Enzymes

Question 1

druggable target

Answer 1

It is a protein, peptide or nucleic acid with acivity that can be modulated by a drug

Question 2

2 Types of Drugs

Answer 2

Small molecular weight chemical compound (SMOL)
Biologic (BIOL)

Question 3

Potential druggable targets

Answer 3

5000 for SMOL
3200 for BIOL

Question 4

why are more targets needed

Answer 4

There are 21000 drugs but they only cover 324 drug targets

Question 5

Four classes that drugs target

Answer 5

enzymes
GPCR
Ion channels
Transporters

Question 6

Protein functions

Answer 6

Catalysis
-Most chemical reactions in cell are catalysed by enzymes
Transport
-Transport various substances such as oxygen, ions, etc.
Information transport
-EG. Hormones

Question 7

Amino acid basic structure

Answer 7

-R group
-Amino group
- Carboxylic group
-Hydrogen

Question 8

Protein structure

Answer 8

Primary structure
- Amino acid sequence
Secondary structure
-alpha helix, beta sheet
Tertiary Structure
-3D structure formed by secondary structures
Quaternary structure
-Structure formed by more than 1 polypeptide chain

Question 9

types of enzymes

Answer 9

-Oxioreductase
-Transferase
-Hydrolase
-Lyase
-Isomerase
-Ligase

Question 10

Oxioreductase

Answer 10

It catalyses redox chemistry by transfering electrons

Question 11

Transferase

Answer 11

Cata;yses the transfer of a functional group

Question 12

Hydrolase

Answer 12

Catalyises the hydrolysis of a chemical bond

Question 13

Lyase

Answer 13

Catalyses the cleavage of a chemical bond in a manner other than hydrolysis or oxidation

Question 14

Isomerase

Answer 14

Cataylses structural rearrangement in order to form substrates

Question 15

Ligase

Answer 15

Catalyses the joinung of large molecules with a chemical bond

Question 16

atructure and function of enzymes

Answer 16

-Globular proteins that act as the body’s catalysts
-speed up reaction time
-lower the activation energy of a reaction

Question 17

‘Lock and key’ model of enzyme

Answer 17

-Active site is correct shape for substrate
-Binding alters the enzyme’s shape
-Results in conformational change of enzyme-substrate complex
-Increases catalytic activity

Question 18

Induced fit

Answer 18

Active site alters shape to maximize intermolecular bonding

Question 19

Binding strength

Answer 19

Binding must be strong enough to hold substrate long enough for reaction to occur but weak enough to allow product to depart

Question 20

Enzyme co-factors

Answer 20

The co-factor binds to the enzyme-substrate complex and supports the enzymatic process. Sometimes it is recycled and other times it must be regenerated. Includes iron, mg, coenzyme Q

Question 21

How are enzymes inhibited

Answer 21

-Competitive inhibition
-Irreversible Inhibition
-Allosteric inhibition

Question 22

Competitive inhbition

Answer 22

-Inhibitor binds reversibly
-Intermolecular bondsare involved in binding
-No reaction takes place on inhibitor as substrate is blocked from active site
-Increasing substrate concentration reverses inhibition
-Inhibitor similar structure to substrate

Question 23

E. Competitive inhbitor

Answer 23

Gleevac

Question 24

Non-competitive inhbitor

Answer 24

-Irreversible
-covalent bnd formed between inhibitor and enzyme
-substrate is blcoked from active site
-Increasing substrate conc. does not reverse inhibition
Inhibitor similar structure to substrate

Question 25

E. Non-competitive inhbitor

Answer 25

antibiotics like pencillin that bind to penicillin-binding sites in bacteria

Question 26

Non competitive allosteric inhibitors

Answer 26

-Inhibitor binds reversibly
-Intermolecular bonds
-Induced fit alters shape
-Active site is distorted and not recognized by substrate
-Increasing substrate does not reverse inhibition
-Inhibitor is not similar structure
-Active site remains unoccupied but inaccessible to natural substrate

Question 27

E. reversible Allosteric inhibitor

Answer 27

CL-140 inhibits MEK1 and MEK2 to reduce progression of cancer
(MEK inhibitor)

Question 28

what type of inhibitors does pharma favour

Answer 28

Allosteric and competitive
-Irreversible inhibiton can lead to many negative consequences by altering rate at which drugs are cleared by the body.
-Binding to ATP site of MEK1 could cause drug to bind to other ATP binding sites and have many fatal consequences