Enzymes, uncertainty Flashcards

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1
Q

What are enzymes

what effects enzyme action

A

Biological catalysts and globular proteins

temperature and PH

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2
Q

How do enzymes bind to substrates and what do they form

A

They bind to a complementary active site by colliding at the right speed and orientation and forms an
Enzyme substrate complex

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3
Q

What leads to enzyme specificity

A

the tertiary structure (determines the active site)

specificity of an enzyme is a result of the complimentary nature

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4
Q

What is a catabolic and an anabolic reaction

A

Catabolic = breakdown of complex molecules into simpler products e.g. respiration

anabolic = building of more complex molecules from simpler ones

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5
Q

What is the induced fit model

A

-enzyme and substrate interact with each other
- The enzyme and its active site can change shape slightly as the substrate binds
- The changes in shape are called conformal changes
-Ensures an ideal binding arrangement
- Maximises ability to catalyse reactions

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6
Q

how does temperature effect enzyme reaction

A
  • Have specific optimum temperature
  • Lower temperature - less kinetic energy - less enzyme substrate complexes formed - lower rate of reaction
  • Higher temperature - Higher kinetic energy - more enzyme substrate complexes formed - higher rate of reaction
  • if temp too high or too low bonds in the tertiary structure break changing it meaning the enzymes denature
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7
Q

What goes on the X and Y axis of a graph

A

X = IV
Y = DV

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8
Q

what is interpolation and extrapolate mean

A

interpolation- Reading of values in between existing data points
extrapolate - Going beyond the range of points to read values

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9
Q

How do you work out the percentage error

A

percentage error=
(uncertainty/measured value) x 100

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10
Q

How does pH affect enzyme action

A
  • Enzymes have an optimum pH
  • Hydrogen and ionic bonds holding together the tertiary structure can break
  • Bellow and above optimum pH solutions with excess H+ ions (acids) and excess OH- ions (alkali) will cause bonds to break
  • Alters the shape of the active site
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11
Q

How can the pH be calculated be calculated if we know the H+ value

A

pH =
-log^10 (H+)

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12
Q

What does a pH buffer do

A

inhibits the change of pH

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13
Q

How does enzyme concentration effect enzyme action

A
  • higher the enzyme concentration in a reaction, the greater number of active sites and likelihood of enzyme-substrate complex formation
  • As long as there’s sufficient substrate available the rate of reaction will increase
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14
Q

How does substrate concentration affect enzyme action

A
  • More substrate molecules increase the likelihood of enzyme-substrate complexes forming
  • if enzyme concentration remains fixed but the amount of substrate rises past a certain point, all available active sites will become saturated and any further increase of the substrate will not increase the rate of reaction
  • When active sites of enzymes any added substrate will have no active site to bind too
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15
Q

What do enzyme inhibitors do?

A

Enzyme activity can be reduced or stopped, temporarily by a reversible reaction

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16
Q

What are the different types of enzyme inhibitors and explain what they do

A

competitive - Have a similar shape to the substrate, they compete with the substrate for the active site blocking it so substrates cannot bind and create ES- complexes

non-competitive - Inhibitors bind to the allosteric site altering the shape of the active site preventing a substrate form binding

17
Q

What do reversible inhibitors do

A
  • can act as regulators in metabolic pathways because metabolic reactions b=must be tightly controlled and balanced
  • Its controlled by using the end product of a ES-complex by it becoming a non competitive inhibitor
18
Q

What happens to a competitive and non-competitive inhibitor when the substrate concentration is increased?

A

. competitive - The rate of reaction will still increase. increasing the concentration of substrates will reverse the effects of the competitive inhibitor as the substrate will out-compete it for active sites
. non-competitive -Will not effect the rate of reaction. Substrates will still not be able to bind to the active site

19
Q

What happens if the concentration of inhibitors increases

A

Rate of reaction will decrease because less Es-complexes can be formed. If the concentration still continues to rise the reaction will stop completely