Enzymes 101 Flashcards

(49 cards)

1
Q

What is the primary role of enzymes in biological systems?

A

To act as biological catalysts that speed up chemical reactions without being consumed

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2
Q

Under what conditions do enzymes typically operate?

A

37°C, pH ~7.0, 1 atm pressure, and in aqueous solution

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3
Q

Do enzymes change the ΔG of a reaction?

A

No, enzymes do not affect the free energy change (ΔG) of a reaction

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4
Q

What is the effect of enzymes on activation energy (ΔG‡)?

A

Enzymes lower the activation energy, increasing reaction rate

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5
Q

What are the six main classes of enzymes in EC classification?

A

Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases, Ligases

(𝑶𝒙𝘦𝘯 𝑻𝒓𝘪𝘤𝘬 𝑯𝒚𝘳𝘢𝘹𝘦𝘴 𝑳𝒚𝘪𝘯𝘨 𝑰𝘯 𝑳𝒊𝒈𝘩𝘵𝘰𝘶𝘴𝘦𝘴)

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6
Q

What does EC 1.1.1.1 represent?

A

Alcohol:NAD⁺ oxidoreductase (alcohol dehydrogenase)

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7
Q

What is the function of an enzyme’s active center?

A

It binds substrates and contains the chemical groups that catalyze reactions

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8
Q

What is the role of regulatory centers in enzymes?

A

They bind modulators that regulate enzymatic activity

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9
Q

In the context of enzymes, what are cofactors?

A

Non-protein molecules that assist enzyme activity, either inorganic ions or organic molecules (coenzymes)

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10
Q

What is a coenzyme?

A

An organic cofactor that can be loosely or tightly bound to the enzyme

(It is NOT an enzyme itself)

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11
Q

Give examples of coenzymes.

A

NAD⁺, FAD, CoA

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12
Q

In the context of enzymes, what is a prosthetic group?

A

A coenzyme that is tightly or covalently bound to the enzyme

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13
Q

What is an isoenzyme?

A

Different molecular forms of an enzyme that catalyze the same reaction but differ in properties

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14
Q

Where are enzymes localized in cells?

A

In specific compartments like mitochondria, cytosol, or endoplasmic reticulum

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15
Q

What does ΔG < 0 indicate about a reaction?

A

That the reaction is spontaneous (exergonic)

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16
Q

What does ΔG > 0 indicate?

A

That the reaction is non-spontaneous (endergonic)

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17
Q

What is ΔG‡ and why is it important?

A

Activation energy; it determines the rate of a reaction

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18
Q

Which step in a reaction do enzymes affect?

A

They lower the activation energy (ΔG‡) to speed up the reaction

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19
Q

What is the enzyme-substrate complex?

A

A transient intermediate formed when the enzyme binds the substrate

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20
Q

What is the lock-and-key model?

A

A model where the enzyme and substrate fit exactly without conformational change

21
Q

What is the induced fit model?

A

A model where the enzyme adjusts its shape to better fit the substrate

22
Q

Why do enzymes bind the transition state more tightly than the substrate?

A

To stabilize the transition state and lower activation energy

23
Q

What is acid-base catalysis?

A

Catalysis involving proton transfer from or to the enzyme or cofactor

24
Q

What is the difference between specific and general acid-base catalysis?

A

Specific uses H⁺/OH⁻ from water; general uses ionizable side chains

25
What is covalent catalysis?
Catalysis where a transient covalent bond is formed between the enzyme and the substrate
26
What is metal ion catalysis?
Use of metal ions to stabilize charges, orient substrates, or mediate redox reactions
27
What percentage of enzymes use metal ion catalysis?
Approximately 30%
28
What is the role of water exclusion in active sites?
To prevent interference with catalysis and allow precise orientation of reactants
29
Do enzymes alter the thermodynamical properties of a reaction?
No, but they provide a pathway of lower activation energy for the reaction
30
How do enzymes affect reaction equilibrium?
They do not affect equilibrium, only the speed at which it is reached
31
What is meant by enzyme specificity?
Enzymes act only on particular substrates or reactions
32
Why are enzymes necessary under biological conditions?
Because biological conditions are mild and insufficient to drive most chemical reactions without catalysis
33
What is the transition state?
The highest-energy intermediate between substrate and product in a reaction
34
What role does substrate orientation play in catalysis?
It aligns reactive groups to favor the transition state
35
How does desolvation aid catalysis?
It removes water molecules that would otherwise shield charged or polar groups
36
What is meant by binding energy?
Energy derived from enzyme-substrate interaction used to lower activation energy
37
What is the function of enzyme classification numbers (EC numbers)?
To standardize enzyme naming based on the reaction they catalyze
38
Can a single enzyme have multiple cofactors?
Yes, complex enzymes may require several cofactors for full activity
39
What does reaction rate depend on in enzymatic reactions?
On activation energy, not on ΔG
40
What is an example of an enzyme using acid-base catalysis?
Ribonuclease A
41
What is the significance of Haldane’s 1930 book 'Enzymes'?
It laid foundational concepts in enzymology and structure-function relationships
42
How do enzymes improve transition state formation?
By stabilizing high-energy intermediates and lowering ΔG‡
43
Why is enzyme-substrate complementarity critical?
It maximizes binding energy and promotes catalytic efficiency
44
Why can enzymes use multiple catalytic strategies?
To enhance specificity and reaction rate through combined mechanisms
45
What is the function of diagnostic enzymes?
They serve as biomarkers for disease or tissue damage
46
What enzyme class forms covalent bonds using energy?
Ligases
47
What enzyme class catalyzes intramolecular rearrangements?
Isomerases
48
Which enzyme class catalyzes bond cleavage using water?
Hydrolases
49
What are lyases?
Enzymes that catalyze the breaking of bonds without hydrolysis or oxidation