Enzymes Flashcards

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0
Q

Properties of enzymes

A
  • Biological catalysts that speed up reactions by lowering energy required
  • made of proteins
  • specific
  • not used up during reaction
  • require optimum conditions at which they work best
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1
Q

Enzymes control what?

A

Almost every metabolic reaction in living organisms

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2
Q

Metabolism

A

Sum of all chemical reactions that occur in a cell

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3
Q

Reactants

A

Substances that participate in a reaction

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4
Q

Substrates

A

Reactants that bind to an enzyme

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5
Q

Products

A

Form as a result of a reaction

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6
Q

Metabolic pathways

A

Consist of chains of complex chemical reactions assisted by enzymes

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7
Q

Energy of activation

A
  • Amount of energy needed to cause a reaction

- enzymes allow reactions to happen at much lower EA

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8
Q

Enzyme substrate complex

A
  1. Substances attach to active site
  2. Enzyme & substrate fit together like a LOCK & KEY
  3. Enzyme holds substances at proper angle for them to react
  4. Enzymes can be reused after
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9
Q

Degradation (hydrolysis)

A

1 substrate becomes 2 products

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10
Q

Synthesis (condensation)

A

2 substrates become 1 product

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11
Q

Induced-fit model

A
  • bit different from lock & key
  • enzyme active site undergoes small change in shape to fit substrate to help reactions occur
  • after rxn, active site returns to original shape
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12
Q

Cofactors

A

Must bind to enzyme before the substrate can bind to enzyme

- enzymes that require cofactors are inactive without them

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13
Q

Coenzymes

A

Organic molecules that function as cofactors

- ex. vitamins

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14
Q

Temperature effects on rate of reaction

A
  • low: molecules move slowly, few hit enzyme or have enough energy to react - slows reaction rate
  • optimal: substrate meters enzyme & has enough energy to react
  • high: enzyme denatures and active site can’t accept substrate - slows rxn
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15
Q

pH effects on rate of reaction

A
  • low or high: affects bonds within enzyme, change structure & active site, no binding - slow
  • optimal: enzymes have specific pH where their bonds aren’t affected
16
Q

Increased Substrate concentration

A
  • more collision with enzymes, active sites fill up -> more products = fast rxn rate
  • max rate of rxn reached once enzyme sites are occupied continuously with substrate
17
Q

Enzyme concentration

A
  • Cells regulate rxn rate by regulating enzyme concentration -> high concentration = high rxn rate
  • genes turned on & off to regulate enzyme concentration
18
Q

Phosphorylation

A

When enzymes require a phosphate group to be activated

19
Q

Inhibition

A

Enzyme is prevented from binding to substrate

20
Q

Competitive inhibition

A
  • competitor molecule shaped similar to substrate
  • binds to active site but can’t react & doesn’t leave
  • May permanently disable enzymes
  • ex poisons …cyanide
21
Q

Non-competitive inhibition

A
  • binds at a site other than active site -> denatures enzyme

- often heavy metals… Lead, mercury, cadmium, etc