Lecture 4 - Enzymology Flashcards

1
Q

What is an enzyme?

A

a generic term for a biological catalyst

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2
Q

What type of molecules are enzymes normally?

A

proteins

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3
Q

How do the primary amino acid affect the tertiary structure?

A

It gives it function.

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4
Q

What is the common suffixes for enzymes?

A

-ase

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5
Q

What are oxidoreductases?

A

catalyze transfer of electrons from reductant (electron donor) to the oxidant (electron acceptor)

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6
Q

What are transferases?

A

an enzyme that transfers functional groups between donor and acceptor molecules

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7
Q

What do hydrolases do?

A

add water across a bond

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8
Q

What do lyases do?

A

add water, ammonia, or carbon dioxide to produce double bonds

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9
Q

What do isomerases do?

A

carry out many kinds of isomerization

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10
Q

What do ligase do?

A

catalyze reactions in which two chemical groups are joined using ATP

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11
Q

How do apoenzymes relate to holoenzyme?

A

cofactors join the apoenzyme (inactive protein portion) in order to create the holoenzyme (active enzyme)

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12
Q

Which things do enzymes prefer?

A

certain temperatures and pH

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13
Q

What is substrate specificity?

A

unique fit of substrate with enzyme which controls selectivity

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14
Q

What is different about the induced-fit model?

A

enzyme changes conformation to fit the substrate

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15
Q

How are enzymes used in regulation?

A

phosphorylation acts as an on/off switch based on availability

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16
Q

Do enzymes appear as a reaction product?

17
Q

Do enzymes affect the equilibrium?

18
Q

Do enzymes need large amounts of quantities in order to work?

19
Q

How do enzymes work?

A

They lower the activation energy of the reaction.

20
Q

If the rate constant changes, does the equilibrium constant change?

21
Q

What does Vmax stand for?

A

maximum velocity of the enzyme reaction

22
Q

What is Km?

A

The substrate concentration at 1/2 of the maximum velocity of the enzymatic reaction

23
Q

When k2 is greather than k3, what is Km an estimate of?

A

the dissociation constant (Kd)

24
Q

What does a small Km mean?

A

tight binding, meaning there is a greater chance of an enzyme-substrate complex

25
What does a high Km mean?
weak binding because the enzyme and substrate are found more singularly instead of together
26
Is Vmax achieved in reality?
Never
27
What is Kcat?
the turnover number, or the number of substrate molecules converted to product per enzyme molecule per unit of time, when E is saturated with substrate
28
What does Et stand for?
the total number of enzymes available
29
What type of inhibitors are there?
competitive inhibitors and non competitive inhibitors
30
How does competitive inhibitors affect Vmax and Km?
Vmax is a constant and stays the same, but Km increases
31
How can we affect competitive inhibition to reach the product?
increasing the substrate concentration overcomes the competitive inhibitors
32
How does non competitive inhibition affect Vmax and Km?
Vmax decreases and Km stays constant
33
How can non competitive inhibition negatively affect product output?
active enzymes will be lost due to binding of non-competitive inhibitors
34
What are activators?
increase velocity of enzymatic reaction
35
How does sigmoidal curve in enzymes happen?
as activators and inhibitors bind
36
What is allosteric regulation?
regulation that is modulated by allosteric effectors at “another site”
37
Where are allosteric effectors usually produced?
elsewhere in the pathway
38
What are feed-forward activators?
positive feedback loop
39
What are feedback inhibitors?
negative feedback loop