Chapter 13 & 14- Enzyme Specificity and Kinetics Flashcards

1
Q

Enzymes are _____ that increase _______ but are not _______

A

catalysts, reaction rate, consumed

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2
Q

Most enzymes are _____, except ____- which are catalytic RNA

A

proteins, ribozymes

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3
Q

What is the active site?

A

the pocket on the enzyme where the reaction takes place

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4
Q

Substrate definition

A

molecule bound in the active site and acted upon

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5
Q

How are enzymes different from ordinary chemical catalysts?

A
  • Higher Reaction Rates
  • Operate under mild reaction conditions
  • Greater reaction specificity
  • Capacity for Control
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6
Q

Enzyme-catalyzed reaction rates are _______ than with chemical catalysts

A

several orders of magnitude higher

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7
Q

Enzymes are named by adding the suffix ____

A

-ase

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8
Q

Enzymes are named for their _____

A

broad function

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9
Q

A substrate binds _____ to an enzyme at a specific site

A

non-covalently

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10
Q

Driving force of substrate binding

A

water release

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11
Q

Interactions and forces involved with substrate binding?

A
  • Van der Waals
  • Electrostatic interactions
  • H-bonding
  • Hydrophobic interactions
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12
Q

What is geometric complementarity

A

the substrate is complementary in shape to the active site

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13
Q

what is electronic complementarity

A

binding site attracts the substrate

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14
Q

Substrate specificity: of serine proteases

A

catalyze hydrolysis of amide bonds via a serine

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15
Q

Substrate specificity of Chymotrypsin

A

specific for a bulky hydrophobic residue

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16
Q

substrate specificity of trypsin

A

specific for a positively charged residue

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17
Q

substrate specificity of elastase

A

specific for a small neutral residue

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18
Q

Enzymes vary in their degree of _____

A

geometric specificity

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19
Q

characteristics of Geometric specificity of enzymes

A
  • some are very specific
  • some have more relaxed specificity
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20
Q

Enzymes bind ______ substrates

21
Q

Enzymes catalyze reactions in a _____

A

stereospecific manner

22
Q

Enzymes and ligands exhibit some degree of ______ fit

23
Q

What does induced fit mean

A

Enzymes change shape around the substrate when they bind and the substrate adapts to the protein

24
Q

Enzymes must be complementary to the ________ state

A

reaction transition

25
Thermodynamics predict _____, it does not say anything about the _____
whether a reaction is spontaneous rate of the reaction
26
Enzymes kinetics are important for:
- Elucidation of catalytic mechanism - Role of a specific enzyme in a metabolic process - Determine binding affinities of substrates or inhibitors to enzymes - determine how much enzyme is present
27
How can the rate of a unimolecular reaction be determined?
measuring [A] or [P] as a function of time
28
For the reaction to occur, the existence of a high energy (unstable) complex is needed which is an _____
activated complex
29
The gibbs free energy of activation is also called the _____
activation barrier
30
Ways to increase the reaction rate
1. raising the temp 2. lowering gibbs free energy
31
Catalysts act by _____
lowering the activation barrier
32
The kinetic barrier is lowered by the _______ for both the forward and the reverse reactions
same amount
33
The equillibrium constant for the reaction _____ when catalyzed
remains the same
34
The slowest step in the reaction has the _____
highest activation barrier
35
If K1< K2 then ____
1st step is the slowest
36
If K1>K2 then ____
2nd step is the slowest
37
The slow step acts as a _____ which is the ______ of the reaction
bottleneck, rate-determining step
38
Assumption of steady state
substrate is in great excess over enzyme
39
[ES] remains ~ _______ until the substrate is nearly exhausted
constant
40
The rate of synthesis of ES must _____ its rate of consumption
equal
41
[ES] maintains a steady stade which means the change in [ES]=? not that [ES]=?
0
42
Vmax occurs when [S] is very ___
high
43
Steps to determine V0
1. measure appearance of the product 2. plot signal vs. time 3. repeat for different [S] ([E] is the same for each experiment) 4. determine d[S]/t or d[P]/t.
44
Km is the substrate concentration at which the reaction velocity is ______
half maximal
45
Km is a measure of the _____ of the enzyme for the substrate
affinity
46
If one step is the rate limiting step, then Kcat is ____ to the rate constant for the limiting step
equivalent
47
A higher value of the specificity constant means ____
a higher catalytic effeceincy
48
two enzymes may have the same Kcat but the rate of the uncatalyzed reactions may be ____
different
49
Virtual catalytic perfection def
Enzyme with Kcat/Km in thsi range must catalyze the reaction every time it encounters the substrate