Enzymes Flashcards

You may prefer our related Brainscape-certified flashcards:
0
Q

What type of proteins are enzymes ?

A

Globular

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

Why do reactions increase their rate due to temperature ?

A

More kinetic energy

More collision between substrate and active site

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

Why are enzymes important ?

A

They sustain life by ensuring that metabolic functions occur at faster rates, by lowering the activation energy level of biochemical processes.

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

Characteristics of an enzyme

A
Globular
Tertiary 
Substrate specific
Needed in Small quantities 
Could be recycled 
Does not change the direction of a reactio
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is the purpose of anabolic and catabolic reactions ?

A

To maintain balance - homeostasis

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

Exergonic reaction

A

Release energy

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

Endergonic

A

Absorb energy

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

Why is the active site so smaller than the enzyme ?

A

Protects the enzyme from free water molecules as active site contains r groups that may be hydrophilic.
Protects from external environment

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

Enzymes have varying degrees of specificity ?

A

Some have absolute specificity and bind to on but bind to no more than one.

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

The lock and key model

A

Only substrates with a complementary shape to the enzymes will bind with enzyme

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

How does heat denature enzymes?

A

Heat changes the shape of the enzyme which therefore is unable to bind to its specific substrate.

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

How is a substrate complementary to its enzyme?

A

Shape
Charge
Hydrophobic or hydrophilic nature

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

What amino acids line the active site ?

A

Substrate binding amino acids

Catalytic amino acids

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

Coenzyme

A

Helper molecules of enzymes which bind to the apoenzyme temporarily to activate an enzyme

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

Examples of coenzymes

A

NAD
FAD
Actyl

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

There are two types of amino acids in the active site , what are they!

A

Substrate binding amino acids

Catalytic amino acids

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

What does a substrate binding amino acid do

A

Bind to substrate

17
Q

What does a catalytic amino acid do

A

Make or break bonds

18
Q

There are two types of enzymes

A

Protein only enzyme

Apoenzyme

19
Q

What is an apoenzyme

A

Has partially protein in its active site but it needs a coenzyme to bind it in its apoenzyme part.

20
Q

Cofactors

A

Some enzymes need a cofactors or a particular ion for their activity.

21
Q

Prosthetic group

A

Tightly bonded part of an enzyme .

22
Q

Enzymes that involve in synthesis of reactions are said to be facilitating a

A

Anabolic reaction.

23
Q

Anabolic reactions are

A

Endergonic reaction

24
Q

Enzymes that involve in breaking down bonds are said to be facilitating a

A

Catabolic reaction

25
Q

Catabolic reactions are

A

Exergonic

26
Q

Feedback inhibition

A

This is when a product of an enzyme in a series of the biochemical process does not get consumed by another reaction so it accumulates and binds to the allosteric site of the first enzyme and therefore stops the entire process from progressing further

27
Q

Effect of PH on active site

A

Changes the charges of the amino acid residues

28
Q

What happens to enzymes when you increase the acidity?

A

H+ ions are increased
COOH- will become COOH
No COOH (carboxyll groups for enzymes to join with.

29
Q

What happens when you increase the ph of enzymes’ environment

A

More OH- ions
Add to NH+3 to make NH2
No attraction between COOH- and NH3 .

30
Q

Inactive precursors

A

Are enzymes which can attack the cell itself so are produced in the inactive form by the cells

31
Q

Induced fit hypothesis

A

Shape of the active site varies slightly from that of the substrate and the two fit only after contact when the substrate induces a complementary shape

32
Q

Reversible inhibitors

A

Competitive
Non competitive
Mixed
Uncompetitive

33
Q

Irreversible inhibitors

A

Permanently modify the enzyme

34
Q

Uses of inhibitors

A
Poison- used for defense 
(Artificial inhibitors are used for ;) 
Drugs 
Pesticides
Herbicide 
Metabolic control
35
Q

How can the effects of inhibitors be overcomed?

A

Increasing the substrate

36
Q

Is the shape of the sure as substrate similar for a competitive or non competitive person ?

A

Competitive for similar

Non competitive have different shapes

37
Q

Where does a non competitive inhibitor bind to in an enzyme ?

A

Allosteric site

38
Q

Galactosemia

A

Galactose cannot be converted into glucose 1 phosphate which is an intermediate compound of galactose

39
Q

Lactose intolerant

A

Enzyme lactase cannot be produced

40
Q

PKU Phenylketonuria

A

Phenylaune hydroxylase enzyme is missing.