module 6 Flashcards

(47 cards)

1
Q

What is an enzyme?

A

Biological catalysts, primarily proteins that speed up chemical reactions within cells.

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2
Q

What is vitalism? (The old way of looking at biochemical reactions)

A

The belief that living things are fundamentally different from non living things; that they contain some non physical element and are governed by different principles that inanimate objects.

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3
Q

Are all enzymes proteins

A

Yes

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4
Q

Are all proteins enzymes

A

No

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5
Q

A coenzyme or cofactor that is tightly associated with the enzyme is called…

A

A prosthetic group

(The difference is the degree of association)

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6
Q

3 points about catalysts

Catalysts…

A

1.Lower the amount of energy required for a reaction to proceed.

2.Speed up attainment of equilibrium, but do not change equilibrium.

3.Are unchanged by the reaction; they are recycled to participate in another reaction.

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7
Q

What are the 4 major differences between enzymes vs chemical catalysts?

A
  1. Speed: Enzymes are often much faster than chemical catalysts
  2. Condition: Many chemical catalysts that require extremes of temperature, presssure, and PH while enzymes function under physiological conditions
  3. Specificity: Enzymes have a higher degree of specificity than most chemical catalysts. This includes specificity for both what they act upon and what they produce.
  4. Regulation: Unlike chemical catalysts, many enzymes are responsive to the dynamic needs of the cell and organism.
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8
Q

What is the Circee effect in enzymes?

A

Some enzymes can go faster than catalytic perfection. Enzymes draw substrates towards them with charge.

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9
Q

Are enzymes, substrates, and products a reversible process in equilibrium

A

yes.

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10
Q

If the product has lower free energy than the substrate, its formation will be…

A

Spontaneous (It will occur without the input of energy)

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11
Q

What are the 5 points on free energy in rates and equilibrium?

A

1) A reaction is spontaneous only in change in free energy is negative.

2) A reaction cannot take place spontaneously if the change in free energy is positive

3) In a system at equilibrium, there is no net charge in the concentrations of the products and reactants, the change is zero.

4) Change in free energy in a reaction depends only on the free energy of the product minus the free energy of the reactants.

5) Change in free energy provides no information about the rate of the reaction.

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12
Q

Enzymes provide an alternate, lower-energy pathway between the substrate and the product, lowering what?

A

It lowers the free energy.

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13
Q

Do enzymes influence the difference in free energy between substrate and product?

A

No.

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14
Q

Catalytic capabilities result from both chemical and binding effects. Give an example of these effects.

A

Chemical: Acid/Base catalysis, Covalent catalysis

Binding: Substrate binding, transition state stabilization

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15
Q

Substrate binding promotes reactions by:

A
  1. Reducing entropy
  2. Alignment of reactive functional groups of the enzyme with the substrate.
  3. Desolvation of the substrate to expose reactive groups
  4. Distortion of substrates
  5. Induced fit of the enzyme in response to substrate binding.
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16
Q

What balance must active sites maintain to function effectively?

A

Active sites must be similar enough to the substrate to ensure specificity, but different enough to promote change.

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17
Q

The active site of an enzyme often contains what type of amino acids?

A

Triprotics. (Chemically reactive sidechains)

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18
Q

Which amino acid is often involved in acid/base catalysis?

A

Histidine

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19
Q

what are important variables to implement during measures of enzyme velocity?

A

-Temperature
-Concentration
-PH

20
Q

What parts of the enzyme catalyze reaction contribute to the velocity of the enzyme?

A

-The ES complex
-K2 of E+P

21
Q

Enzymes provide a lower-energy pathway between the substrate and product, _________ the activation energy of the transition state and _________ the rate of reaction.

A

-decreasing
-Increasing

22
Q

What is the formula for finding the velocity in an enzyme

A

-Change in the concentration of the product over the change in time.

23
Q

K1 and K-1 represent…

A

Rapid, non-covalent interactions between enzyme and substrate.

24
Q

K2 and K-2 represents…

A

Rate constant of formation of product from ES.

25
What does the michaelis-menten equation describe?
The Michaelis-Menten equation and plot describe the relationship between substrate concentration and initial velocity.
26
What is Km?
Its the concentration of substrate required for the enzyme to function at half maximal velocity.
27
How sensitive to change in substrate, and how active are enzymes... When [S] < Km When [S] > Km When [S] = Km
When [S] < Km: highly sensitive to changes in substrate concentration but have very little activity. When [S] > Km: high activity but are insensitive to changes in substrate concentration. When [S] = Km: significant activity and is responsive to changes in substrate concentration.
28
What does Lineweaver burke plot tell us?
It is a double reciprocal plot that determines Vmax and Km. It also determines the relationship between [S] and Vo.
29
What is the enzyme turnover number?
It equals the number of molecules of substrate converted into product per unit time under saturating conditions.
30
What are the 3 different categories of reversible enzyme inhibitors?
-Competitive -Uncompetitive -Noncompetitive
31
With competitive inhibitors what's the difference of Vmax and Km? Where does it bind?
-Vmax is the same but apparent Km is increased. -It binds to the active site
32
With uncompetitive inhibitors whats the difference of Vmax and Km? Where does it bind?
-Vmax is decreased, Km decreased -It binds to the enzyme substrate complex
33
With Noncompetitive inhibitors whats the difference of Vmax and Km? Where does it bind?
-Vmax is decreased with no change in Km -Binds to enzyme substrate complex and active site
34
What are serine proteases?
Serve as digestive enzymes that split peptide bonds in protein substrates.
35
What are zymogens?
-Digestive serine proteases are synthesized in an inactive form (zymogens) to prevent damage to cellular proteins. -Zymogens are just inactive forms of serine proteases. -Zymogens are activated at the appropriate time by selective proteolysis.
36
What are the triad of amino acids in the catalytic mechanism of serine proteases
-Histidine -Aspartate -Serine
37
What does ASP, HIS, and SER do in the protein
ASP: stabilizes the positively-charged His to facilitate serine ionization. SER: attacks the carbonyl group of the peptide bond to be cleaved (covalent catalysis). HIS: acts to accept and donate a proton at each of the two stages of the reaction mechanism (acid base catalysis).
38
How can enzyme activity be regulated in the long term?
Regulation of enzyme availability: Controlled by enzyme location, and rates of synthesis and degradation.
39
How can enzyme activity be regulated in the short term?
Regulation of enzyme activity: a) Covalent modification — phosphorylation, methylation, glycosylation, etc. b) Non-covalent (allosteric) modification — allosteric regulation.
40
Allosteric enzymes general properties:
-Usually examples of quaternary structures -Serve as information sensors to coordinate cellular metabolism -have sigmoidal curves rather than Michaelis Menten kinetics
41
In PFK1 -When ratio [PEP]/[ADP] is high, PFK1 is ________ -When ratio [PEP]/[ADP] is low PFK1 is _________
-When ratio [PEP]/[ADP] is high, PFK1 is inhibited. -When ratio [PEP]/[ADP] is low PFK1 is activated.
42
In response to hormones that are released when you are hungry (_________) or scared (_____________) both enzymes are phosphorylated
1(glucagon) 2(epinephrine)
43
the enzyme thrombin cleaves...
Arg-Gly bonds
44
The enzyme trypsin cleaves...
Lys and Arg
45
The enzyme Chymotrypsin cleaves...
Phe, Tyr, or Met
46
The enzyme elastase cleaves...
Gly and Ala
47
the enzyme papain cleaves...
all peptide bonds