Enzymes and active site Flashcards

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1
Q

What does the lock and key model show?

A

-Substrate is complimentary to the active site of the enzyme
-Active site doesn’t change and fits the substrate like a key in a lock
-Produces get made and active site is the same

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2
Q

What does the induced fit model show?

A

-Substrate colliding with the active site
-Active site changes shape to fit the substrate in, holds in position by opposite charged groups in animo acids in active site
-Enzyme-substrate is formed
-A change in active site shape puts strain on substrate/ brings two closer, reaction energy decreases
-Enzyme-product is formed
-Product released as no longer fits
-Active site changes to og shape

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3
Q

What is an intercellular and an extracellular enzyme?

A

Intercellular- Work inside cell
Extracellular- Secreted outside of cell

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4
Q

What is the structure and type of molecule of an enzyme?

A

-A globular 3D protein (tertiary structure)
-Very specific, catalyse only one substrate
-Active site has a complimentary shape to the substrate

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5
Q

What is made when a substrate fits into the active site?

A

Enzyme-substrate complex

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6
Q

Catabolic reaction?

A

Hydrolysis larger into smaller molecules

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7
Q

Anabolic reactions?

A

Larger molecules made by condensation of smaller ones

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8
Q

What is an enzymes turnover number?

A

No. of substrate to products per unit of time

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9
Q

How does slight and extreme difference from optimum pH do to an enzyme?

A

Slight- OH-/H+ ions intervene with the ionic bonds of the r group of amino acids causing temporary reversible changes to the 3d globular tertiary structure

Extreme- OH-/H+ ions break ionic bonds and permanent changes to the tertiary 3d structure, enzyme becomes denatured eventually

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10
Q

What are immobilised enzymes?

A

Enzymes that are attached to an inert, insoluble material

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11
Q

What are the advantages of using an immobilised enzyme?

A

-Can be reused, reduced costs
-Product can’t be contaminated by enzyme
-Easy to recover and add
-Stable at high temperatures and wide range of pH

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12
Q

What are the disadvantages of using immobilised enzymes?

A

-More expensive than free enzymes
-Immobilisation can change the shape of the active site, meaning les s-e complexes are formed

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13
Q

Ways an enzyme can be immobilised?

A

In gel membrane, in alginate beads

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14
Q

What happens when an enzyme is working at its optimum pH?

A

-Charges and shape complementary
-Working at max. turnover rate
-Max no. of e-s complexes formed and amount of substrate broken down

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