Enzymes Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

How can you measure the course of enzyme catalyzed reactions?

A

Measuring time taken for reaction to occur, measuring rate of reaction, measuring concentration of product

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

How can you impact the RoR of a catalyised reaction?

A

pH, temp, concentration of enzymes or substrate, presence of inhibitors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

At optimum temperature?

A

Ek increases, more successful collisions between enzyme and substrate, more E-S complexes formed

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

pH at optimum?

A

Charge of active site is complementary to charge of substrate, more successful collisions, more ES complexes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Minor pH change?

A

Small reversible change to enzyme structure, H/OH ions cause charge of active site to repel substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Extreme pH changes?

A

H/OH ions interfere with ionic bonds (excess H or OH are attracted to their complementary charges in R groups neutralising them.) Ionic bonds break (and hydrogen), unravel tertiary structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

how does a competitive inhibitor reduction the rate of reaction?

A

The inhibitor competes with the substrate to bind to the active site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

where do non competitive inhibitors bind?

A

allosteric sites

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

what is cyanide an inhibitor for?

A

cytochrome oxidase, found in the inner mitochondrial membrane, stops the sequence of reactions that produces ATP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Cofactor?

A

Non-protein chemical that helps/ is necessary for a biological chemical reaction

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Types of cofactor?

A

Cofactor: relatively small chemical, normally inorganic
Coenzyme: Large organic molecule
Prosthetic group: permanent part of the enzyme structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

example of cofactor?

A

NAD, large organic molecule which temporarily binds to respiration enzymes. Transfer H atoms from one molecule to the next

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

what is meant by enzymes being specific?

A

any individual enzyme can only catalyse one reaction, only one substrate can fit

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

more advantages of immobilised enzymes?

A

high temp would denatured other unwanted enzymes/ kill contaminating microorganisms
Can make more product/ make product faster at higher temperature.
Enzymes can be easily added or removed to control RoR
Can be reused
Dont contaminate product

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Disadvantages of immobilised enzymes?

A

substrate needs to diffuse through gel/membrane
smaller SA of enzyme
Enzyme is at a lower concentration when immobilised
immobilised have low Ek
Immobilization can affect active site so fewer E-S complexes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Immobilised enzymes?

A

Enzymes fixed to an inert matrix/ insoluble agent through which the substrate flows/diffuses

17
Q

uses of immobilization?

A

measuring blood sugar in diabetics, producing lactose free milk, in biosensors

18
Q

bio sensor?

A

instrument that measures a SPECIFIC metabolite in a mixture of molecules by converting energy into an electrical signal

19
Q

what are the pros of using biosensors?

A

They give quantitative data, and they can detect very small concentrations of molecules:sensitive, they can detect a single type of molecule in a mixture: specific

20
Q

methods of immobilising enzymes?

A

Fix in gel beads/ membrane or cellulose fibres

21
Q

is non competitive inhibition permanent?

A

many are permanent but those involved in control of metabolic pathways are reversible

22
Q

example of competitive inhibition

A

malonic acid inhibits succinate which breaks down succinc acid into fumaric acid

23
Q

metabolism?

A

summer of all of an organisms chemical processes, comprising anabolic and metabolic pathways

24
Q

Metabolic pathway?

A

A sequence of enzyme controlled reactions in which a product of one reaction is a reactant in the next

25
Q

Inactivation?

A

A small reversible reduction in enzyme activity e.g at low temperatures or slightly varied pH

26
Q

Example of enzyme with highest turn over number?

A

Catalase: breaks down toxic waste, hydrogen peroxide

27
Q

higher RoR wit immobilised enzymes in beads?

A

Use smaller beads= larger surface area= substrate has easier access to enzyme molecule

28
Q

Effect of temperature on a free enzyme compared to immobilised?

A

IE has a greater range of optimum, IE denatured at a greater temperature, IE has a higher RoR at lower temperatures