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Biology > C1.1 > Flashcards

C1.1 Flashcards

Enzymes and metabolism

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1
Q

What are enzymes?

A

proteins that function as biological catalysts

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2
Q

What are catalysts?

A

a substance that speeds up the rate of a chemical reaction. They are effective in small amounts and remain unchanged at the end of the reaction

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3
Q

How are enzymes classfied?

A

according to the reaction they catalyse

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3
Q

What is anabolism?

A

the synthesis of complex molecules from simpler molecules including the formation of macromolecules from monomers by condensation reactions

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3
Q

What is catabolism?

A

the breakdown of complex molecules into simpler molecules including the hydrolysis of macromolecules into monomers

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4
Q

what is the substrate?

A

the starting substance or reactant in a reaction catalyzed by an enzyme. It is the molecule which the enzyme reacts with

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4
Q

What is the product?

A

what the substrate is converted to after the reaction catalysed by the enzyme

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5
Q

What is the active site?

A

region of an enzyme molecule where the substrate molecule hinds and catalysis occurs

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5
Q

What is the enzyme-substrate complex?

A

the temporary structure formed when a substrate binds to the active site of the enzyme

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6
Q

What is the induced-fit model?

A

the binding of the substrate to the enzyme causes a change in the shape of the enzyme and the substrate resulting the proper alignment of the catalytic groups on its surface which enable catalysis to take place

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6
Q

What is the Lock and key model?

A

when the active site of the enzyme is the complementary shape of the substrate and so fits to the substrate precisely.

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6
Q

What type of reactions does an enzyme catalyse?

A

each enzyme catalyses either a single chemical reaction or a group of closely related reactions.

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7
Q

How do the substrate and active site come together?

A

through collisions between the two thats caused by kinetic energy in both of them.

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8
Q

What is an immobilized enzyme?

A

an enzyme attached to an inert, insoluble material, enabling recovery, reuse and improved enzyme stability

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9
Q

What are the advantages of using an immobilized enzyme in an industrial process?

A

it permits the reuse of the enzyme preparation
the product is enzyme free
the enzyme may be much more stable and long lasting, due to protection by the inert matrix

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9
Q

What is the EIM system?

A

the enzyme immobilized on or in a membrane is a widely used method in food processing or pharmaceuticals

10
Q

What type of protein is an enzyme?

A

Globular

10
Q

What is Denaturation?

A

denaturation occurs when weak intermolecular interactions within the globular protein break, changing the 3 dimensional shape of the active site.

11
Q

What is the impact of denaturation?

A

since the shape of the active site has changed, the enzyme and substrate can no longer bind together.

11
Q

What is the effect of temperature on enzymes?

A

proteins are denatured by heat, hence the rate of denaturation increases at temperatures higher than the optimum so at the temperature rises the amount of enzyme activity progressively decreases and the rate of reaction is slowed.

12
Q

What is catalase?

A

the enzyme which catalyzes the breakdown pf hydrogen peroxide

12
Q

What are the effects of PH on enzymes?

A

a change in ph alters the bonding patterns, progressively changing the 3d shape of the molecule rendering the active site inactive, however unlike temperature this may be reversed if the change in PH is not too extreme

13
Q

What is activation energy?

A

the small amount of energy needed to initially weaken or break down the bond of the substrate

14
Q

What are extracellular enzymes?

A

an enzyme secreted by the cell through endocytosis that carries out functions outside the cell

15
Q

What are intracellular enzymes?

A

an enzyme that functions within the cell it was produced

15
Q

What is an exergonic reaction?

A

reactions that release free energy

16
Q

What is free energy

A

the energy in a stored molecule that can be used to do work

17
Q

What are endergonic reactions?

A

reactions where energy is absorbed back into the cell

17
Q

What is a linear metabolic pathway?

A

a series of enzyme-catalysed reactions that run in one direction, from reactant to product

17
Q

What are cyclical metabolic pathways?

A

a circular series of enzyme-catalysed reactions where there is no end to the series, one reaction leads to the next and eventually back to the starting point

18
Q

What is a metabolic pathway?

A

sequence of enzyme-catalyzed biochemical reactions in cells and tissues

19
Q

What are competitive inhibitors?

A

a substance that binds to the active site of an enzyme, slowing or blocking the enzyme action.

19
Q

What are enzyme inhibitors?

A

a substance that slows down or blocks enzyme action

19
Q

What are non-competitive inhibitors?

A

a substance that does not bind to the active site but to another part of the enzyme slowing or blocking enzyme action

20
Q

What are allosteric regulators?

A

molecules that change the shape and activity of an enzyme by reversibly binding to a site on the enzyme

21
Q

What is the rate of an enzyme-catalysed reaction?

A

the amount of substrate that has disappeared of the amount of product that has been created in a period of time

21
Q

What is a statin?

A

any of a class of drugs that lower the level of low-density lipoproteins in the blood by inhibiting the activity of an enzyme involved in the production of cholesterol in the liver. They are examples of competitive inhibitors

22
Q

What is end-product inhibiton?

A

when the product of the last reaction in a metabolic pathway inhibits the enzyme that catalyses the first reaction of the pathway

23
Q

What is mechanism-based inhibition?

A

a process that occurs when unreactive molecules are transformed into an active form through catalytic reactions, these active forms inhibit the enzyme, typically through covalent modification of the active site. It is an irreversible form of enzyme inhibition

Biology (13 decks)

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