L4 Flashcards

1
Q

What three factors determine of a chemical reaction? And how does this effect it’s rate?

A
  1. Activation energy - energy that must be overcome for chemical reaction to continue
  2. Concentration - substrate increases = increase reaction until enzyme hits saturation

Increase enzyme = increase rate of reaction

  1. Temperature - increase temp = speed up molecule movement ; slow down = low temp
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2
Q

What does activation energy mean?

A

The kinetic energy required for 2 colliding molecules to react

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3
Q

How to enzymes increase the rate of reactions?

A

Lower activation energy

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4
Q

How do enzymes differ from Catalyst? What do enzymes names tend to end with?

A

Enzymes = biological catalyst found w/in cells of the body

  • names end in “ase”.
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5
Q

Describe the characteristics of an enzyme (6)

A
  • increase reaction rate (lowering activation energy)
  • Not chemically altered
    Can be reused
  • doesn’t change chemical reaction.
  • made of protein
  • regulate cellular metabolism
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6
Q

Specificity

A

Each unique enzyme has one unique substrate

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7
Q

Saturation

A

Maximal rate of substantiate converted to product ( reaching its max amount)

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8
Q

Cofactors

A

Metals (cu+, zn+)

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9
Q

Coenzymes

A

Organic molecules
- derived from water soluble vitamins (b’s)

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10
Q

Function of an enzyme and its mechanism

A

Function = chemical reaction speeds up

Mechanism = decrease activation energy for Chemical reaction

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11
Q

How are enzymes regulated. And why is regulation important

A
  1. Allosteric regulation - regulation of enzyme by binding substrate to site other than active site
  2. Covalent Modulation - (phosphorylation) adding of phosphate
  3. Proteolytic cleavage - enzyme is released in an inactive form (zymogen)
  4. Genetic control of synthesis - cells make enzymes that are not currently present
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12
Q

Allosteric regulation

A

regulation of enzyme by binding substrate to site other than active site

Activation + inhibition

Able to turn on/off

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13
Q

Covalent modulation

A

Aka phosphorylation ( adding of phosphate)

  • turns protein on
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14
Q

Proteolytic cleavage

A

enzyme is released in an inactive form (zymogen)

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15
Q

Genetic control of synthesis

A

Cells make enzymes that are not currently present

Ex) pregnancy = lactation ( producing milk)

Males during puberty

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16
Q

Isoenzyme

A

Enzyme with same active site & substrate

17
Q

How are isoenzymes the same and how are they different?

A

Same - same active site & substrate

Different - have a few different amino acids (which help distinguish which organ)

18
Q

Describe how enzymes are used in diagnosis

A

They have different amino acids therefore, if you took a sample of each and compared it to the “diseased” one you will find the correct enzyme it belongs to and organ

19
Q

Where is the defect when an enzyme is lacking/ dysfunctional?

A

End product ( excessive accumulation of intermediates)

20
Q

Significance in pH optimum? What happens at extremes?

A

Enzymes have maximum activity at specific pH

On either side of that enzyme activity deceases ( not at its optimum or favorable amount)

21
Q

Significance of Temperature optima? What happens if it’s at extremes?

A
  • temperature optima = favorable temperature (98..6)

If above optima, enzymes will denature (unfold) slowing enzyme activity until fully denatured

If optima is below optima, molecules will slow down movement decreasing collision rate, therefore decreasing enzyme activity

22
Q

Explain how an enzyme can cause 2 substrates to join creating only one product

A

Substrates bind to enzyme ➡️ shape change bringing molecules closer together (electrons interact) ➡️ electrons interacting = covalent bond / new Chemical (product) formed

23
Q

Explain how an enzyme with one substrate can produce 2 products

A

Degradation- strain / breakdown of a chemical

Substrate binds to enzyme➡️ cause shape change putting stress onto covalent bond ➡️ breaking bond due to extreme stress