Enzymes I Flashcards

1
Q

What are enzymes?

A

Proteins that speed up the rate of chemical reaction

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2
Q

Function of enzymes

A

○ Digestion of carbohydrates, fats and proteins
○ Blood clotting (thrombin, thromboplastin)
○ Defence-immune system-activation of complement
○ Movement
Nerve conduction
Drug targets

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3
Q

How do enzymes speed up rate of reaction?

A

Increase rate of reaction by choosing the pathway with a lower activation energy

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4
Q

Properties of enzymes

A

Specific
Defects in enzymes cause disease
Drug targets
Do not change position of equilubrium

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5
Q

What are Cerebrosides?

A

Glycosphingolipids which are an important component in animal muscle cells

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6
Q

Active site and the evidence of the way it works

A

• 3D cavity binds to substrate using forces like electrostatic, hydrogen bonding, hydrophilic and hydrophobic
○ Evidence from X-ray crystallography

Kinetic studies of enzyme activity

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7
Q

Induced fit theory

A

The active site senses the substrate and the active site changes shape slightly

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8
Q

Substrate binding

A
  • There is a limit to how many substrates an enzyme can process in a given time
  • An increase in concentration increases rate at which product is formed eventually reaching a maximum value(Vmax)
  • Another parameter used to characterize an enzyme is its Km(the concentration of substrate that allows the reaction to proceed at one-half its maximum rate(0.5 Vmax)
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9
Q

Drug targets in antibiotics example

A

Penicilin’s inhibit cell wall synthesis

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10
Q

Drug target in anti-inflammatory agents example

A

Aspirin block prostaglandin

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11
Q

Drug target in anti-cancer drug example

A

§ Methotrexate is a folate analogue

Interferes with synthesis of DNA precursors

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12
Q

What diseases can enzyme defects cause?

A

○ Phenylketonuria
Glycogen storage disease
Tay-sachs disease

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13
Q

What happens in phenylketonuria?

A

Cannot convert Phe to Tyr

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14
Q

What happens in tay sachs disease?

A

Membrane Cerebroside

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15
Q

What is more favourable and drives a reaction?

A

Drop in free energy

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16
Q

What is the equation for turnover number?

A

Vmax/[enz]total

17
Q

How is enzyme activity regulated?

A
  • Control of gene expression amount
  • Compartmentation
  • Allosteric regulation

Covalent modification of enzyme

18
Q

What is feedback inhibition?

A

End product inhibits one of the enzymes in the chain process to regulate its own production

19
Q

What is an allosteric enzyme?

A

A multi-subunit complex

20
Q

Where are the regulatory and catalytic site on allosteric enzymes located?

A

On different subunits

21
Q

How does regulation occur in allosteric enzymes?

A

Via conformational changes

22
Q

What are allosteric enzymes involved in ?

A

In feedback inhibition of metabolic pathways

23
Q

Km and Vmax in competitive inhibition

A

Km increases

Vmax remains unaffected

24
Q

Km and Vmax in uncompetitive inhibition

A

Km reduced

Vmax reduced

25
Q

Km and Vmax in non competitive inhibition

A

Km unaffected

Vmax reduced

26
Q

What is ATCase regulated by?

A

Regulated by CTP