3. 1. 4. 2 Many Proteins are Enzymes Flashcards

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1
Q

What does the enzymes do to the activation energy?

A

Each enzyme lowers the activation energy of the reaction it catalyses.

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2
Q

What does the induced fit model of enzyme action state?

A

It states that a substrate binds to an active site and both change shape slightly - an ideal fit for catalysis.

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3
Q

What does the properties of an enzyme relate to?

A

The properties of an enzyme relate to the tertiary structure of its active site and its ability to combine with complimentary substrates to form an enzyme-substrate complex.

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4
Q

Describe the specificity of enzymes.

A

Enzymes have an active site where specific substrates bind forming an enzyme-substrate complex.
Active site of enzymes have specific shape to fit a substrate.

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5
Q

What is the effect of enzyme concentration on the rate of enzyme-controlled reactions?

A

rate of reaction increases as the enzyme concentration increases, until a limiting point is reached.

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6
Q

Why does rate increase?

A

More enzyme molecules can bind to more substrate molecules and catalyse the reaction.

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7
Q

Why does it reach a limiting point?

A

All the substrate has bound and adding more enzymes won’t affect reaction rate as there are no more substrates to bind to.

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8
Q

How does the substrate concentration effect the rate of enzyme-controlled reactions?

A

rate of reaction increases as the substrate concentration increases, until a limiting point is reached.

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9
Q

Why does rate of reaction increase?

A

There are more/plenty of substrates to bind to the active site of an enzyme.

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10
Q

Why does it reach a limiting point?

A

So much substrate is present that all of the enzyme active sites have substrates bound to them; enzyme molecules saturated with substrate.

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11
Q

How do competitive inhibitors work?

A
  • Compete with substrate for the binding site on enzyme
  • Binds to an enzyme and prevents real substrate from binding
  • occupy only some of enzyme active site; gradual increase in reaction rate
  • Decrease reaction rate when there’s not much substrate (can be out-competed by many substrates)
  • given enough substrate, enzyme can still reach max reaction rate
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12
Q

How do non-competitive inhibitors work?

A
  • Decreases rate of enzyme controlled reaction by binding to an allosteric site
  • Changes shape of enzyme active site
  • Unable to bind to substrate
  • Slows down product formation
  • Doesn’t affect activation energy
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13
Q

What is an allosteric site?

A

An allosteric site is a location on an enzyme molecule where a nonsubstrate molecule can bind and affect the enzymes activity.

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14
Q

How does the pH affect the rate of enzyme-controlled reactions?

A
  • Deviating from the optimum causes the enzymes active site to become denatured (change charge on enzymes, affects ionic bonding)
  • This leads to a decrease in enzyme activity; no enzyme-substrate complexes formed
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15
Q

What is the effect of temperature on the rate of enzyme controlled reactions?

A
  • Rate increases as temperature increases
  • Kinetic energy increases
  • More collisions between enzyme and substrate
  • Beyond optimum- rate will decrease as enzyme becomes denatured (H-bonds break)
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16
Q

What are the models of enzyme action?

A
  • Lock and Key
  • Induced fit
17
Q

Describe the lock and key model.

A
  • Enzyme fits exactly into active site (complimentary)
  • Form enzyme-substrate complex
  • Enzyme-product complex formed
  • Products released
18
Q

What was wrong with the lock and key model?

A

Lock and key suggests that the rigid shape of the active site of the enzyme was a precise fit for the specific shape of substrate.
However, proteins aren’t rigid and they don’t have a precise fit (not exactly complimentary).

19
Q

Describe the induced fit model.

A
  • Substrate enters enzymes active site, forming enzyme-substrate complex.
  • Enzyme forms conformational change causing conversion of substrate into products, enzyme-product complex.
  • Product is released.