Ch 7 Enzyme Activity Flashcards

1
Q

What does the Michaelis–Menten equation describe?

A

Enzyme kinetics with hyperbolic characteristics

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2
Q

What does Vmax represent in the Michaelis–Menten equation?

A

The maximum rate of reaction

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3
Q

What is the relationship expressed by the Michaelis–Menten equation?

A

V = Vmax[S] / (KM + [S])

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4
Q

What type of plot is a Lineweaver-Burk plot?

A

A plot of 1/V versus 1/[S]

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5
Q

In a Lineweaver-Burk plot, what does the x-intercept represent?

A

-1/KM

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6
Q

What does the turnover number (kcat) measure?

A

Moles of substrate converted to product per unit time by a mole of enzyme

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7
Q

What is the turnover number for Carbonic anhydrase?

A

1,000,000 s–1

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8
Q

Who won the Nobel Prize in Chemistry in 2018 for directed evolution of enzymes?

A

Francis Arnold

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9
Q

What is a competitive inhibitor?

A

A substance that competes with the substrate for the active site

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10
Q

True or False: A competitive inhibitor changes Vmax.

A

False

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11
Q

What happens to KM in the presence of a competitive inhibitor?

A

KM increases

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12
Q

What is the effect of noncompetitive inhibition on Vmax?

A

Vmax decreases

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13
Q

In noncompetitive inhibition, what happens to KM?

A

KM remains unchanged

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14
Q

What is feedback inhibition?

A

Formation of a product inhibits its continued production

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15
Q

What is an allosteric enzyme?

A

A multi-subunit protein whose activity is affected by other substances binding to it

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16
Q

What are allosteric effectors?

A

Substances that modify the behavior of an allosteric enzyme

17
Q

What is the role of kinases in enzyme activity?

A

They attach phosphates to proteins

18
Q

What is a zymogen?

A

An inactive precursor of an enzyme

19
Q

What is the active form of chymotrypsinogen called?

A

α-chymotrypsin

20
Q

What type of modification can activate an enzyme?

A

Phosphorylation

21
Q

What does the concerted model of allosteric enzymes imply?

A

The enzyme can only exist in the T or R states

22
Q

Fill in the blank: A protein that controls enzyme activity through phosphorylation of amino acid side chains is called a _______.

23
Q

Which of the following is an example of a co-enzyme: ATP, a zymogen, biotin, or ATCase?

24
Q

Which type of inhibition allows increased substrate concentration to overcome the inhibitor?

A

Competitive inhibition

25
Q

What does a suicide inhibitor do?

A

Acts irreversibly on the enzyme

26
Q

What is a co-enzyme example?

A

Biotin

Biotin is a vitamin that acts as a co-enzyme in various biochemical reactions.

27
Q

What is the inactive form of chymotrypsin called?

A

Chymotrypsinogen

Chymotrypsinogen is an inactive precursor that is activated to chymotrypsin.

28
Q

Which enzyme cleaves chymotrypsinogen?

A

Trypsin

Trypsin activates chymotrypsinogen by cleaving it.

29
Q

Where is chymotrypsinogen stored?

A

Pancreas

Chymotrypsinogen is stored in the pancreas before being activated.

30
Q

True or False: Chymotrypsinogen is a multimeric enzyme.

A

False

Chymotrypsinogen is a single polypeptide chain and not multimeric.

31
Q

What is the hydrogen ion concentration in an aqueous solution when the pH is 7.5?

A

~3.3 X 10^-8 M

The hydrogen ion concentration can be calculated using the formula [H+] = 10^(-pH).

32
Q

What is the pH in water when the hydrogen ion concentration is ~3.3 X 10^-7 M?

A

~6.5

The pH can be determined using the formula pH = -log[H+].