Chapter 4.1 Flashcards

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1
Q

Why are enzymes used?

A
  • possible to speed up the rate of reaction of important reactions with temperature and pressure, but this would DAMAGE cell components

So enzymes are used instead

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2
Q

What are enzymes?

A

Enzymes are biological catalysts

  • they increase the rate of reaction without being used up in Biolocial organisms
  • globular proteins
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3
Q

What types of reactions do enzymes do? (2)
Where can these be? (Examples) (2)
-Where in bacteria

A

ANABOLIC = building up in growth molecules from smaller
CATABOLIC (thing catalyse) = breaking down reactions
2) BOTH INTRACELLULAR - reactions for cells such as respiration (fats,Ayse for hydrogen peroxide in cells )
OR EXTRACELLULAR- reactions outside cells like digestion (trypsin for proteins analyse for starch in mouth ) or even outside organism (in bacteria / fungi)

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4
Q

Describe enzyme structure + how catalysations Hallen and why are enzymes highly specfic

A
  • they have an active site, which is where the substrate binds to, determined by tertiary structure
  • for the enzyme to work substrate has to fit exactly in (complimentary)
  • thus an enzyme substrate complex can be formed and the reaction catalysed
  • or else it can’t, thus enzymes are highly specific .
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5
Q

Briefly say Why do enzymes speed up rate of reaction

A
  • enzyme Substrate complex allows for the activation energy to be lowered so overall more reactants can react in successful collisions
  • there are two ways
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6
Q

What is the lock and key hypothesis (1)

What happens at each step + remember what complexes made!

A

In the same way a key will only fit into one lock, the substrate only complimentary and can only fit into one enzyme

  • when bound an enzyme substrate complex is formed
  • then substrate reacts and products are formed
  • this makes aN ENZYME PRODUCT COMPLEX
  • THEN PRODUCTS RELEASED
  • now Enzyme unchanged can do another reaction again

(Again bonds made put strain / atom groups of substrate held close enough so reaction happens)

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7
Q

What is the induced fit hypothesis!

What happens

A
  • Also shows how high specfic I enzymes are. They have to be able to make the active site of the enzyme change shape exactly to fit their complimentary shape too!
  • it works by initial Interactions between enzyme and substrate being weak, but these interactions rapidly cause change in enzyme tertiary 3D structure, that then STRENGHTENS BINDING
  • these strengthend bonds between enzyme and substrate now put a strain on substrate bonds, lower activation energy etc
  • enzyme substrate = enzyme product complex = split

(Again atom groups Of substrate held close enough so react)

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8
Q

How does the binding of enzyme to Su rate actually lower activation energy (like what actually happens)
Anabolic and catabolic / both

A

1) FOR ANABOLIC enzyme substrate complexes ensure that RIGHT ATOM groups of substrate are held CLOSE ENOUGH to react, this means any repulsion received is reduced and they can bond easily
2) FOR CATABOLIC Active Site of Enzyme R- groups can also interact with he substrate, creating TEMPORARY BONDS, which puts a strain on the bonds in THE SUBSTRATE, which can weaken the bonds and thus LOWER THE ACTIVATION ENERGY NEEDED SO RATE KF REACTION INCREASES.

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9
Q

Example of extra cellular enzyme - starch digestion

WHat enzymes + where + why (2 steps)

A

1) begins in mouth , amylase (produced in saliva and from pancreas) breaks down starch into maltose, a disaccharide
2) then small intestine , where maltose broken down into glucose by maltase
- now glucose small enough to enter cell

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10
Q

Example of extracellular enzyme trypsin

What is it Where it made + where it works

A

Tyrpsin is a type of protease

  • catalysed polypeptides into smaller peptides which then broken into amino acid
  • trypsin produced in pancreas , and digested in small intestine
  • then amino acid can be absorbed by bloodstream
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11
Q

What happens if you increase temperature on rate of reaction for enzymes substrate (key words!)

