Enzymes

Question 1

Carbonic anhydrase

Answer 1

Zn 2+ , prosthetic

Question 2

Haemoglobin

Answer 2

Fe , prosthetic

Question 3

Amylase

Answer 3

Cl– , cofactor

Question 4

Example of a co- enzyme

Answer 4

NAD+ and FAD+

Question 5

What do NAD+ FAD+ coenzymes do?

Answer 5

Intracellular, has a role in redox reactions.

Question 6

Inactive precurser?

Answer 6

An enzyme that must undergo changes to the tertiary structure of the active site.

Question 7

A protiens catalytically active form is called a

Answer 7

holoenzyme

Question 8

A holoenzyme consists of…

Answer 8

an apoenzyme and a cofactor/coenzyme

Question 9

two types of inactive precursors I need to learn?

Answer 9

proenzyme- needs cleaving/ tertiary structure of active site must be broken down.
apoenzyme- needs a cofactor or coenzyme to become a working holoenzyme.

Question 10

What turns a proenzyme into an active enzyme? (3 things)

Answer 10

• pH change
• temp change
• cleaved by another enzyme

Question 11

How does aspirin work?

Answer 11

Inhibits enzyme that catalyses reaction that produces cell signalling molecules responsible for pain sensitivity or inflammation.

Question 12

Temperature coefficient (Q 10) equation…

Answer 12

rate of reaction x +10 °c / rate of reaction x

Question 13

what does reversible inhibition do?

Answer 13

• removes coenzyme or cofactor
• only create hydrogen bonds with substrate (no ionic or covelant)
• does not denature enzyme

Question 14

Irreversible inhibition…

Answer 14

• permanently denatures
• creates strong ionic or covelant bonds with enzyme.

Question 15

Medicines..

Answer 15

inhibit essential enzymes in pathogens

Question 16

explain the process of end product inhibition…

Answer 16

A sunstance is broken down into products by enzyme 1, and the products of this reaction are broken down by enzyme 2. The products of this reaction are broken down by enzyme 3. the products produced by this enzyme catalysed reaction act as reversible inhibitors to enzyme catalysed reaction 1.

Question 17

Why does end product inhibition occur?

Answer 17

To regulate how much product is produced.

Question 18

What is protein specificity?

Answer 18

The specific shape of the teriary structure of an active site. This forms a complex. This also applies to the protien specificity of antibodies and receptor protiens.

Question 19

Non functional protiens

Answer 19

Mutated or denatured proteins that can not function.

Question 20

Explain the effects of mutations on protien specificity.

Answer 20

• change in base sequence of DNA or mRNA
• change in primary, secondary, tertiary, and quaternary structure.
• changes shape of binding site
• no longer complimentary.

Question 21

Explain the effects of denatured protiens on protein specificity?

Answer 21

• increased kinetic energy
• bonds (hydrogen) between R groups of amino acids.
• disulfide bonds not easily broken.
• change to teriary structure of active site.
• no E-S complex can form.

Question 22

explain an example of end product inhibition…

Answer 22

• the production of ATP
• this involves a series of reactions that transform glucose into ATP.
• ATP molecules inhibit an enzyme in the early stages of the metabolic pathway.

Question 23

digestion of starch

Answer 23

• first broken down by amylase into maltose
• then broken down into glucose in the small intestine by maltase

Question 24

V max

Answer 24

point at which all enzymes become saturated.

Question 25

Anabolic

Answer 25

reactions that build up/ cause growth

Question 26

catabolic

Answer 26

resction that break down

Question 27

metabolic pathway

Answer 27

a series of reactions all catalysed by enzymes