Enzymes Flashcards

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

what kind of proteins are enzymes

A

globular

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

what is an anabolic and catabolic reaction

A

anabolic – chemical reactions required for growth

catabolic – breaking down reactions

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

define metabolism

A

sum of all different reactions and reaction pathways happening in a cell or organism

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

Define Vmax

A

enzymes can only increase the rate up to a certain point

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

Define specificity

A

Each enzymes catalyses a different biochemical reaction

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

Define the lock and key hypothesis

A

Only a specific substrate will fit into the active site of an enzyme

When bound, an ESC forms

Substrate reacts forming an EPC

The products are released

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

define the induced fit hypothesis

A

active site changes slightly as the substrate enters the active site

initial interaction between substrate and enzyme induces changes in the enzyme’s tertiary structure

that strengthen binding and weakens the bonds in the substrate

lowering the activation energy

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

what is an intracellular enzyme and extracellular enzyme

give examples

A

intra – act within cells
> hydrogen peroxide broken down to oxygen and water by catalase

extra – work outside the cell that secreted them
> amylase and trypsin

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

define the temperature coefficient

A

measure of how much the rate increases with a 10 degree rise in temperature

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

how does denaturation occur when the temperature goes above optimum

A

vibration of bonds causes strain then breaking of bonds

causing a change in the tertiary structure of protein

so it is no longer functional as it is no longer complementary to its substrate

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

compare enzymes that are adapted to cold environments to enzymes adapted to hot environments

A

cold – have flexible structures which make them less stable (small temp changes denature them)

hot – have more sulfur bridges and hydrogen bonds so more stable
(makes them more resistant to temp change)

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

define renaturation

A

pH returns to optimum which means the protein can resume its original shape and function properly

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

what causes changes in protein structure when the pH changes (low and high)

A

low – less R-groups interact with each other causing bond breaking

high – more R-groups interact with each other, more bonds are formed

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

explain substrate and enzyme saturation

A

more substrate –> higher collision rate with active sites and formation of more ESC, higher rate

more enzymes –> more active sites available so more ESC, so higher rate

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

when substrate saturation occurs, what can increase the rate

A

temperature

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

why shouldn’t reactions happen too quickly in organisms

A

could lead to build-up of excess products and waste of resources

17
Q

define an inhibitor

A

molecule that prevents an enzyme from carrying out its function

18
Q

define competitive inhibition

A

molecule binds to active site to block the substrate
prevents ESC
substrate and inhibitor compete to bind to the active site

their effect is reversible

19
Q

what does the degree of competitive inhibition depend on

A

relative conc of the enzyme, substrate and inhibitor

20
Q

how does competitive inhibitors affect the rate and the Vmax

A

reduces the rate

Vmax stays the same

21
Q

define non-competitive inhibition

A

molecule binds to allosteric site
cause change in enzyme’s active site
enzyme becomes non-complementary

22
Q

how does increase the concentration of the enzyme affect the effect of the non-competitive inhibitor

A

doesn’t overcome the effect of the non-competitive inhibitor

23
Q

define end-product inhibition

A

when the product inhibits its enzyme

> negative feedback
prevents waste of resources
(non-competitive reversible inhibition)

24
Q

define a cofactor and coenzyme

A

component of an enzyme required for it to function

cofactor – inorganic, come from diet
coenzyme – organic, come from vitamins

25
Q

define a prosthetic group

A

permanently bound to their enzyme

required for the enzyme to function

26
Q

define precursor activation

A

enzymes produced in inactive form because it causes damage when it released

27
Q

how does the precursor enzyme become activated

A

addition of a cofactor cause change in their tertiary structure

28
Q

what is apoenzyme and what does it become when a coenzyme is added to it

A

precursor protein

becomes holoenzyme

29
Q

define a proenzymes/zymogens

A

change in the tertiary structure (activation of enzyme) brought about by the action of another enzyme or the changes in conditions

30
Q

are globular proteins hydrophilic or hydrophoboc on the outside

A

hydrophilic