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Enzyme Inhibition and Allosteric Regulation: Mechanisms and Kinetics, Study notes of Biochemistry

A detailed overview of enzyme inhibition, covering competitive, uncompetitive, and non-competitive inhibition mechanisms. It explains how inhibitors affect enzyme activity, substrate binding, and catalytic function. The document also discusses allosteric regulation, including how molecules binding to regulatory sites can alter enzyme activity. Key concepts such as vmax, km, and the effects of inhibitors on lineweaver-burk plots are explained. Useful for students studying biochemistry and enzymology, offering insights into enzyme kinetics and regulatory mechanisms. It also covers end-product inhibition and the conformational changes induced by inhibitors and activators, enhancing understanding of enzyme regulation.

Typology: Study notes

2022/2023

Available from 05/23/2025

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bg1
Competitive
Inhibition
Inhibitors
are
compounds
that
decrease
an
enzymes
activity
competes
with
substrate
for
binding
Irreversible
inhibitors
Cin
activators
)
react
with
enzyme
Binds
active
site
One
inhibitor
molecule
can
permanently
shut
off
one
enzyme
molecule
Does
not
affect
catalysis
Often
powerful
toxins
;
can
also
be
used
as
drugs
=
(
÷?)É]+Émax
Reversible
Inhibitors
bind
-10
and
can
dissociate
from
enzyme
a.
=zCI
]
No
change
In
Vmax
;
apparent
Increase
in
14M
Line
Weaver
-
Burk
:
lines
intersect
at
they
-
axis
often
structural
analogs
of
substrates
or
products
-
1-
-
c-
+
s
-
Es
-
up
No
inhibitor
Often
used
as
drugs
to
slow
down
a
specific
enzyme
+
cÉmm
)
I
can
bind
-10
:
%
.
•-¥
•q:¥¥
free
enzyme
/
prevents
binding
of
the
substrate
El
Enzyme
substrate
complex
/
prevents
reaction
Un
-
Competitive
Inhibition
Ets
Es
El-P
Lb+É¥
+
,
only
binds
to
ES
complex
%
:
¥
Est
9
/
(UH
Does
not
affect
substrate
binding
and
Inhibits
catalytic
function
Decrease
in
Vmax
;
apparent
decrease
in
kna
No
change
in
km
/
Vmax
Non
-
Competitive
Inhibition
É=GY÷*)És]+Éma×
i
Line
Weaver
-
Burk
;
lines
are
parallel
Binds
enzyme
with
or
without
substrate
s
Enzyme
Allosteric
Regulation
Binds
-10
regulatory
site
canister
'd
÷a¥,ÉÉ("
Binding
of
a
molecule
to
a
different
location
from
active
site
causes
changes
in
Inhibits
both
substrate
binding
/
catalysis
enzymatic
activity
;
either
4)
orcs
,
(4)
or
(
)
activity
of
enzyme
Decrease
in
Vmax
;
apparent
change
In
Km
Allosteric
Inhibition
binding
of
a
molecule
to
allosteric
site
causes
a
shape
change
that
reduces
the
affinity
of
the
enzyme
for
the
substrate
Line
Weaver
-
Burk
:
lines
intersect
left
from
the
y
axis
Allosteric
activator
conformational
change
that
(4)
affinity
Noncompetitive
inhibitors
are
mixed
inhibitors
;
no
change
in
km
of
an
enzyme
for
the
substrate
inhibitor
0
(
t
)
modulator
Enzyme
Non
-
Competitive
Competitive
Inhibition
End
product
inhibition
Substrate
Rtd
2¥
substrate
inhibitor
substrate
enzyme
substrate
Inhibitor
§v
substrate
binding
binding
5µg
iq
site
site
site
binding
Less
active
enzyme
INHIBITOR
substrate
Allosteric
Ste
The
inhibitor
binding
-
Dd
and
substrate
site
_
substrate
Ggg
Cf
64b
Ind
independently
"
%g%
,
substrate
-1
binds
for
¥£÷?.⑤¥¥;÷÷
.
"
"
"
"
"
"
"
"
"
"
"
"
"
G-
"
󲰜
.
chemical
-
"
"
"
"
"
nd
gg.nga.gg?h1b'
+
"
'
same
"
"
^
at
anytime
s
shape
;
compete
reaction
1
LA
"
"
"
"
"
"
"
°
s(
°ᵗˢ"bˢ
"
"
"
Z
binding
site
§
Completing
reaction
fits
e-
ɧ
.
1%
More
active
enzyme
enzyme
undergoing
binding
E
+
um
,
,ma
,
,
,na
,
g
,
,
,
§
,
y
,
+
"
"
"
"
"
"
"
"
"
"
"
"
"
󲰜
¥¥ÉɥɥÉ÷!÷÷󲰜󲰜󲰜
󲰜
.
by
inhibition
end
product
Inhibitor
binds
[
1%4
to
enzyme
;
substrate
reaction
IS
g|
Binding
of
not
carried
instead
Of
too
much
end
product
inhibitor
causes
"
+
:(
"
°
Inhibitor
.
_
excess
binds
to
the
substrate
binding
site
substrate
chemical
ward
to
change
shape
:
without
inhibitor
can
bind
)
reaction
Is
allosteric
site
:
changes
carried
out
/
the
shape
of
the
substrate
causes
chemical
end
product
bind
site
;
substrate
complex
not
carried
out
reaction
-10
be
carried
produced
no
longer
binds
;
stops
out
/
product
produced
metabolic
pathway
"
"
"
"
"
"
"
"
"
"
"
"
"
"
"
"
"
"
󲰜
,
Imai
-
-
-
-
-
-
-
-
-
-
-
-
Fiona
-c+Ty-------_
R
state
¥¥
.
:
!
Allosteric
Regulation
kinetics
;
Kos
"
%
_s[g]gmK%
*
Differs
from
Micheal
is
-
Menten
kinetics
*
[
s
>
(
mM
)