1) increase to optimum
2) increase past optimum

A

1) increasing temperature of reaction environment increases rate of reaction
- this is because reactants gain KINETIC ENERGY
- so they VIBRATE , with all more energy (so greater proportion to be at activation energy) and thus collide frequently , leading to SUCCESSFUL COLLISIONS
- thus rate of reaction increases

2) However this only happens until an optimum temperature
- this is the temperature at which the rate of reactions is highest, (no longer limiting but)
- . Past the optimum temperature an increase in temperature can cause ATOMS AND BONDS TO VIBRATE MORE, THUS PUTTING STRAIN ON BONDS LIKE HYDROGEN (or ionic etc) BONDS CAUSING THEM break between R groups in the tertiary structure of a protein .
- This breakage of the bonds causes changes in the 3D structure of the protein, and thus the active site of the enzyme CHANGES
- thus the active site is no longer COMPLIMENTARY TO THE SUBSTRATE , the enzyme is DENATURED AND a complex can’t be made so rate of reactions decrease until all enzyme denatured …
- this Is IRREVERSIBLE

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12
Q

What happens if you DECREASE temperature on rate of reaction for enzymes substrate

A

-decreasing temperature does not denature the enzyme, and decrease of reaction is not that rapid , here there is less kinetic energy and less proportion of reactants with activation energy essentially, so rate of reaction will be low due to infrequent successful collisions

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13
Q

More on optimum temps on how much temp needs to change for it

A
  • only a small change past optimum temperature is needed for RAPID denaturation , because only a small change in tertiary structure is needed to ruin 3d steucture So no longer COMPLIMENTARY
  • Q10 don’t work after denatured
  • optimum temp is different for different, could be low could be high
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14
Q

Q10.?

What is it normally for enzyme controlled reactions here

A

Just a measure of how much the rate of reaction changes with an increase of 10° of temperature.
- here it is increased temp / old temp rate of reaction x 100
2 = doubles every 10°

2) It is normally 2!, but after denaturation this would not apply
- this assumes everything is constant too

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15
Q

How do enzymes deal with extreme temps? In terms of structure

A
  • in cold, structures tend to be less stable so that a small change in temp will denature them, so they have to keep cold
  • high temps like for thermphiles will have very stable structures such as high proportions of HYDROGEN BONDS AND
    DISULFIDE BRIDGES , which makes them more RESISTANT to temperature changes
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16
Q

Why does PH cause a change in structure in an enzyme?

2 ways
Check summary

A
  • Enzymes are held by various bonds including hydrogen and ionic bonds in r groups of tertiary structure
  • high ph= low h+ vice verca

1) hydrogen ions interact with polar and charged r groups. So changing concentration of H+ ions changes the DEGREE OF THIS INTERACTION.
2) ALSO the interaction of hydrogen ions with r groups also affects interaction of R groups with each other

= THUS
- TOO MUCH hydrogen ions, the less r groups can interact with each other
- and TOO LITTLE hydrogen ions= less r groups CAN react with each other
Thus this leads to BONDS BREAKING and thus 3d structure changing, changing active site and so on

-3) as a result enzymes change with PH can only work in a NARROW RANGE (where they can renature too )

Summary

1) amount of H+ ions changes degree of interaction between hydrogen ions and polar / charged r groups, which changes structure
2) amount of h+ ions determine how much other r groups can interact with each other: too much / too little cause little interactions causing bonds to break and 3d structure to change etc

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17
Q

How does pH have effect on enzyme

1) deviating a bit from optimum
2) deviating a lot from optimum

A
  • increasing or decreasing pH towards optimum pH will cause rate of reaction to increase
  • however past this pH the structure changes of teritary so active site is altered and rate of reaction decreases.
  • HOWEVER, if the pH returned to optimum it will RENATURE and return to higher rates of reaction !

2) however if you take it beyond optimum pH too much , structure of enzyme is IRREVERSIBLY CHANGED, so it cannot renature
- thus enzyme has DENATURED and rate of reaction decreases as substrate no longer complimentary , complex can’t be made etc

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18
Q

When does rate of reaction highest and why

How to work out

A
Initial
# this because at the start you have the highest amount of substrate molecules , over time you will lose some so you will lose rate of reaction

2) draw gradient from 0!!!

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19
Q

Substrate concentration increase ?

What happens initially
When vmax hit

A
  • increasing substrate concentration means there is a higher chance reactants will collide leading to successful collisions and thus rate of reaction increases due to more ENZYME SUBSTRATE COMPLEXES BEING MADE
  • however after a point you will hit a point of saturation where all the active sites of an enzyme are taken and you have to wait for products to be released and so V MAX IS ACHIEVED
  • at this point substrate concentration is NO LONGER LIMITING FACTOR
20
Q

Enzyme concentration ?

