3. Enzymes Flashcards

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1
Q

Define activation energy

A

Energy needed in a chemical reaction for a product to form

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2
Q

(Q1) What is the activation energy of the reaction in the presence of the enzyme?

A

A

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3
Q

(Q2)Which statement explains how the substrate is able to enter the active site of the enzyme?

A

Contact between the substrate and the enzyme causes a change in the enzyme shape.

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4
Q

(3) why did the actual rate of reaction decrease over time?

A

Substrate molecules were used up

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5
Q

(4) Catalase is an enzyme that catalyses the conversion of hydrogen peroxide into water and oxygen.
Two students investigated the effect of enzyme concentration on the rate of reaction of the
enzyme catalase. The students predicted their results would show the same trend. The graphs
show the rates obtained by each student.

A

Student 2 used a lower concentration of substrate in the investigation

can’t be temp bc that’s not what they’re studying and changing

can’t be pH bc that’s also kept constant

can’t be inhibitor bc that’s not what they’re studying

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6
Q

What is an enzyme inhibitor?

A

Something that inhibits the rate of enzyme activity

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7
Q

What is a competitive inhibitor?

A

It has a similar shape to the substrate and temporarily fits into the enzymes active site, competing with the substrate

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8
Q

What can make a competitive inhibitor reversible?

A

Increasing the substrate concentration will reduce effect of inhibitor

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9
Q

What is non-competitive inhibition? 2

A

It doesn’t bind to the active site, but another part of the enzyme

causing a change in the enzymes shape so it’s no longer complementary

Increasing substrate has no effect

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10
Q

What level of protein structure is always involved in competitive and non-competitive inhibitors of enzymes?

A

tertiary

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11
Q

How do you calculate mean?

A

Sum of terms divided by number of terms

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12
Q

what is an enzyme-substrate complex?

A

a temporary molecule formed when the substrate binds to the enzyme

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13
Q

(7) which graph shows the change in concentration of enzyme substrate complex?

A

A

not B bc not just concentration but CHANGE in concentration

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14
Q

What is the lock and key hypothesis

A

Active site has perfectly complementary shape to substrate

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15
Q

What is induced-fit hypothesis?

A

Active site, or sometimes substrate, can change shape slightly to fit together better for more efficient enzyme activity

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16
Q

What do the lock and key and induced fit hypotheses have in common

A

Substrate is converted to product by specific R groups in the active site

17
Q

Lysozyme is secreted from tear glands & forms deposits in contact lenses. How would one clean this?

A

Protease dissolves lysozyme

18
Q

(13) Which graph statement is correct?

A

Between X & Y, the number of enzyme molecules is limiting

19
Q

What is involved in enzyme regulation? 3

A

Change in enzyme concentration

Change in substrate concentration

Inhibition by final product of reaction

20
Q

What type of bond is formed between an enzyme and a substrate?

A

Hydrogen bond

21
Q

How do you plot the initial rate of reaction? 3

A

draw a tangent to the curve at the start of the reaction

Find an easy- to read part of the scale to stop drawing

Make triangle as big as possible

22
Q

How do you calculate the initial rate of reaction? 2

A

Calculate the gradient of line

Change y / change x

23
Q

(18) which graph represents action of a non-competitive inhibitor?

A

A

24
Q

Which orders of protein structure control the shape of the active site

A

Primary, secondary, tertiary & quaternary

25
Q

(20) n an experiment, 5cm^3 of 1% salivary amylase is added to 100cm^3 of different concentrations of starch

Which graph shows the results of plotting the initial rate of reaction (y axis) against substrate concentration (x axis)

A

A