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q5 Flashcards

1
Q

what is kinetics

A

movement

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2
Q

define enzyme kinetics

A

the rates of enzymatic reactions
relates activation energy and equilibrium

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3
Q

what is the basic reaction rate

A

S—>P

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4
Q

define dP

A

appearance over time

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5
Q

define dS

A

disappearance over time

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6
Q

dP/dt is the same as what

A

dS/dt

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7
Q

unit=

A

concentration/time

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8
Q

what is the normal standard

A

m/s

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9
Q

rate=

A

V
or
k[S]^n

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10
Q

describe k, the rate constant

A

does not depend on concentration
can be altered by catalyst or temp
determined experimentally

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11
Q

describe n, the order of reactant

A

effect of substrate concentration on rate

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12
Q

define and describe order

A

sum of exponents
affects all reactants on rate

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13
Q

define and describe order

A

sum of exponents
affects all reactants on rate

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14
Q

what does it mean if there is order with respect to a reactant

A

affects of single reactants can be seen
there is an exponent in a specific reactant

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15
Q

how is order found

A

must have a reaction and data
set 2 rates equal
solve with respect to S
use one row to solve for K

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16
Q

what does enzyme kinetics depend on? why can’t that be used?

A

[S], but it is hard to measure so [P] is used

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17
Q

Vo=

A

dP/dT

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18
Q

describe the michaelis-mention plot

A

t vs [P] plot
each line will have a different S

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19
Q

define Vmax

A

max velocity of reaction
top of curve
hyperbolic

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20
Q

what are kinetics used for

A

steady state conditions
single enzymes
single substrates

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21
Q

what is Km

A

michaelis constant
[S] at 1/2Vmax

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22
Q

Vo=

A

Vmax[S]/Km+[S]

23
Q

describe the lineweaver-burk equation

A

reciprocal of mm plot
allows mm to be plotted linearly

24
Q

what is the equation for lineweaver-burk?

25
what is the plot for lineweaver-burk?
26
what are the assumptions of velocity
rxn at an early time means no products are made no reverse rxn from EP to ES products are released quickly Et is constant steady state is reached quickly ES is constant
27
what is the new assumption equation
E+S<——>ES——>E+P
28
describe steady state
rate of formation of ES=rate of breakdown of ES
29
what is the plotting criteria for steady state
ES is constant E is constant S is decreasing P is increasing
30
what is the plotting criteria for steady state
ES is constant E is constant S is decreasing P is increasing
31
draw a steady state graph
32
draw a steady state graph
33
Vmax=
K2[Et]
34
define Kcat
turnover number or catalytic constant with unit (s-1)
35
what does the catalytic constant do
determines how fast an enzyme works after ES is formed, but does not determine binding affinity or enzyme efficiency
36
Kcat/Km=
catalytic efficiency (M-s-)
37
define Kd
dissociation constant inverse of binding affinity
38
what is enzyme efficiency controlled by
K
39
what do grey arrows represent? green arrows?
bioavailability catalytic efficiency
40
what is activation inhibited by
substrate analogues transition state analogues
41
define inreversible inhibition
non-dilutable covalent bonding/noncovalent bonding
42
define reversible inhibition
noncovalent and dilutable
43
name and describe DFP
diisopropfluorophosphate irreversible protease inhibitor blocks protease and phospholipase enzymes forms bonds with certain serine residues
44
what are the types of reversible inhibitions
competitive uncompetitive mixed
45
Ki=
[E][I]/[EI]
46
Ki’=
[ES][I]/[ESI]
47
define competitive inhibitors
competes with substrates for active binding site inhibitor may unbind
48
what is an example of competitive inhibitors
malonate-mimics succinate ligand competes to bind succinage dehydrogenase enzyme
49
what does competitive inhibitors do to Km and Vmax
increases Km and does nothing to Vmax needs higher S Km increases to Km-app substrate binding weakens no physical effects
50
a=
I+[I]/KI
51
Km-app=
Km(1+[1]/KI)
52
describe uncompetitive inhibition
decrease Km and Vmax, but slope stays binds away from active site binds ES Km decreases to Km-app LB stays the same
53
describe mixed inhibition
decreased Vmax, either for Km binds away from activation site binds enzyme or ES affects S binds Ki- binding affinity for I for E Ki’- binding affinity for I for ES
54
describe noncompetitive inhibitor
decreased Vmax, no change in Km mixed inhibition does not bind active site causes conformational change and affects activation site Ki=Ki’

biochem (11 decks)

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