Enzymes as catalysts Flashcards

1
Q

Enzymes do what

A

Speed up reaction without being change during the reaction or affecting the equilibirum

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2
Q

Chemical catalysts vs enzyme catalysts

A

enzyme don’t usually produce side reactions whereas chemical ones do

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3
Q

Describe how the enzyme binds the substrate and the energy involved

A

The substrate binds the enzyme at the active site. The enzyme will then conform more closely to the shape of the substrate. Then the enzyme will match the transition state of the substrate pushing it towards that and then it will will push the substrate to its product form and this whole process is energetically favorable so it will push it forward to completion.

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4
Q

Factors that affect enzyme activity

A
  1. substrate concentration
  2. Temperature
  3. pH
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5
Q

how does substrate concentration affect enzyme activity

A

rate of enzyme-catalyzed reaction will increase the more that substrate is added until a certain point when Vmax is reached. All available active sites are saturated.

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6
Q

temperature

A

reaction rate will increase as temperature increases until a certain temp is reached than anything over than maximum temp will denature the enzyme.

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7
Q

pH

A

each enzyme works best at a specific pH, and anything over or under this ideal pH can denature the enzyme

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8
Q

oxidoreductases

A

add or remove one or more electron from or to substrates (often called dehydrogenases)

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9
Q

transferases

A

transfer a group from one substrate to another (ex. kinases)

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10
Q

hydrolases

A

carry out the hydrolysis of substrates (ex. phosphtases)

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11
Q

lyases

A

carry out the cleavage of a molecule into parts

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12
Q

isomerases

A

rearrange a substrate into an isomeric form

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13
Q

ligases

A

join molecules together by condensation, usually eliminating water

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14
Q

gibbs free energy

A

it is the difference between energy of the products and the substrates

if it is negative is is favorable and occurs spontaneously

enzymes change the rate at which equilibirum is achieved but they do not change equilibirum

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15
Q

energy coordinate diagram

A

the bigger the activation energy the slower the conversion from substrate to product.

enzymes can lower this activation energy

enzymes do not change delta G

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16
Q

four ways enzymes increase rate of reaction

A
  1. binding energy: the binding of the substrate with the active site liberates energy, which brings the substrate closer to its transition state quicker
  2. proximity: the binding of the enzyme and substrate increases concentration within active sites. If they are already in contact the reaction will occur quicker. They don’t have to randomly collide with each other if they are already in contact with each other.
  3. Induced Fit: Substrate binds to enzyme, which conforms tertiary structure of enzyme, which in turn further increases the affinity of the enzyme for the substrate and pushes the substrate towards the transition state
    4: The geometry of the substrate will allow it to slide right into the active site easier and increase the reaction rate.
17
Q

serine proteases

A
  • enzymes that hydrolyze specific peptide bonds in proteins (splits the protein into small polypeptides)
  • hydrolyze amide bonds adjacent to specific amino acid residues
  • digestion
  • synthesized in the pancreas as pro-enzymes or zymogens that are initially inactive. Activated after released from the pancreas
18
Q

chymotrypsin

A

favors aromatic residues and large non polar residues

19
Q

trypsin

A

negatively charged residue in its binding pocket that favors lysine and arginine

20
Q

elastase

A

favors binding of alanine or glycine