Enzymes Flashcards

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1
Q

What are enzymes?

A

Protiens that act as biological catalysts for intra and extracellular reactions to determine strucutre and function. Therefore affect the metabolism of cells and whole organisms.
Specific tertiary structure determines shape of active site, complementary to a specific substrate
Formation of enzyme substarte complexes lowers activation energy of metabolic reactions

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2
Q

What is an example of an enzyme that catalyses intracellular reactions?

A

Catalase: catalyses decomposition of hydrogen peroxide into water and oxygen

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3
Q

What is an example of enzymes that catalyse extracellular reaction?

A

Amylase- carbohydrates catalyses digestion of startch to maltose in saliva/ small intestine lumen.
Trypsin- pancreatic endopetidase catalyses hydrolysis of peptide bonds in the small intestine lumen.

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4
Q

What are the 5 factors that affect the rate of enzyme-controlled recations?

A
Enzyme concentration 
Substrate concentration
Concetration of inhibitors 
pH
Temperature
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5
Q

What are cofactors?

A

Non-protein conpounds required for enzyme action:
Coenzymes
Inorganic cofactors
Prosthetic groups

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6
Q

What are coenzymes?

A

Organic cofactors. Do not bind permanently. Often transport molecules or electrons between enzymes.
Frequently derived from water-soluble vitamins

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7
Q

What are inorganic cofactors?

A

Facilitate temporary binding between substrate and enzyme. Often metal ions.

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8
Q

What are prosthetic groups?

A

Tightly-bound cofactors act as a permanent part of enzymes binding site

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9
Q

What are active sites?

A

indented area on the surface of an enzyme molecule, with a shape that is complementary to the shape of the substrate molecule.

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10
Q

What are catalysts?

A

A chemical that speeds up the rate of reaction and remains unchanged and reusable at the end of reaction.

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11
Q

What is a metabolism?

A

The chemical reactions that take place place inside living cells or organisms

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12
Q

What is an enzyme-substrate complex?

A

A complex formed by temporary binding of enzyme and substrate molecules during an enzyme-catalysed reaction.
Enzyme molecule with substrate molecule in its active site, The two are joined temporarily by non-covalent bonds.

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13
Q

What is an enzyme-product complex?

A

Enzyme molecule with product molecule(s) in its active site. The two are joined temporarily by non-covalent forces.

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14
Q

What is a buffer?

A

Something that resists the changes in pH.

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15
Q

What is the competive inhibition of enzymes?

A

Inhibition of an enzyme, where the inhibitor molecule has a similar shape to that of the substrate molecule and competes with the substrate for the enzyme’s active site. It blocks the active site and prevents the formation of enzyme-substrate complexes.

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16
Q

What is non-competitive inhibition?

A

Inhibition of an enzyme, where the competitor molecule attaches to a part of the enzyme molecule but not the active site. This changes the shape of the active site, which prevents ES complexes forming, as the enzyme active site is no longer complementary in shape to the substrate molecules.

17
Q

What is an inhibitor?

A

A substance that reduced or stops a reaction