Enzymes!! Flashcards

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1
Q

define an enzyme

A

globular protein
biological catalysts
speed up a rate of a reaction

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2
Q

define anabolic

A

this type of pathway requires energy and is used to build up large molecules from smaller ones

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3
Q

define catabolic

A

this type of pathway releases energy and is used to break down large molecules into smaller ones

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4
Q

define activation energy

A

energy needs to be supplies to start a reaction

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5
Q

describe and explain the lock and key hypothesis

A

the substrate binds to the active site forming an enzyme-substrate complex
the substrate then reacts and the products are formed in an enzyme-product complex
substrate has complementary shape to its active site

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6
Q

describe and explain the induced fit hypothesis

A

when the substrate binds to the active site, the tertiary structure of the enzyme slightly changes this is due to the weak interactions between the enzyme and substrate
this strengthens binding putting a strain on the substrate molecule

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7
Q

what are the two types on enzymes

A

intracellular

extracellular

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8
Q

describe and explain intracellular

A

enzymes that act within cells are called intracellular enzymes
hydrolytic enzymes

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9
Q

describe and explain extracellular

A

enzymes that work outside the cell

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10
Q

what are coenzymes

A

Coenzymes are organic cofactors which do not bind permanently. They facilitate the
binding of substrate to enzyme. Many coenzymes are vitamin derived, examples include
NAD derived from niacin, which acts as a hydrogen acceptor.

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11
Q

what are coefactors

A

A cofactor is a non-protein compound required for the enzyme’s activity to occur. There
are three types of cofactors: coenzymes, activators and prosthetic groups.

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12
Q

what are activators

A

Activators are inorganic metal ions which temporarily binds to the enzyme and alters its
active site, making the reaction more feasible. For instance, magnesium ion is an important
activator which is involved in processes such as shielding negative charge.

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13
Q

what are prosthetic groups

A

Prosthetic groups are permanently attached to the enzyme. For instance, haemoglobin
contains a prosthetic haem group which contains iron, permanently bound to the molecule,
which serves as a means of binding oxygen.

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14
Q

what is the precursor before and after the enzyme reaction

A

it is called an apoenzyme and after the coefactor and the enzyme is activated is added it is called a halo-enzyme

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15
Q

what happens when the enzyme has been denatured

A

vibrations increase until the bonds strain and then break
tertiary structure of the enzyme changes
active site is no longer complementary to the substrate
enzyme will no longer function as a catalyst

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16
Q

what is renaturation

A

when the pH returns to the optimum then protein will resume its normal shape and catalyse the reaction