Enzymes Flashcards

1
Q

Enzymes function by…

A

lowering the activation energy of reactions

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2
Q

Enzymes biochemically are:

A

Proteins
(except ribozymes)

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3
Q

Catabolic enzymes

A

Breakdown reactions, usually generates energy

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4
Q

Anabolic enzymes

A

Build up reactions, always use energy

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5
Q

How do enzymes exhibit optical specificity?

A

They act only on the L-isomer of an amino acid or D-isomer of a sugar

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6
Q

How do enzymes catalyze specific reaction or reaction types?

A

Exhibiting optical specificity

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7
Q

Are enzymes used up in the reaction?

A

No

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8
Q

Do enzymes alter the equilibrium constants?

A

No

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9
Q

Do enzymes change the free energy for the reaction?

A

No

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10
Q

Exergonic reactions

A

reactions with a –ΔG that spontaneously occur

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11
Q

Endergonic reactions

A

reactions with a +ΔG that require energy input to occur

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12
Q

Factors affecting the rates of enzyme catalyzed reactions:

A

Temperature
pH
Enzyme concentration
Substrate concentration
Inhibitors

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13
Q

When temperature increases the rate of reactions…

A

increase, but at temperatures greater than 102 degrees F, proteins denature

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14
Q

At temperatures below 98 degrees F, reaction rates…

A

slow down

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15
Q

Example of an enzyme with an optimal pH in acid 1.5-2.0

A

pepsin in the stomach

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16
Q

Example of an enzyme with a neutral optimal pH 7.3-7.4

A

carbonic anhydrase in RBC

17
Q

Example of an enzyme with an optimal pH in base 8.0-9.0

A

trypsin in small intestines

18
Q

Increasing both the enzyme and the substrate concentration will…

A

increase the rate of reaction until a maximum velocity of the reaction is reached

19
Q

What does the Michaelis-Menten curve describe?

A

the effects of substrate concentration on activity of many (not all) enzymes

20
Q

What does the Lineweaver-Burke plot determine?

A

Experimentally determines Km and Vmax

21
Q

What is the disadvantage of the Lineweaver-Burke plot?

A

small experimental error can result in large error in the graphically determined values

22
Q

What does the Eadie-Hofstee plot determine?

A

Experimentally determines Km and Vmax

23
Q

What is the advantage of the Eadie-Hofstee plot?

A

only one reciprocal

24
Q

Enzyme inhibition can be:

A

Competitive, non-competitive, or irreversible or poisons

25
Competitive inhibitors include:
most enzymes
26
Non-competitive inhibitors include:
Allosteric enzymes and Hemoglobin
27
Where do competitive inhibitors bind?
At the catalytic or active site
28
Where do non-competitive inhibitors bind?
At an allosteric site
29
Is competitive enzyme inhibition reversible?
Yes
30
Is non-competitive enzyme inhibition reversible?
Yes
31
How do competitive inhibitors affect Vmax?
no effect
32
How do non-competitive inhibitors affect Vmax?
decrease Vmax
33
What do competitive inhibitor molecules look like?
an S
34
What do non-competitive inhibitor molecules look like?
does not resemble an S
35
How do competitive inhibitors affect Km?
increase Km
36
Examples of irreversible enzymes or poisons
Heavy metals (silver, mercury), nerve gas, carbon monoxide (CO), cyanide (CN)
37