5.1 Enzymes Flashcards

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1
Q

enzyme

A

biological catalyst
speeds up chemical reactions by reducing activation energy

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2
Q

substrate

A

reactant that binds to an enzyme

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3
Q

active site

A

where substrates bind to an enzyme

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4
Q

activation energy

A

amount of energy required for a chemical reaction to occur

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5
Q

reaction specific

A

each enzyme has specific substrates that can bind to it

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6
Q

not consumed in reactions

A

one enzyme can perform many reactions

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7
Q

affected by cellular conditions

A

enzymes are made of proteins and can be denatured by the same conditions (temperature, concentration of ions)

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8
Q

substrate concentration and reaction rate

A

more substrate = more successful collisions
eventually, enzymes become a limiting factor in reaction rate

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9
Q

enzyme concentration and reaction rate

A

more enzymes = more successful collisions
eventually, substrate becomes a limiting factor in reaction rate

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10
Q

temperature

A

higher temp = more successful collisions
to hot = enzyme denatures
optimal temperature (humans) = 37 Celsius

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11
Q

pH

A

too low/too high = enzyme denatures
optimal pH depends on environment (pepsin is in the stomach, a very acidic environment, and optimal pH is around 3. trypsin is in the small intestine, a basic environment, and its optimal pH is around 9. most are in neutral environments and their optimal pH is 7

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12
Q

How would you maximize enzyme activity considering all of the factors discussed in class? Minimize?

A

Maxime: increase enzyme and substrate concentration, optimize temperature and pH
Minimize: decrease enzyme and substrate concentration, un-optimize temperature and pH

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13
Q

Compare and contrast inhibition and activation of enzymes

A

Inhibition:
- competitive: inhibitor binds to active site to prevent substrate from binding
- noncompetitive: inhibitor binds to enzyme and changes shape of active site to prevent substrate from binding
Activation:
- activator binds to enzyme and changes shape of active site to allow substrate to bind
Both:
- noncompetitive inhibition and activation change shape of active site

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