then quickly shut the bung -as the reaction process water will be dispensed and the volume of oxygen collects -in this reaction the volume of water dispensed=the volume of oxygen produced -take readings of oxygen produced every 20 seconds for 5 min -repeat
22
how can you calculate the initial rate if the reaction
draw a graph with oxygen produced over time -then draw a tangent at time= o, -then calculate the gradient of that line by doing a change in y/change in x -the gradient is the initial rate of the reaction,the smaller the gradient the slower the initial rate of the reaction
23
explain the different rates of reaction observed at each temperature
-talk about initial rates of reaction and why that is,the steeper the line the faster the initial rate of creation -talk about line plateauing , whether because the substrate has depleted or because the enzyme has denatured -talk about the peak on the graph= Vmax
24
what does an alkaline solution have a lot of
OH- ions
25
what does an acidic solution have a lot of
H+ ions