Enzymes Flashcards

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1
Q

how do enzymes increase the rate of a chemical reaction?

A

Lower the amount of activation energy needed to i make the reaction proceed.

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2
Q

What is a intracellular and extra cellular enzyme?

A

Intracellular-inside cells
Extracellular-outside cells.

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3
Q

What does the lock and key model suggest?

A

The active site is always the exact complementary shape at the optimum temp, so reactions are fastest in these conditions.

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4
Q

The enzyme combines reversible with the substrate to form a what…?

A

Enzyme-substrate complex.

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5
Q

What does the induced fit model suggest?

A

The active site changes shape to become complementary
(This ‘strained’ fit between the active site and substrate distorts a particular bond and so reduces the activation energy needed to break the bond.)

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6
Q

What is want by metabolism?

A

All reactions in the body

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7
Q

When would the rate of reaction increase in an enzyme?

A

-The temp increased
-The concentration of a dissolved reactant is increased
-Solid reactants are broken into smaller pieces
-A catalyst is used.

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8
Q

WhY is the substrate later released in the lock and key model?

A

Because when the reactions occur they no longer fit as well so are released to allow for more reactions.

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9
Q

Draw a graph of the effect of temperature on enzyme activity

A

.

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10
Q

Why do enzyme reactions produce a curve; why is it the fastest at the start and slower as it progresses?

A

More substance as the start=more ES complexes. As substrate used up fewer successful collisions.

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11
Q

What happens to an enzyme when temperature increases?

A

Enzyme and substrate molecules gain more kinetic energy so move about quicker. As a result they collide more frequent lymph so a greater number of enzyme-substrate complexes are formed.

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12
Q

What happens to enzymes at low temperatures?

A

Molecules are inactive but undamaged move around slowly so rarely collide.

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13
Q

What happens to enzymes at temp above 40 degrees?

A

-hydrogen bonds break
-tertiary structure changes
-active site changes shape and substrate no longer fits
-enzyme substrate complexes cannot form
-enzymes are denatured

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14
Q

What is an inhibitor?

A

A substance which decreases the rate of enzyme controlled reaction and may bring it to a halt.

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15
Q

How does a competitive inhibitor compete with a substrate?

A

Inhibitors are a similar shape to the enzyme. substrate it binds to the active site and blocks the substrate from binding.

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16
Q

What is the bond formed in the reversible inhibitors?

A

Weak hydrogen bonds or non-covalent bonds.

17
Q

What are the bonds formed in irreversible inhibitors?

A

Strong covalent bonds

18
Q

Draw a graph of the effect of PH on enzyme activity

A

.

19
Q

Draw a graph off the effect of increasing concentrations of substrate on enzyme activity

A

.

20
Q

Why does increasing concentration of a substance make the graph level out at a certain period of time?

A

All the active sites are occupied/saturates. the concentration of enzyme is a limiting factor.

21
Q

What does the graph look like when you increase enzyme concentration but there isn’t enough substrate molecules to occupy all the sites at one time?

A

.

22
Q

What alters if there is a change in PH?

A

It alters the charges on the amino acids which make up the active site of the enzyme. this causes some of the hydrogen and ionic bonds to break these alter the shape of the active site.

23
Q

Why do enzymes work best at the optimum PH?

A

The active site is exactly complementary to teh substrate, so the max number of ES complexes are formed.

24
Q

How does a non-competitive inhibitor decrease the rate of reaction?

A

Bind to the allosteric site which changes the tertiary structure of the enzyme, so changes the active site so the substrate cannot bind.

25
Q

What does the rate of reaction look like when the substrate reaction increases with and without a competitive inhibitor?

A

.

26
Q

What are enzymes?

A

Biological catalysts

27
Q

What is collision theory?

A

When molecules collide bonds between their atoms can break, and then new bonds can form to make new molecules.

28
Q

Sketch a graph to show the effect of increasing substrate concentration on the rate of reaction, with and without a non-competitive inhibitor.

A

.

29
Q

Enzymes catalyse both anabolic and catabolic what does this mean?

A

Anabolic= to build up
Catabolic=to break down

30
Q

What is the equation for calculating rate?

A

Amount of product/time taken.