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VET 401 > Lecture 4 - Enzymology > Flashcards

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?

A

No

17
Q

Do enzymes affect the equilibrium?

A

No

18
Q

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

A

No

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?

A

No

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
Q

What does a high Km mean?

A

weak binding because the enzyme and substrate are found more singularly instead of together

26
Q

Is Vmax achieved in reality?

A

Never

27
Q

What is Kcat?

A

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
Q

What does Et stand for?

A

the total number of enzymes available

29
Q

What type of inhibitors are there?

A

competitive inhibitors and non competitive inhibitors

30
Q

How does competitive inhibitors affect Vmax and Km?

A

Vmax is a constant and stays the same, but Km increases

31
Q

How can we affect competitive inhibition to reach the product?

A

increasing the substrate concentration overcomes the competitive inhibitors

32
Q

How does non competitive inhibition affect Vmax and Km?

A

Vmax decreases and Km stays constant

33
Q

How can non competitive inhibition negatively affect product output?

A

active enzymes will be lost due to binding of non-competitive inhibitors

34
Q

What are activators?

A

increase velocity of enzymatic reaction

35
Q

How does sigmoidal curve in enzymes happen?

A

as activators and inhibitors bind

36
Q

What is allosteric regulation?

A

regulation that is modulated by allosteric effectors at “another site”

37
Q

Where are allosteric effectors usually produced?

A

elsewhere in the pathway

38
Q

What are feed-forward activators?

A

positive feedback loop

39
Q

What are feedback inhibitors?

A

negative feedback loop

VET 401 (1 decks)

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