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Biochemistry 2 > Module 6 Unit 2-3 > Flashcards

Module 6 Unit 2-3 Flashcards

1
Q

What is typically the ending of an enzyme?

A

-ase

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2
Q

What is the structure of Enzymes?

A

Enzymes are proteins
- a few RNA molecules have been found to have biocatalytic function (catalysts are not used up in reaction they accelerate)
Enzymes have an active site that is complementary to the substrate

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3
Q

What is the analogy used for the substrate and active site?

A

Key and lock

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4
Q

How do enzymes function?

A

Enzymes = Biocatalysts
- Increase reaction rate (V0) by lowering the activation energy of a chemical reaction

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5
Q

What happened with a lower activation energy?

A

A much-increased probability of the reaction proceeding
Higher rate of reaction (V0)

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6
Q

What are the factors impacting enzyme velocity (rate)?

A

pH
Temperature
Concentration of certain ions, regulatory factors…
Cells have regulation strategies to adapt to
-Changing situations of supply and demand
- Get back to homeostasis

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7
Q

What is the typical pH level for pepsin?

A

1.5-2.0

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8
Q

What is the typical pH level for trypsin?

A

7.0-8.5

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9
Q

What is actetate used for?

A

Energy production (TCA cycle and oxidative phosphorylation)
As a building block for fatty acids, stored in the form if triacylglycerol (fat)

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10
Q

What is the big picture of alcohol (ethanol) processing in our body (primarily in the liver)?

A

CH3CH2OH (hydroxyl) —> CH3CHO (Acetaldehyde) —> CH3COO- (Acetate)

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11
Q

What does the graph of Enzyme Kinetics look like?

A

Hyperbola
Independent variable (x) = [s] [Alcohol] (mM)
Dependent variable (y) = Alcohol Dehydrogenase Activity (V0) (mM/min)

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12
Q

What is the mathematical model for hyperbolic enzyme kinetics?

A

V0 = (Vmax[S])/(Km+[S])
[S]: independent variable
V0: dependent variable
Vmax: constant (maximal velocity)
Km: constant (special [S])

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13
Q

What are the different schematic depiction of inhibitor action?

A

Normal binding
Competitive inhibition
Noncompetitive inhibition
Uncompetitive inhibitor

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14
Q

What types of changes on the constants Vmax and Km and the mechanism of inhibition for competitive inhibitor?

A

Vmax: unchanged
Km: increase
Mechanism of Inhibition: The inhibitor binds at the active site instead of substrate

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15
Q

What types of changes on the constants Vmax and Km and the mechanism of inhibition for mixed (noncompetitive) inhibitor?

A

Vmax: decrease
Km: increase
Mechanism of Inhibition: The inhibitor binds at a site other than the binding site, affects the conformation of the enzyme, including the shape of the active site (allosteric effect)

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16
Q

What is the allosteric effect?

A
17
Q

What types of changes on the constants Vmax and Km and the mechanism of inhibition for Uncompetive?

A

Vmax: decrease
Km: decrease
Mechanism of Inhibition: The inhibitor binds at a site other than the binding site other than the binding site, but only if substrate is bound; once the inhibitor binds, the reaction does not proceed.

18
Q

What type of enzymes are rarely regulated?

A

Reversible enzymes

19
Q

What enzymes are more commonly catalyzed reactions independently of other enzymes?

A

Enzymes in Extracellular Space

20
Q

What are examples of Enzymes in the Extracellular Spaces?

A

Enzymes in the digestive tract (break down nutrients to building blocks - which then can be absorbed)
Proteases (break down proteins in blood, lymph, interstitial spaces —> refreshing of needed proteins)

21
Q

What are the enzyme regulation overview?

A

Regulation goes to non-covalent and covalent
Covalent goes to reversible and non-reversible

22
Q

What are the key factors of the Enzyme regulation for non-covalent?

A

Allosteric
- Uncompetitive
- Mixed
Competitive
- Always reversible (equilibrium)

23
Q

What are the key factors of the Enzyme regulation for covalent?

A

Reversible:
- Phosphorylation/dephosphorylation
- methylation/demethlation

Non-Reversible:
- Removal of C-/N- terminal amino acids

24
Q

What type of enzymes are intracellular?

A

Non-covalent and reversible

25
Q

What type of enzymes are extracellular?

A

Non-reversible

Biochemistry 2 (15 decks)

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