Test 3 Flashcards

(48 cards)

1
Q

what are most enzymes

A

proteins

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2
Q

does a lower or higher activation barrier allow the system to come to equilibrium faster

A

lower

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3
Q

what are pros to enzymes

A

function at low temps
fast (order of milliseconds)
occurs in H2O
Few side products
higher yields

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4
Q

what is what slows down a reaction

A

the activation barrier

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5
Q

what causes an alternate pathway

A

enzyme

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6
Q

delta G

A

final - initial

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7
Q

what does a negative delta G mean

A

spontaneous

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8
Q

what are cofactors

A

molecules that the enzymes need help from, not an amino acid residue but involved in function of enzyme, ions

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9
Q

what is a coenzyme

A

not an ion, but some small organic molecule involved in enzyme function

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10
Q

acid

A

donates protons

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11
Q

base

A

accepts protons

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12
Q

covalent bonds in enzymes

A

temporary covalent bonds provide an alternative, lower energy reaction pathway

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13
Q

non covalent interactions in enzymes

A

form an ES complex: weak interactions between enzymes and substrate stabilize the transition state (binding energy)

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14
Q

when does the ES complex form

A

when substrate binds active site

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15
Q

Enzyme substrate complex equation

A

S+E –> ES –> E+P

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16
Q

is the enzyme substrate complex permanent

A

no it is is temporary held together by non covalent bonds

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17
Q

what does lower substrate entropy mean

A

holds it steady (substrate), more ordered so they can react

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18
Q

substrate desolvation

A

removes water from around substrate which males available all functional groups of molecule

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19
Q

what does induced fit mean

A

enzyme active sites are complementary to transition states

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20
Q

what shape does the enzyme need to be

A

shape that the transition needs to be
bends when at ideal amount where it cant bend anymore

21
Q

what does the inhibotor look like

A

inhibitor looks similar to transition state but stops it from occuring

22
Q

typical enzyme enhancement

A

10^5 to 10^17 x

23
Q

what can you reduce for a reaction to happen faster

A

reduce entripy

24
Q

what is the rate of reation a function of

A

function of substrate concentration

25
what does more S mean
more Product can be formed
26
what is km
concentration of substrate at 1/2 max rate of concentration
27
what is the best speed for an enzyme
10^9
28
what is 10^9 known as
diffusion control limit, can't go faster than that
29
EI
enzyme inhibitor complex
30
K1
dissociation complex
31
what does the I do
takes up the S spot
32
do good inhibitors have small or large KI
small
33
uncompetitive inhibition
structural changes happens to enzymes once the enzyme binds inhibitor can only bind to enzyme substrate complex
34
apparent value
values mean what they appear to be when an inhibitor is present
35
what chnages in mixed inhibition
both slope and Y intercept
36
what does HIV 1 protease facilitate
direct attack of water on the peptide bond
37
2 substrates of HIV 1 protease
H2O and protein
38
why do we avoid chiral centers in drugs
too expensive
39
how does hexokinase keep water out
without substrate present the enymes will close
40
what does chymotrypsin do
catalyzes hydrolysis on peptide bonds using serine rsidues
41
optimum pH of chymotrypsin
8
42
Kcat
measure of speed, measured at turnovers per second
43
how is chymotripsin activated
proteolytic cleavage
44
chymptrypsinogen
inactive, when syntheizes not active yet, ready to be tunred on
45
pi chymotripsin
partially active, 1 st cut is to remove ser14 and arg15
46
what does peptidoglycan need
transpeptidase
47
what inhibits transpeptidase
B lactan antibiotics
48
gram negative vs gram positive bacteria
gram positive has a thick cell wall