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BIOL 3600 > Chapter 8- Enzymes > Flashcards

Chapter 8- Enzymes Flashcards

1
Q

Life can be defined as what?

A
  • dynamic
  • coordinated network of chemical reactions
  • avoiding equilibrium
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2
Q

How do we coordinate chemical reactions? And why are they usually not coordinated?

A
  • we want them coordinated which is done by enzymes
  • they can’t because they have different kinetics
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3
Q

what brings about coordination in individual reactions?

A

catalysis and the catalysts are enzymes

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4
Q

How are enzymes catalysts?

A

adjust there RATE of every reaction

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5
Q

Do the rates of catalysis differ? And why is this important?

A

Yes, completely. From seconds to billions of years. This refers to the reason of coordination and how it becomes completely coherent.

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6
Q

How do catalysts work?

A
  1. decrease activation energy (Ea)
  2. change kinetics but not the thermodynamics of a reaction
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7
Q

What do catalysts take time?

A

transition state

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8
Q

If DELTA G is positive what can be said about the the reaction? And what about if DELTA G is negative?

A

-: favorable
+: not favorable

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9
Q

If DELTA G is at 0 what can be said about the reaction?

A

at equilibrium

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10
Q

Enzymes have two part active site that accomplishes what?

A

substrate binding and catalysis

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11
Q

What are the two things that enzymes do?

A
  1. bind substrate (enzyme- substrate complex)
  2. change substrate into product and dissociate
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12
Q

What do enzymes have in relation to there substrates?

A

specificity (unique and wide open)

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13
Q

Substrate binding is usually what kind of model? What is the other model that it sometimes can be?

A
  1. induced fit
  2. lock and key
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14
Q

Enzymes are classified how?

A

proteins

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15
Q

Michaelis Menten kinetics characterizes a majority of enzymes quantifying what?

A
  1. substrate affinity (KM)
  2. catalysis (V-max)
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16
Q

For the Michaelis Menten curve what is the x axis and what is the y axis?

A

x: substate concentration
y: reaction velocity

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17
Q

For a simple saturated curve what can be explained about it?

A

it asymptotically reaches max velocity

18
Q

The rate for enzymes in MM is dependent on what?

A

concentration

19
Q

How many experiments do you have to do for enzyme kinetics?

A

multiple more than 4

20
Q

What is the slope in Enzyme kinetics?

A

velocity

21
Q

Why does the enzyme go at different rates?

A

concentration varies of 1 substrate

22
Q

Why is MM kinetics important?

A

Help understand how enzymes work

23
Q

What is KM?

A

substrate concentration yielding a velocity of Vmax/2
The KM value for an enzyme depends on the particular substrate and on environmental conditions such as pH, temperature,
and ionic strength.

24
Q

What does the KM value depend on?

A
  1. on the particular substrate
  2. on environmental conditions
  3. pH
  4. temperature
  5. ionic strength
25
Q

Big VMAX is…..

A

high rate at better which it catalyzes

26
Q

Big KM is….

A

worse substrate affinity

27
Q

Enzymes that have what have non MM kinetics?

A

cooperativity

28
Q

Sigmodial curve means

A

cooperative enzyme and Non MM kinetics

29
Q

Standard inhibition means what?

A

MM behaving

30
Q

What are some types of standard inhibition?

A

competitive, non competitive, and uncompetitive

31
Q

What can regulate enzymes?

A

Standard inhibition or MM behaving

32
Q

What is a non competitive inhibitor?

A

affects the substrates ability to catalyze but not to bind

33
Q

What is an uncompetitive inhibitor?

A

affects both the binding and catalysis

34
Q

In competitive inhibition what is to be said about KM and Vmax?

A

KM change
Vmax same

35
Q

In non competitive inhibition what is to be said about KM and Vmax?

A

Vmax change
KM same

36
Q

In uncompetitive inhibition what is to be said about KM and Vmax?

A

Vmax change
KM change

37
Q

What makes good competitive inhibitors?

A

transition state analogs

38
Q

How do enzymes work?

A

decrease activation energy make the transition state with lower energy

39
Q

Can you make a transition state? If so why not?

A

You cannot make a transition because unless an analog (or similar compound) is used

40
Q

When is standard inhibition most commonly used in a pharmacology application?

A

Penicillin

41
Q

Enzymes can use what and can be classified how?

A

cofactors
coenzymes
cosubstrates
can be classified by the type of reaction they catalyze

BIOL 3600 (12 decks)

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