Enzymes Flashcards

0
Q

What type of proteins are enzymes ?

A

Globular

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1
Q

Why do reactions increase their rate due to temperature ?

A

More kinetic energy

More collision between substrate and active site

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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.

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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
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4
Q

What is the purpose of anabolic and catabolic reactions ?

A

To maintain balance - homeostasis

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5
Q

Exergonic reaction

A

Release energy

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6
Q

Endergonic

A

Absorb energy

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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

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8
Q

Enzymes have varying degrees of specificity ?

A

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

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9
Q

The lock and key model

A

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

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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.

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11
Q

How is a substrate complementary to its enzyme?

A

Shape
Charge
Hydrophobic or hydrophilic nature

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12
Q

What amino acids line the active site ?

A

Substrate binding amino acids

Catalytic amino acids

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13
Q

Coenzyme

A

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

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14
Q

Examples of coenzymes

A

NAD
FAD
Actyl

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15
Q

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

A

Substrate binding amino acids

Catalytic amino acids

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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
Enzymes that involve in breaking down bonds are said to be facilitating a
Catabolic reaction
25
Catabolic reactions are
Exergonic
26
Feedback inhibition
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
Effect of PH on active site
Changes the charges of the amino acid residues
28
What happens to enzymes when you increase the acidity?
H+ ions are increased COOH- will become COOH No COOH (carboxyll groups for enzymes to join with.
29
What happens when you increase the ph of enzymes' environment
More OH- ions Add to NH+3 to make NH2 No attraction between COOH- and NH3 .
30
Inactive precursors
Are enzymes which can attack the cell itself so are produced in the inactive form by the cells
31
Induced fit hypothesis
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
Reversible inhibitors
Competitive Non competitive Mixed Uncompetitive
33
Irreversible inhibitors
Permanently modify the enzyme
34
Uses of inhibitors
``` Poison- used for defense (Artificial inhibitors are used for ;) Drugs Pesticides Herbicide Metabolic control ```
35
How can the effects of inhibitors be overcomed?
Increasing the substrate
36
Is the shape of the sure as substrate similar for a competitive or non competitive person ?
Competitive for similar | Non competitive have different shapes
37
Where does a non competitive inhibitor bind to in an enzyme ?
Allosteric site
38
Galactosemia
Galactose cannot be converted into glucose 1 phosphate which is an intermediate compound of galactose
39
Lactose intolerant
Enzyme lactase cannot be produced
40
PKU Phenylketonuria
Phenylaune hydroxylase enzyme is missing.