Enzymes Flashcards

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1
Q

Define enzymes

A

Biological catalysts which speed up the rate of chemical reaction s without themselves being chemically changed at the end of chemical reactions. They can be reused and effective in small concentrations

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2
Q

Define catabolic reactions

A

Reactions that break up complex molecules into simpler molecules

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3
Q

Define anabolic reactions

A

Consist of chemical reactions which build up simpler molecules into complex molecules

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4
Q

Define activation energy

A

The energy that must be supplied to reactant molecules for them to react

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5
Q

Why is heating inappropriate for a biological system

A

High temperatures denature proteins and kills cells. Heating will also speed up all chemical reactions and not just the intended ones

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6
Q

Describe the lock and key hypothesis

A

Substrate is “key” and enzyme is “lock”. Substrate whose shape is complementary to shape of active site of enzyme. Active site of enzyme has specific shape into which substrate fits exactly. Substrate binds to active site of enzyme, forming enzyme-substrate complex. Once products are formed, they no longer fit into active site of enzyme and are released into surrounding medium

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7
Q

Describe the induced fit model

A

Active site of enzyme is complementary in shape but not perfect fit to substrates it catalyses. When substrate binds to the active site of the enzyme, it incudes a change in the shape of the active site. This allows the substrate to fit more tightly into the active site. Binding of substrate to active site of enzyme occur, enzyme-substrate complex is formed. Chemical reaction occurs and formed products are released into surrounding medium as they no longer fit into active site of enzyme

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8
Q

What are the characteristics of enzymes

A

They speed up chemical reactions by lowering activation energy. Enzymes are extremely efficient. They remain chemically unchanged after the reactions and can be used repeatedly, hence required in small concentration. Enzymes are specific in action due to its 3D shape

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9
Q

Define optimum temperature of enzymes

A

The temperature at which the rate of enzyme activity is at its maximum. Different enzymes have different optimum temperatures

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10
Q

What happens when temperature of enzymes is low

A

Rate of enzymes is low at low temperatures and are inactive. This is a reversible condition where enzymes increase in activity when temperature increases

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11
Q

What happens when temperature of enzyme increases towards optimum temperature

A

As temperature increase, kinetic of substrate and enzyme molecules increases. Enzymes are more active. Substrate and enzyme molecules collide more often, increases number of effective collisions and formation of enzyme-substrate complex and rate of reaction. Rate of reaction maximum at optimum temperature

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12
Q

What happens when temperature increases beyond optimum temperature

A

Rate of reaction starts to decrease. Enzyme is denatured, loses 3D shape and active site is unable to bind to the substrate. Once enzyme is denatured, it is irreversible and cannot regain function. As temperature continues to rise, more enzyme molecules are denatured which causes rate of reaction to decrease further

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13
Q

Define optimum pH

A

The pH at which enzymes activity is at its maximum. Different enzymes have different optimum pH

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14
Q

Describe the effect of pH on enzymes

A

Any pH that deviates from the optimum pH will cause rate of reaction to decrease. At extreme pH, enzyme loses 3D shape and active site is unable to bind to the substrate. When enzyme is denatured, it is irreversible and cannot regain its function

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15
Q

Define limiting factor

A

A factor that directly affects the rate of chemical reaction if quantity is changed. The value of factor has to be increased in order to increase the rate of process

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16
Q

Describe effect of varying enzyme concentration

A

Rate of reaction dependent on number of effective collisions between enzyme and substrate molecules. Adding more enzymes increase rate of chemical reaction (enzyme conc is limiting). When enzyme conc increases, more effective collision occurs, resulting in formation of more enzyme-substrate complexes. At plateau, rate of reaction is constant, and enzyme conc is not limiting factor. Substrate concentration is limiting. Not enough substrate to occupy active sites of enzymes

17
Q

Describe the effect of varying substrate concentration

A

At low substrate concentration, few substrate molecules are present, many available enzyme active sites for effective collision to occur. Rate of reaction increases with substrate concentration until point where substrate conc will not increase rate of reaction. Rate of reaction is constant and reaches plateau. Enzyme conc is limiting factor. All active sites of enzymes are saturated with substrate molecules and conc of product formed per unit time remains the same

18
Q

What are two methods of measuring rate of reaction

A

Measuring the rate of concentration/volume/mass of products formed
Measuring the rate of concentration/volume/mass of reactants used up

19
Q

How to set up a control experiment for enzymes

A

Boil the reactants to denature the enzymes and keep all other factors constant