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NYCC Biochem I > Enzyme Kinematics > Flashcards

Enzyme Kinematics Flashcards

1
Q

How do enzymes function?

A

Lower activation energy

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2
Q

What category of macromolecules are enzymes?

A

Proteins (except ribozymes)

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3
Q

What is the optical specificity of enzymes?

A

Only act on D-isomer of sugars, or L-isomer of amino acids

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4
Q

What happens to enzymes in a reaction?

A

E + S -> ES -> E + P
Enzymes are not used up

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5
Q

What do enzymes do to the equilibrium constants?

A

Enzymes do not alter equilibrium constants

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6
Q

What do enzymes do to the free energy (^G)?

A

Enzymes do not change the free energy for the reaction

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7
Q

Exergonic reactions are reactions with a ____ and ____ or ____

A

-/ve ^G
Spontaneously occur or may generate energy

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8
Q

Endergonic reactions are reactions with a ____ and ____

A

+^G
Require energy input to occur

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9
Q

What are 2 factors that affect enzymes?

A

Temperature
pH

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10
Q

What happens when temperature increases?

A
  • Rate of reaction increases
  • Proteins denature at >102°F
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11
Q

What happens when temperature decreases?

A

Reaction rate slows down at <98°F

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12
Q

What enzymes work at acidic pH (1.5-2.0)?

A

Pepsin in stomach

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13
Q

What enzymes work at neutral pH (7.3-7.4)?

A

Carbonic anhydrase in RBC

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14
Q

What enzymes work at basic pH (8.0-9.0)?

A

Trypsin in small intestines

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15
Q

Name 2 experimental plots used to determine Km and Vmax? Which is better?

A

Eadie-Hofstee > Lineweaver-Burke

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16
Q

What are the 3 types of enzyme inhibition?

A

Competitive
Non-competitive
Irreversible/poisons

17
Q

Competitive inhibition

a. Reversible/irreversible
b. Binding site
c. Molecule looks like ____
d. Effect on Vmax
e. Effect on Km

A

a. Reversible
b. Competitor binds at active site
c. Molecule looks like S
d. No effect on Vmax
e. Increases Km

18
Q

Non-Competitive inhibition

a. Reversible/irreversible
b. Binding site
c. Molecule appearance
d. Effect on Vmax
e. Kinetics explained by ____

A

a. Reversible
b. Binds at Allosteric site
c. Molecule does not look like S
d. Decreases Vmax
e. Kinetics explained by Hill equation/plot

19
Q

Examples of Irreversible/poisonous

A

Heavy metals (silver, mercury)
Nerve gas
Carbon monoxide (CO)
Cyanide (CN)

20
Q

What enzymes have competitive inhibition?

A

Most enzymes

21
Q

What enzymes have non-competitive inhibition?

A

Allosteric enzymes & Hb

22
Q

What is the Michaelis-Menten curve?

A

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

23
Q

What is Vmax?

A

Maximum velocity of reaction

24
Q

What is Km?

A
  • Concentration of substrate at which reaction occurs at rate of 1/2 Vmax
  • estimated physiological concentration of substrate
25
Q

Who first experimentally determined Km and Vmax?

A

Lineweaver-Burke

NYCC Biochem I (46 decks)

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