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Competitive

Inhibition

Inhibitors are compounds that

decrease

an

enzymes activity competes

with substrate for

binding

Irreversible inhibitors Cin

activators ) react with

enzyme

Binds

active site One inhibitor molecule can

permanently

shut off one

enzyme

molecule

Does not affect

catalysis Often powerful toxins ;

can also be used as

drugs = ( ÷?)É]+Émax

Reversible

Inhibitors bind -10 and can dissociate from

enzyme a. =z↑CI

]

No

change

In Vmax ; apparent Increase in 14M

Line Weaver

Burk : lines intersect at

they

axis

often structural

analogs

of substrates or

products

1-

c-

  • s
  • Es

up No inhibitor

Often used as

drugs

to slow down a

specific

enzyme

cÉmᵗm) I

can bind -10 :

%

④•-¥

•q:¥¥

free enzyme / prevents binding

of the substrate

El Enzyme

substrate

complex / prevents

reaction Un

Competitive Inhibition

Ets

Es → El-P

Lb+É¥

only

binds to ES

complex

% : ¥

Est

9 / ①

(UH

Does not affect substrate

binding

and

Inhibits

catalytic

function

Decrease

in Vmax ; apparent decrease in kna

No

change in km

Vmax

Non

Competitive Inhibition É◦=GY÷*)És]+Éma× i

Line Weaver

Burk

lines

are parallel

Binds enzyme

with or without substrate s

Enzyme Allosteric Regulation

Binds -

regulatory site

canister'd

÷a¥,ÉÉ("

Binding

of

a molecule to a different

location

from active

site causes changes in

Inhibits both substrate

binding

/ catalysis

enzymatic activity;

either 4) orcs

, (4) or

activity

of

enzyme ecrease in

Vmax ;

apparent

change

In Km Allosteric Inhibition

binding

of a molecule to allosteric site causes a

shape

change that

reduces the

affinity of the

enzyme

for the substrate ine

Weaver

Burk :

lines intersect left from

he

y

axis Allosteric

activator

→ conformational

change that (4)

affinity

oncompetitive inhibitors are

mixed

inhibitors

no change in km

of

an enzyme

for the substrate

④ inhibitor

( t

) modulator

Enzyme Non

Competitive

Competitive Inhibition End product inhibition

Substrate

Rtd 2 ¥ substrate inhibitor substrate

enzyme substrate

Inhibitor §vsubstrate binding binding 5 μg iq site site site binding Less

active

enzyme

INHIBITOR

substrate Allosteric Ste The

inhibitor binding

and substrate ⑨D⑨d site _ substrate Ggg

Cf

€64b Ind

independently

" %g% , substrate

binds for

¥£ ÷?.⑤¥¥;÷÷

""""" ②"

G-

chemical

"nd

gg.nga.gg?h1b'

  • " 'same

^

at

anytime

s shape ; compete reaction 1 ⑨ LA

" " " " °

s(

ᵗ°ᵗˢ"bˢ"""

Z

binding

site §

Completing reaction

fits e- ɧ . 1% More active enzyme ⑥ enzyme

undergoing

binding E

um,,ma

,,na , g,,,

y

"

:÷¥¥ÉɥɥÉ÷!÷÷

by inhibition end

product

Inhibitor binds

[ 1% to

enzyme;

substrate reaction IS g| ⑨ Binding of ↓ not carried instead Of too much end product inhibitor causes

Inhibitor. _ excess binds to the

substrate binding

site ① substrate

chemical

ward to change shape : without inhibitor can bind

) reaction

Is allosteric site :

changes

carried out/

the shape of the substrate causes

chemical end product

bind site ; substrate

complex

not carried out reaction -10 be carried

produced

no longer binds ; stops out

/ product

produced metabolic pathway

"""" " ,

Imai


Fiona

-c+Ty-------_ R state ¥¥

! Allosteric Regulation kinetics ;

Kos

_s[g]gmK%

  • Differs from Michealis

Menten

kinetics

[s> (mM)