1.6 Enzyme Kinetics Flashcards

0
Q

How are enzymes classified and organized?

A

According to the type of reaction they catalyze

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1
Q

T or F, Enzymes are biocatalysts that increase the rate of chemical reactions and are consumed during the reaction

A

False. They are NOT consumed during the reaction

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2
Q

What is an enzyme and its cofactor called?

A

Holoenzyme

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3
Q

What is an Apoenzyme

A

The protein portion of the holoenzyme

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4
Q

Prosthetic groups

A

Tightly bound coenzyme

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5
Q

Three types of enzymatic reactions?

A
  1. Random
  2. Sequential Displacement
  3. Double Displacement (ping-pong)
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6
Q

What is Double displacement enzymatic reactions

A

When one or more products are released before all substrates have been bound by enzyme

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7
Q

Rate of reaction in enzyme kinetics is directly proportional to what?

A

[E] and [S]

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8
Q

Allosteric enzymes give what type of curve on the substrate vs V0 graph?

A

Sigmoidal curve

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9
Q

What is the Km

A

It reflects the affinity of the enzyme for the substrate

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10
Q

Km = what?

A

the [substrate] at 1/2 Vmax

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11
Q

T or F, Km varies with Enzyme concentration?

A

False, It does not vary with enzyme concentration. It is dependent upon the [S]

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12
Q

Small Km = what type of affinity that E has for S

A

A high affinity

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13
Q

_______ Km = low affinity of E for S

A

Large Km

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14
Q

What does the slope represent on the Lineweaver-Burke plot

A

slope = Km/Vmax

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15
Q

What is the x axis on the Lineweaver-Burke plot

16
Q

Y-axis of the Lineweaver-Burke plot

17
Q

What is the turnover number

A

number of molecules of [S] converted to product per enzyme per second

18
Q

High Kcat and low Km are markers of what?

A

Enzyme efficiency

19
Q

Explain reversible enzyme inhibition

A

Enzyme inhibition in which there are noncovalent bonds used and the enzyme can continue functioning

20
Q

What is irreversible enzyme inhibition

A

Enzyme does not regain activity

21
Q

What are the two most common reversible enzyme inhibitions

A
  1. Competitive

2. Non-competitive

22
Q

Which type of inhibitor reduces rate of catalysis by reducing the proportion of enzyme molecules bound to a substrate?

A

Competitive inhibitor

23
Q

What type of inhibitor functions by binding to the enzyme at a different location than the active site?

A

Non-competitive inhibitor

24
What type of enzyme inhibitor increases the Km
Competitive Inhibitor
25
What happens to a competitive inhibitor if extra substrate is added
The inhibition can be dampened
26
Which inhibitor decreases the Vmax and keeps Km the same
Noncompetitive Inhibitor
27
Why does a noncompetitive inhibitor not affect the Km
The inhibitor does not interfere with the substrate and enzyme binding.
28
What is an Isozyme?
Alternative form of same enzyme activity that exist in different proportions in different tissues
29
What is a Proenzyme or a Zymogen
Inactive storage forms of enzymes