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biochem > q5 > Flashcards

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?

A
25
Q

what is the plot for lineweaver-burk?

A
26
Q

what are the assumptions of velocity

A

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
Q

what is the new assumption equation

A

E+S<——>ES——>E+P

28
Q

describe steady state

A

rate of formation of ES=rate of breakdown of ES

29
Q

what is the plotting criteria for steady state

A

ES is constant
E is constant
S is decreasing
P is increasing

30
Q

what is the plotting criteria for steady state

A

ES is constant
E is constant
S is decreasing
P is increasing

31
Q

draw a steady state graph

A
32
Q

draw a steady state graph

A
33
Q

Vmax=

A

K2[Et]

34
Q

define Kcat

A

turnover number or catalytic constant with unit (s-1)

35
Q

what does the catalytic constant do

A

determines how fast an enzyme works after ES is formed, but does not determine binding affinity or enzyme efficiency

36
Q

Kcat/Km=

A

catalytic efficiency (M-s-)

37
Q

define Kd

A

dissociation constant
inverse of binding affinity

38
Q

what is enzyme efficiency controlled by

A

K

39
Q

what do grey arrows represent? green arrows?

A

bioavailability
catalytic efficiency

40
Q

what is activation inhibited by

A

substrate analogues
transition state analogues

41
Q

define inreversible inhibition

A

non-dilutable covalent bonding/noncovalent bonding

42
Q

define reversible inhibition

A

noncovalent and dilutable

43
Q

name and describe DFP

A

diisopropfluorophosphate
irreversible protease inhibitor
blocks protease and phospholipase enzymes
forms bonds with certain serine residues

44
Q

what are the types of reversible inhibitions

A

competitive
uncompetitive
mixed

45
Q

Ki=

A

[E][I]/[EI]

46
Q

Ki’=

A

[ES][I]/[ESI]

47
Q

define competitive inhibitors

A

competes with substrates for active binding site
inhibitor may unbind

48
Q

what is an example of competitive inhibitors

A

malonate-mimics succinate ligand
competes to bind succinage dehydrogenase enzyme

49
Q

what does competitive inhibitors do to Km and Vmax

A

increases Km and does nothing to Vmax
needs higher S
Km increases to Km-app
substrate binding weakens
no physical effects

50
Q

a=

A

I+[I]/KI

51
Q

Km-app=

A

Km(1+[1]/KI)

52
Q

describe uncompetitive inhibition

A

decrease Km and Vmax, but slope stays
binds away from active site
binds ES
Km decreases to Km-app
LB stays the same

53
Q

describe mixed inhibition

A

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
Q

describe noncompetitive inhibitor

A

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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