Module 2 - Enzymes Flashcards

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1
Q

What is an enzyme?

A

An enzyme is a biological catalyst that can speed up metabolic reactions in living orgs

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2
Q

What can catalysts do?

A

Speed up chemical reactions

Catalyse conversions of large amount of substrates into products

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3
Q

What is an enzymes ‘turn over number’?

A

Number of reactions that an enzyme can catalyse per second

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4
Q

Why are enzymes so efficient?

A

They can work fast in low temperatures, neutral pH and at normal pressures
More specific than chemical catalysts
Don’t produce unwanted by products/ rarely make mistakes

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5
Q

How does an enzymes structure determine its function?

A

They may need help by cofactors
If there is a gene mutation then the amino acid sequence is altered altering the tertiary structure preventing it from functioning
Causes a metabolic disorder

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6
Q

What are intracellular enzymes?

A

They are enzyme working inside a cell usually in metabolic pathways

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7
Q

What are catabolic and anabolic pathways?

A

Catabolic - breaking down of molecules into smaller ones releasing energy

Anabolic - synthesise large molecules from smaller ones

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8
Q

What is amazing about the enzyme catalase?

A
Found in nearly all living orgs
Prevents cells from being damaged by reactive oxygen by breaking down hydrogen peroxide (by product of metabolic reactions to water or oxygen) 
Fastest acting enzyme 
Contains haem group 
WBC use it to kill invading microbes
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9
Q

Describe the functions of some extra cellular enzymes

A

Amylase - produced in salivary gland and acts in the mouth to digest starch

Trypsin - made in pancreas and acts in the lumen of small intestine to digest smaller peptides

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10
Q

What is a prosthetic group?

A

A cofactor permanently bound by covalent bonds to an enzyme molecule
Eg
Enzyme carbonic anhydrase contains a zinc prosthetic group to its active site

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11
Q

What is the enzyme substrate complex?

A

Enzyme and substrate molecule temporarily bind to form this

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12
Q

Describe how two types of cofactors act

A

Some cofactors act as co-substrates by aiding the substrate to form the correct shape to bind to the active site

Some cofactors change the charge distribution on surface of enzyme active site or substrate to help make temporary bonds

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13
Q

What are co enzymes?

A

Small organic non-protein molecules that temporarily bind to active site of enzymes

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14
Q

What is the Lock and Key Hypothesis?

A

Active site has a complimentary shape to the substrate molecule like a key fitting into a lock
Either molecules are formed or broken

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15
Q

What is the ES and EP complex?

A

ES is the enzyme substrate complex

EP is the enzyme product complex

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16
Q

How are these (ES/EP) formed?

A

Substrate and enzyme have kinetic energy thus always moving
If there is a successful collision the ES complex will be formed
Substrate molecules are either broken or built up into product molecules to form the EP complex

17
Q

What is the Induced Fit hypothesis

A

The active site, at the presence of a substrate, induces a shape change
Active site slightly changes shape to mould around substrate molecule
This enables the substrate to bind more effectively to the active site

18
Q

Why is induced fit hypth better than lock and key hypth?

A

This is because it explains how the transition stage (ESC) is stabilised