Enzymes Flashcards

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

what do Oxidoreductases do ?

A

Transfer electrons

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

What type of enzyme forms isomers (transfers groups within a molecule) ?

A

Isomerase

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

What type of enzyme enables hydrolysis ?

A

Hydrolase

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

What type of enzyme forms double bonds & adds groups to double bonds ?

A

Lyase

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

What does Isomerase do ?

A

Forms isomers (transfers groups within a molecules)

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

What do ligases do ?

A

Forms bonds via ATP splitting

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

What type of enzyme forms bonds via ATP splitting ?

A

Ligases

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

What type of enzyme transfers electrons ?

A

Oxidoreductase

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

What is desolvation

A

Where an enzyme loses hydrogen bonds

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

What is induced fit ?

A

Where a protein changes shape to induce a lock & key formation & a conformational change takes place when the substrate binds

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

Define ∆H

A

Enthalpy change: Change in potential energy (∆H must be negative for a reaction to take place)

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

Define ∆S

A

Entropy change: Change in disorder, the more disordered the more likely the reaction.

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

Name 3 ways enzymes lower the activation energy ?

A

Decrease entropy: Particles more aligned and less energy is required to collide.
Desolvation: Where weak H bonds between enzyme & substrate are replaced by strong H bonds between substrate and aqueous soloution
Induced fit: conformational changes in enzyme allow enzyme and substrate to bind.

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

What is happening at V0 ?

A

The reaction is at a steady state (initial reaction velocity) & ES is stable

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

What is Vmax & what does it tell us about the reaction ?

A

Vmax is the maximum reaction velocity where the enzyme is saturated with substrate. Vmax tells us how fast the reaction is.

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

What is Km & how is it calculated ?

A

Km is Michaelis constant & is calculated as half of Vmax.

17
Q

What does Km tell us about the reaction ?

A

High Km = Loose fit and unstable
Low Km = Tight fit and stable
Stability of ES complex

18
Q

What is a non-competitive inhibitor ?

A

It binds to the enzyme but not at the active site.

19
Q

What does a non-competitive inhibitor do to the Vmax and the Km ?

A

Vmax: Is decreased due to the binding & possible change of active site, reaction slowed.
Km: Unchanged as substrate can still bind to active site.

20
Q

What is a competitive inhibitor ?

A

It binds to the active site on the enzyme

21
Q

What does a competitive inhibitor do to the Vmax and the Km ?

A

Vmax: Unchanged as enzyme can overcome inhibition by increasing substrate inhibition.
Km: Increased, as the inhibitor does not fit the enzyme as tight as the substrate therefore high Km means loose fit and unstable.

22
Q

What are the properties of Allosterically-regulated enzymes ?

A

Made up of many sub-units with many biding sites
Cooperatively bound
They are examples of non-competitive inhibitors
Bind to the enzyme and change the shape of binding site

23
Q

What is a concerted model enzyme ?

A

Where binding to one active site opens up all active sites and allows S to bind more effectively

24
Q

What is a sequential model enzyme ?

A

Where S binding to an active site only opens one active site a ta time in sequence.

25
Q

What is a covalently-modified enzyme ?

A

They are reversible and have multiple phosphorylation sites allowing for fine tuning of enzyme function.