Enzymes Part 2 Flashcards

(28 cards)

1
Q

What are the two types of modifications that alter the rate of enzyme reactions?

A

Covalent and noncovalent modifications

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2
Q

What term is used for non-protein components required for enzymatic activity?

A

Cofactors

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3
Q

What is the active enzyme called when it includes its non-protein components?

A

Holoenzyme

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4
Q

What is the term for the inactive protein component of an enzyme?

A

Apoenzyme

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5
Q

What are the two main categories of cofactors?

A
  • Metal ions
  • Organic molecules
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6
Q

What are coenzymes?

A

Organic cofactors that bind temporarily and detach after catalysis

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7
Q

What are prosthetic groups?

A

Organic cofactors that are permanently bound to the enzyme

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8
Q

What is an example of a metalloprotein?

A

Hemoglobin

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9
Q

What is the difference between metalloproteins and metal-activated enzymes?

A

Metalloproteins contain permanently bound metal ions; metal-activated enzymes temporarily bind metal ions

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10
Q

What does the induced fit model describe?

A

The binding of enzyme and substrate leading to a conformational change

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11
Q

What is the role of residues in the active site of enzymes?

A

Interact with substrates and can form temporary covalent bonds with reaction intermediates

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12
Q

What type of specificity does an enzyme with absolute specificity have?

A

Catalyzes the reaction of only one substance

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13
Q

What does Km (Michaelis constant) represent?

A

The substrate concentration at which the reaction rate is 50% of Vmax

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14
Q

What does a lower Km value indicate about an enzyme?

A

Higher affinity for its substrate

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15
Q

What is Kcat?

A

The turnover number, or the number of substrate molecules converted to product per second

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16
Q

What does Kcat/Km represent?

A

Catalytic efficiency

17
Q

Fill in the blank: The optimal temperature for human enzymes is _______.

18
Q

What regulates enzyme activity at the transcriptional level?

A

Histone modifications that affect DNA accessibility

19
Q

What are zymogens?

A

Inactive forms of enzymes that require proteolytic cleavage to become active

20
Q

What is the function of hexokinase?

A

Catalyzes glucose uptake in all cells

21
Q

What distinguishes glucokinase from hexokinase?

A

Glucokinase has a higher Km and acts as a glucose sensor

22
Q

What does an elevation of lactate dehydrogenase (LDH) indicate?

A

Tissue damage or disease

23
Q

What is the role of glucose oxidase in diagnostics?

A

Catalyzes glucose oxidation to produce detectable color changes

24
Q

What is the function of EDTA in blood sample analysis?

A

Prevents clotting by chelating calcium

25
What are the two distinct roles of the active site of an enzyme?
* Binding site * Catalytic site
26
How does a mutation in the binding site affect Km?
It alters the enzyme's affinity for the substrate
27
True or False: Alterations in the catalytic site affect Km.
False
28
What does the rate enhancement measure?
How much the enzyme enhances the reaction rate compared to the uncatalyzed rate