  • When vmax hit
  • when
A
  • increasing enzyme increases rate of reaction because that increases number of active sites available , leading to more frequency and thus successful collisions and higher enzyme substrate complexes being made
  • however after a point all the substrates would have been catalysed leaving none left, so rate of reaction just ends
  • at this point V MAX IS ACHIEVED AND NO LONGER LIMITING FACTOR
21
Q

Why do enzymes need to be inhibited

A
  • it is Important that products not made too quickly as could build up excess in products
    As resources become WASTED
22
Q

Competitive inhibition

A
  • A molecule that is STRUCTURALLY SIMILAR to the substrate in the sense that it is COMPLIMENTARY to the enzyme’s active site in the same way Competes for the active site with the substrate
  • if it binds, then the enzyme can not catalyse the reaction, AS THE SUBSTRATE CAN NOT FIT IN IF SPADE IS OCCUPIED and so is INHIBITED
  • reduces the amount of enzyme substrate complexes made in a given time = reduce the rate of reaction
23
Q

Are competing inhibitors temporary or permanent

A

Most of the time TEMP because they Bind temporarily but some are permanent like aspirin

24
Q

What happens to the VMAX of the rate of reaction with a COMPETITIVE INHIBITOR
- why

A

Nothing, the VMAX is still achieved but after a longer time so line is less than what it did but still hits
- as it binds temporarily eventually all substrates will be catalysed anyways
(Assuming reversible )

25
Q

How can you change the effect of competitive Inhibitors

A

Here by increasing substrate concentration there is a higher chance at any one time the substrate will out compete the competitive inhibitor (assuming temporary one) .
- so increasing the substrate concentration increases rate of reaction , in Italy, but same VMAX is still achieved just quicker

26
Q

Non competitive inhibitors

How do they work and why is it called thst

A
  • here a molecule binds to an ALLOSTERIC site on the enzyme, a place OTHER than active site
  • as a result if it binds it will cause changes in the tertiary structure and thus 3D structure of enzyme
  • thus shape of ACTIVE SITE CHANGES
  • substrate is no longer complimentary to the active site and so an enzyme substrate complex cannot be made
  • reaction cannot be catalysed and rate of reaction stops
    But it wasn’t competing for active site = non competitive
27
Q

What happens if you increase substrate / inhibitor concentration for non competing inhibitors

What is the line graph for non competing inhibitor

A

By increasing the substrate concentration nothing happens

  • by increasing inhibitor concentration the rate of reaction decreases even more as less active sites are available
  • here remember if a bit is added there is still some rate of reaction not all is gone so line drawn is below (fixed quantity )
28
Q

Non competitive inhibitors reversible or irreversible

A
  • can be both
  • normally irreversible
    This can be bad and good, like something blocking nerve impulses = bad but something blocking excess acid irreversibly in stomach = good (prevents ulcers
29
Q

1) What is end product inhibition when does it happen
Why is it used + what mechanism
Give example

A

Where product produced at the end acts as an Inhibitor = NON COMPETITIVE REVERSIBLE

  • this is used to control the amount of product being released so resources aren’t wasted = NEGATIVE FEEDBACK LOOP
  • it happens in reaction pathways where final product inhibits first enzyme, cancelling it and regulate

2) when levels of ATP are high, ATP will inhibit the enzyme on allosteric site, preventing more glucose from converting
- when ATP IS LOW, atp won’t inhibit / will inhibit much less then geifre enzyme so more ATP is made

30
Q

Example of a metabolic poison cyanide?

A

Chance is non competing irreversible inhibitor of cytochrome C oxidase which is an enzyme that catalysed respiration reactions

  • a cell that can’t respire causes death
31
Q

Why is product / end product inhibition reversible

A

This is so that when product is being used up and low inhibition drops so more can be produced, it is all regulated!!!

32
Q

What are inactive precursor enzymes!

