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Biochemistry > Enzymes > Flashcards

Enzymes Flashcards

1
Q

What are enzymes

A
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2
Q

Define substrate

A

The molecule the enzyme acts upon to form product

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3
Q

Define substrate binding site

A

A particular region on the enzyme surface having a specific arrangement of chemical groups formulated to bind a specific substrate
Termed as the active or catalytic site

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4
Q

Define allosteric sites

A
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5
Q

List the types of enzymes

A

Oxidoreductase
Transferases
Hydrolases
Lyases
Isomerase
Ligases or synthetases

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6
Q

What is the function of oxidoreductase

A
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7
Q

What is the function of transferases

A

These enzymes catalyze the transfer of functional groups between acceptors and donors

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8
Q

What is the function of hydrolases

A

Catalyze the hydrolytic breakdown of one substrate to 2 products by the addition of water

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9
Q

What is the function of lyase

A

They catalyze the cleavage of bonds

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10
Q

What is the function of isomerase

A

These enzymes catalyze changes within one molecule
They alter the structure but not the atomic composition of the substrate by moving a group from one position to the other

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11
Q

What is the function of ligases or synthetases

A
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12
Q

What are the two models that explain substrate specificity for the enzyme

A

Lock and key model
Induced fit model

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13
Q

Explain the lock and key model

A
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14
Q

Explain the induced fit model

A
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15
Q

List the factors affecting the rate of enzyme-catalyzed reactions

A

Substrate concentration
pH
Temperature
Enzyme concentration
Coenzymes
Metals

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16
Q

How does substrate concentration effect enzyme catalyzed reactions

A

Substrate concentration increase = initial velocity increases to a maximum V max and no further

17
Q

What is Vmax

A
18
Q

What is Km

A
19
Q

What is the importance of Km

A
20
Q

How does pH effect the enzyme catalyzed reaction

A
21
Q

How does temperature affect enzyme catalyzed reaction

A
22
Q

How does enzyme concentration affect enzyme catalyzed reaction

A
23
Q

How does coenzyme effect enzyme catalyzed reaction

A

Many enzymes require the presence of coenzyme which is a molecule that helps to activate enzymes

24
Q

What are the types of enzyme inhibitors

A

Competitive
Non competitive
Uncompetitive

25
Q

What are the sites of attachment of each of the inhibitors

A

Competitive - active site
Non competitive - allosteric site
Uncompetitive - enzyme complex

26
Q

What is the effect of Km and Vmax of each of the inhibitors

A

Competitive - Km increased and Vmax same
Non competitive - Km same and Vmax decreased
Uncompetitive - Km decreased and Vmax decreased

27
Q

What are the two types of enzyme regulation

A

Qualitative - activity
Quantitative - amount of enzyme

28
Q

What is the duration of enzyme regulations

A

Quantitative - long term (hours to days)
Qualitative - short term (seconds to minutes)

29
Q

What are examples of quantitative regulation

A

Gene level and protein level

30
Q

Explain gene level regulation

A

Induction - more copies of enzymes
Repression - stop synthesis

31
Q

Explain enzyme level regulation

A

Enzyme degradation (breakdown)

32
Q

What are the examples of qualitative regulation

A

Allosteric regulation
Covalent modification
Proteolytic cleavage

33
Q

Explain allosteric regulation.

A
34
Q

Explain covalent modification

A
35
Q

Explain proteolytic cleavage

A

Biochemistry (27 decks)

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