Enzymes Flashcards

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1
Q

what are enzymes?

A

biological catalyst which speed up the rate of chemical reactions without lowering the activation energy

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2
Q

Why are enzymes different shapes?

A

because it is made from a unique sequence of amino acids

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3
Q

Why is the shape of the enzyme important?

A

vital for its function

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4
Q

what is the active site?

A

part of an enzyme where molecules (substrate) can fit during a reaction

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5
Q

if the shape of the active site is changed..?

A

Then the enzyme will not work as the enzyme will be denatured

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6
Q

what type of proteins are enzymes?

A

globular proteins, tiertiary structure

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7
Q

what is the activation energy?

A

the minimum amount of energy required for a reaction to start

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8
Q

other functions of proteins?

A

biological catalysts, control the rate of metabolic reactions

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9
Q

explain enzyme activity using the lock and key model?

A

an enzyme has a specific active site. the substrate will have a complimentary shape and size to the enzymes active site and fit in/binds to the enzymes active site. The enzymes active site will break down the substrate into smaller molecules.

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10
Q

limitations of the lock and key model?

A

Enzymes are not a fixed shape like a ‘lock’. It explains how other molecule affect enzyme action (by binding away from the active site). It explains how activation energy is lowered (by
changing shape the enzyme puts a strain on the
substrate molecule and distorts the bonds)

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11
Q

explain enzyme activity using the induced fit model?

A

the enzyme has a specific active site. the substrate will be complimentary and fit into the active site.This is the inital binding. then the enzyme changes shape and the substrate will fit more closely and strongly to the active site. This is called the induced fit. and the enzyme will break down the substrate then release the products.

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12
Q

factors effecting the rate of enzyme-controlled reactions?

A

temperature, pH, enzyme concentration, substrate concentration and inhibitors

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13
Q

Explain how temperature effects the rate of reaction?

A

increasing temperature increases the kinetic energy of the molecule so there is faster movement. Collisions between enzyme and substrate or more frequent and energetic the rate of reaction increases.

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14
Q

explain how temperature effects the rate of reaction? (high temperature)

A

The enzyme molecule vibrates so much that the weak bonds maintaining the tertiary structure are broken hydrogen and ionic bonds cannot reform so the shape of the molecule changes and the active site can no longer function. It is denatured

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15
Q

explain how pH effects the rate of reaction?

A

Changing pH alters the amount of hydrogen and hydroxyl ions these are attracted to the charges on the amino acids in the polypeptide to strong bonds altering the enzyme shape

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16
Q

what pH does intracellular enzymes work best in?

A

7.3-7.45

17
Q

what pH do extracellular enzymes work best in?

A

at extreme pH e.g pepsin =pH2

18
Q

what is the pH of chymotrypsin?

A

pH8

19
Q

explain how substrate concentration effects the rate of reaction?

A

As substrate concentration increases so does the rate of reaction as more collisions can occur between substrate and enzyme until all the active sites of failed. when all the artists sites have filled the rate is limited by enzyme concentration and can only be increase if more enzyme is added

20
Q

explain how enzyme concentration effects the rate of reaction?

A

As enzyme concentration increases so does the rate of reaction as more collisions can occur between substrate and enzyme until all the substrate is used. there are many enzymes with empty active sites but the substrate concentration is the limiting factor.

21
Q

what are enzyme inhabitors?

A

slow down or stop enzyme reactions

22
Q

explain competitive enzyme inhibition on the rate of reaction ?

A
  • the 3d tiertiary structure of proteins gives enzymes the specific shape of an active site. - competitive inhibitors are similar in shape to the substrate and bind to enzymes active sites. this prevents the substrate from binding to the active site and no enzyme substare complexes form. instaed a enzyme-inhibitor complex is formed. this decreases the ROR. The ROR increases with a hgher substrate concentration
23
Q

explain non-competitive enzyme inhibition on the rate of reaction?

A

the 3D tertiary structure of proteins give enzymes the specific shape of an active. the enzyme also has another active site away from the original called the allosteric site. the non-competitive inhibitor is not similar in shape to the substrate and binds away from the from the active site to the allosteric site. this changes the shape of the active site so the substrate cannot bind to the active site so no enzyme-substrate complexes are formed. this decreases the rate of reaction.

24
Q

what are the uses of inhibitors?

A

many enzyme inhibitors are natural poisons so inhibitors in venom can irreversibly block enzymes which cause death and paralysis

25
Q

ph caluclations?

A

pH = -log[H+]

26
Q

what is the definition of pH?

A

pH is equal to the negative log of the hydrogen ion concentration of a solution