A

These are when enzymes are synthesised like this so they don’t do damage to their environment and are only ACTIVATED in a chemical reaction to then function

X for example protease enzymes are sometimes synthesised as inactive precursors so they don’t DAMAGE THE CELL THEY MADE IN, and activated later on…

33
Q

What is the basic difference between cofactors coenzymes and prosthetic groups

What are all of they

A

Sometimes enzyme needs extra NON PROTEIN component to make it work, this could be transferring atoms or form part of active site

  • if that is inorganic + temporarily bound (reversible )= cofactors (Na+)
  • if Organise = coenzyme (vitamin B3 making coenzyme NAD)

IF inorganic + PERMANENTLY BOUND (non reversible ) = prosthetic group

34
Q

What are specific differences between cofactors and coenzymes

Differences? (Changed vs unchanged?)

A

Cofactors = inorganic and loosely bonded
- they remain UNCHANGED IN REACTION

Coexnhmes = organic and
- they do GET CHANGED IN REACTION , often carry atoms or groups and can be RECYCLED

35
Q

Example of cofactors need to remember! (Cl) !!!

Need to know

A

Chlorine , Cl - ion is a cofactors for enzyme Amylase which breaks down STARCH, FORMS PART OF THE ACTIVE SITE

36
Q

Example for COENZYME (NAD) (not as necessary as other two)

A

NAD is a coenzyme made from vitmain B3 which is needed for transfer of hydrogen atoms in respiration

NADP for same thing in photosynthesis

37
Q

Example need to know for PROSTHETIC GROUP !!!!

A

Zn2+ needed permanently in carbonic anhydride , which is enzyme for metabolism of carbon dioxide

(Catalysed carbonic acid from water and carbon dioxide )

38
Q

How are PRECURSOR ENZYMES ACTIVATED
What must be done
How (3)
What is name for precursors that change because of enzyme or temp/ ph

A

Need a CHANGE IN TERTIARY STRUCTURE

1) Can be done by adding reversible inrogsnic molecule cofactors (apo -> halo)

2) change in pH or temp
3) another enzyme acting in it
- these are called PROENZYMES

39
Q

What is the inactivated form and activated form of a precursor enzyme called if activated by A COFACTORS

A

inactivated form= apoenzyme , after = holoenzyme

40
Q

How to investigate different conditions using upturned cylinder with hydrogen peroxide experiment

HOW TO CONTROL PH?
Make sure to add what?

A

Change temp
Make the cylinder upturned with water and clamps stand
Oxygen from hydrogen peroxide mixed with catalase will displace water
Rate of reaction = product produced / time
3) do a negative control each time

2) keep EVERYTHING ELSE CONSTANT, for pH add equal amounts of buffer solution Esch time

41
Q

How to do starch and amylase time taken for starch to turn in into maltose experiment?

A

In spotting tiles add a lot of drops of iodine
Then add starch to amylase in a temperature , or concentration depending on what you changing

Every 10s add a drop and keep doing until colour remains maltose (no starch left)

42
Q

How to do for ph or concentrations

A

Use buffers for pH / serial dilutions for substrate or enzyme concentration

43
Q

How to do experiment to investigate rate reaction enzyme

A

Substrat = Hydrogen Periode and Enzyme = catalase .

Catalyse found in tissued like liver / potato , so use this into hydrogen peroxide and see rate of reaction by collecting oxygen in upturned flask / gas syringe over time

Here change temp by = either changing temp of hydrogen peroxide or Catalsee
Change substrate conc with serial dilutions
Change enxyme conc by crushing into solution and serial dilution
Ph by adding acid conc ?

Control everything else, like amount of hydrogen periodise and conc of it each time, temoertaure and pH and only change what you measure

Dependent variable is the oxygen released and independent what you change , here you are plotting graphs of amount of oxygen produced against time , and this should decrease no matter what as time increases due to decreade in substrate

44
Q

Another experiment to investigate enzyme activity

A

Amylase enzyme catalyses starch to maltose

So here out one drop of iodine in potassium iodide solution in Esch dropping tile

  • then mix together a known concentration of amylase with starch solution and volume
  • start a clock and drop one into a tile every ten seconds. You are measuring the time it takes for it to REMAIN orange (as this means all the starch has been cat,seed)

Can vary conditions such as putting starch snd amylase into heat bath for a bit first to change temp, change the conc using serial dilutions ,

Make sure to do everything 3 times and mean and control everything

45
Q

How to keep pH constant

A

Add equal amount of pH buffer to both