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CH 336 > Ch.22 > Flashcards

Ch.22 Flashcards

1
Q

how do grignards work

A

pg. 3
they add on to a carbonyl

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2
Q

describe how enzymes are catalysts

A

pg. 4
enzymes are proteins that catalyze chemical reactions. these are generally globular proteins meaning they fold up to create a perfect chemical environment for a specific region

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3
Q

draw reaction coordinate diagram that displays when a catalyst is or isn’t present

A

pg. 4

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4
Q

positive delta G

A

endergonic

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5
Q

draw the mechanism of a proton based acid catalyst

A

pg. 5

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6
Q

where is the most nucleophilic site on the compound on pg. 5 and why is that the most nucleophilic location

A

most nucleophilic location because its stabilized via resonance compared to the other oxygen (which if you tried to stabilize that other oxygen via resonance youd get a texas oxygen)

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7
Q

specific vs. general catalysis

A

pg. 6
specific catalysis: reactant or intermediated fully protonated after rate determining step

general catalysis: proton transfer takes place during the rate determining step (partial proton transfer: simultaneous protonation and bond breaking / forming to form the transition state)

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8
Q

draw the difference in mechanism between specific and general catalysis on pg. 6

A
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9
Q

draw the difference in reaction coordinate diagrams between specific and general catalysis

A

pg.6

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10
Q

how metals affect acidity

A

pg. 8

metals are positive cations and when they bind to a compound, the compound becomes more acidic (more electrophilic)

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11
Q

draw the general catalysis example on pg. 9

A
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12
Q

draw the difference between specific and general catalysis under basic conditions

A

pg. 10

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13
Q

what is the difference between specific and general catalysis under basic conditions

A

pg. 10

general catalysis is not as highly reactive compared to the specific mechanism

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14
Q

answer the question on pg. 12

A
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15
Q

what is something you have to be cognizant of in terms of catalysis in the active site

A

pg. 13

you also have to be careful of lewis acids in the enzyme active site (ex. other metals that interact with Zn2+). These are other points of acidity.

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16
Q

how do amino acids engage in catalysis

A

pg. 13

AAs need to have the right charges; general pH is 7.4 when considering the conjugates and for thinking about the catalytic roles

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17
Q

draw how a mechanism can be changed to a more favorable pathway

A

pg.14

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18
Q

draw the general redox mechanism and catalysis

A

pg.16

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19
Q

NAD+

A

pg.16

NAD+ is an oxidizing agent

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20
Q

the catalytic triad

A

pg.17

a set of three coordinated amino acids that can be found in the active site of some enzymes

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21
Q

proton shuttle

A

pg. 17

a molecule that protonates something at one point and deprotonates at another point in the mechanism

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22
Q

answer practice question on pg. 19

A
23
Q

answer practice question on pg. 20

A
24
Q

answer practice question on pg. 21

A
25
Q

answer practice question on pg. 22

A
26
Q

draw the usage of NAD+

A

pg. 23

27
Q

where is catalytic activity manifested

A

pg. 24

the active site of the enzyme

28
Q

what produces catalytic activity

A

pg. 24

the folding pattern of the enzyme

29
Q

what type of binding occurs in the active site

A

pg.25

H-bonding
hydrophobic pockets
salt bridges
pi-interactions

30
Q

alcohol dehydrogenous

A

pg. 26

responsible for metabolizing the bulk of ethanol consumed as part of the diet

31
Q

draw the general mechanism for alcohol dehydrogenase

A

pg. 27

32
Q

absolute specificity

A

pg. 28

enzymes can be very specific for a single substrate – absolute specificity would mean that a substrate has near perfect interactions for its specific structure

33
Q

relative specificity

A

pg. 28

enzymes that can catalyze a range of substrates

34
Q

how can enzymes have relative specificity

A

pg. 28

most enzymes can catalyze a range of substrates having the same functional groups. they can also select based on stereochemistry (stereospecificity)

35
Q

Km

A

is the substrate concentration at which half of an enzyme is saturated and the reaction rate is 50% of Vmax. Km is a measure of how much an enzyme is attracted to its substrate. A lower Km value means the enzyme is more efficient at carrying out its function at a lower substrate concentration.

(lower Km = more affinity of a compound for the active site)

36
Q

relative maximum velocity (Vmax)

A

the maximum rate of reaction (the fastest ability for an enzyme to do the rxn)

37
Q

draw the utility of lipase in the lab

A

pg. 29

lipase is a well known stereospecific enzyme – it is used in the lab to isolate one enantiomer over the other. draw its uses

38
Q

absolute vs. relative specificity in the formation of a product

A

pg. 31

absolute –> one pdt
relative –> multiple pdts

39
Q

explain / draw the lock and key model

A

pg. 32

the substrate entering the active site of the enzyme creates an enzyme/substrate complex. the enzyme changes shape slightly as the substrate binds which forms the enzyme/product complex. the products leave the active site of the enzyme

40
Q

what is the ideal enzyme catalysis pH

A

7.4

41
Q

what is the ideal enzyme catalysis temperature

A

37 degrees celcius

42
Q

answer the question on slide 34. when would the answer be none of the above?

A

relative specificity –> the twodselected compounss are close enough to ethanal.

the answer would be E if you were attempting with absolute specificit –> the compound would HAVE to be an ethanal

43
Q

what controls the rate of a reaction

A

pg. 35

activation energy (lower activation energy enhances rate)

44
Q

how do enzymes effect activation energy and reaction rate

A

pg. 35

enzymes lower the activation which speeds up the reaction

45
Q

how can you increase the rate of the forward reaction

A

pg. 35

  1. add heat (in bio you can’t do that)
  2. raise concentration –> you can sort of do this in bio
  3. add a catalyst –> you can do this in bio
46
Q

michaelis-menten kinetics

A

pg. 36 / 37

there is a limit to how fast the forward reaction goes

as the substrate increases, its interaction with the enzyme increases; but, you reach a point where all the active sites are filled, which doesn’t give any higher interactions (maximal velocity)

47
Q

what does 1/2 vmax tell you

A

pg. 38

how well the enzyme binds to the active site

48
Q

what changes vmax or km

A

pg. 39

  • the substrate
  • the pH
  • the temperature
49
Q

if comparing two kms - one is 0.006 and the other is 57 - what does this tell us

A

pg. 39

the compound with a km of 0.006 binds to the active site quicker than the compound with the km of 57

50
Q

how might an enzyme be inhibited (overall)

A

pg. 42

enzyme can be slowed and/or stopped not only by denaturation but by small molecules and other chemicals. any chemical that interferes with an enzymes catalytic ability is an inhibitor

51
Q

what are the three types of inhibitors

A

pg. 42

  1. competitive inhibition
  2. non-competitive inhibition
  3. covalent inhibition
52
Q

describe competitive inhibition

A

pg. 44

involves a direct assault on the active site. if the inhibitor is in the active site, the substrate cannot be.

53
Q

what are the kinetic effects of competitive inhibition

A

pg. 45

competitive inhibitors raise km but do not change the vmax

Increased km: More substrate is required to achieve half of vmax due to the competitive inhibition.

Unchanged vmax: The maximum velocity remains the same because, at high substrate concentrations, the inhibitor’s effect is negated.
This is why competitive inhibition raises km but does not change vmax
.

54
Q

describe covatent inhibition

A

pg. 47

irreversibly bind to the active site

CH 336 (6 decks)

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