[bio] enzymes Flashcards

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1
Q

what are enzymes & function?

A

biological catalysts that speed up the rate of chemical reactions without themselves being chemically changed at the end of chemical reactions

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2
Q

can enzymes be reused?

A

yes

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3
Q

what type of concentrations are enzymes effective in?

A

small concentrations

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4
Q

what are catabolic reactions?

A

chemical reactions which break up complex molecules into simpler molecules

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5
Q

example of catabolic reactions

A

hydrolysis - digestion in the alimentary canal

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6
Q

what are anabolic reactions?

A

chemical reactions which build up simpler molecules into complex molecules

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7
Q

examples of anabolic reactions

A

condensation reaction - synthesis of proteins from amino acids

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8
Q

strucutre of enzymes

A

most enzymes are proteins with unique 3-dimensional strucutre

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9
Q

characteristics of enzymes

A

specific in action

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10
Q

what is an active site?

A

the site where substrates bind

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11
Q

what is a substrate?

A

substrate is the molecule which an enzyme acts on

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12
Q

how do enzymes speed up the rate of chemical reactions?

A

lowering the activation energy

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13
Q

what is activation energy?

A

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

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14
Q

how does lowering the activation energy allow faster chemical reactions?

A
  • increases the speed of the reactant molecules/substrates
  • collide more frequently and more forcefully in the correct orientation for chemical reactions to occur
  • hence, higher rate of effective collision
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15
Q

how does heating affect the enzymes?

A

when the temperature goes beyond the optimum temperature, the enzymes will be denatured and loses its 3d shape. This process is irrreversible

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16
Q

explain the lock-and-key hypothesis

A
  • the substrate is the “key”, and the enzyme is a “lock”
  • the substrate, whose shape is complementary to the shape of the active site of the enzyme
  • the substrate will fit exactly into the active site of the enzyme
  • the substrate enters the active site, and binds with the active site
  • enzyme-substrate complex is formed
  • after the chemical reaction occurs, the products no longer fit the active site, and will get released
  • the enzyme will be ready for the next reaction
17
Q

explain the induced fit model

A
  • the substrate, whose shape is complementary to the shape of the active site of the enzyme
  • shape of the active site will change slightly to fit the substrate more snuggly
  • the substrate enters the active site, and binds with the active site
  • enzyme-substrate complex is formed
  • after the chemical reaction occurs, the products no longer fit the active site, and will get released
  • the enzyme will be ready for the next reaction
18
Q

factors affecting the rate of reaction

A
  1. temperature
  2. pH
  3. enzyme concentration
  4. substrate concentration
19
Q

what is optimum temperature

A

the temperature at which the rate of enzyme activity is at its maximum

20
Q

general range of optimum temperature

A

37 to 45 degree Celsius

21
Q

what happens to enzyme at low temperature?

A

rate of enzyme activity is low at low temperatures of near or below 0deg.C, enzymes are less active at low temperatures, but structure is intact
it is a reversible condition where enzymes increases in activity when temperature increases.

22
Q

what happens from low temperature to optimum temperature?

A

as temperature increases, kinetic energy of substrate and enzyme molecules increases. enzymes start to be more active. substrate and enzyme molecules collide more often, and this increases the chances of effective collisions and formation of enzyme-substrate complexes and thus the rate of reaction increases

23
Q

what do you mean by effective collision?

A

it means that the substrate has entered the active site

24
Q

what happens at the optimum temperature?

A

the rate of reaction is the highest

25
Q

what is the optimum temperature of the human body?

A

usually higher than 40degC

26
Q

what happens to the enzyme beyond the optimum temperature?

A

as temperature increases beyond the optimum temperature, rate of reaction starts to decrease
the enzyme is denatured and loses its 3d shape and its active site is unable to bind to the substrate as their shapes are no longer complementary.
therefore, enzyme-substrate complex cannot be formed and the rate of reaction decreases to zero

27
Q

what happens after an enzyme is denatured? can it be reversed?

A

no, once an enzyme is denatured, it is irreversible, and it cannot regain its function even when the temperature is lowered

28
Q

what is optimum pH of an enzyme?

A

the pH at which enzyme activity is at its maximum

29
Q

what happens when an enzyme is at extreme pH?

A

at extreme pH, the enzyme is denatured, loses its 3d shape and the active site is unable to bind to the substrate. therefore, enzyme-substrate complex cannot be formed

30
Q

what is a limiting factor?

A

a limiting factor is any factor that is in the shortest supply

31
Q

effect of varying enzyme concentration (at low, high and maximum)

A
  • at lower enzyme concentration, adding more enzyme increases the rate of chemical reactions [enzyme concentration is limiting]
  • when the enzyme concentration increases, more effective collision occurs, resulting in the formation of more enzyme-substrate complexes
  • at the plateau, the rate of reaction becomes constant and enzyme concentration is no longer a limiting factor. instead, substrate concentration is limiting.
  • there are not enough substrates to occupy all the active sites of the enzymes
32
Q

effect of varying substrate concentration (at low, high and maximum)

A
  • at low substrate concentrations, few substrate molecules are present. hence, there are many available enzyme active sites for effective collision to occur
  • the rate of reaction increases with an increases in substrate concentration until a point when further increase in substrate concentration will no longer increase the rate of reaction
  • the rate of reaction becomes constant and reaches a plateau
  • at higher substrate concentrations, increasing the concentration of substrate cannot increase rate of reactions. enzyme concentration is the limiting factor.
  • this is because all active sites of the enzyme molecules are saturated with substrate molecules, and the concentration of product formed per unit time remains the same
33
Q

how to measure the rate of reactions?

A
  1. measuring the rate of concentration/volume/mass of products formed
  2. measuring the rate of concentration/volume/mass of reactants used up