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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.
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Inhibitors are compounds that
an
enzymes activity competes
activators ) react with
enzyme
active site One inhibitor molecule can
enzyme
Does not affect
catalysis Often powerful toxins ;
drugs = ( ÷?)É]+Émax
Inhibitors bind -10 and can dissociate from
enzyme a. =z↑CI
In Vmax ; apparent Increase in 14M
they
axis
analogs
products
1-
up No inhibitor
drugs
specific
enzyme
cÉmᵗm) I
%
•q:¥¥
free enzyme / prevents binding
El Enzyme
complex / prevents
reaction Un
Competitive Inhibition
←
Lb+É¥
binds to ES
% : ¥
9 / ①
Inhibits
catalytic
Decrease
in Vmax ; apparent decrease in kna
change in km
Vmax
Competitive Inhibition É◦=GY÷*)És]+Éma× i
are parallel
Binds enzyme
Enzyme Allosteric Regulation
regulatory site
Binding
a molecule to a different
location
site causes changes in
enzymatic activity;
, (4) or
activity
enzyme ecrease in
Vmax ;
change
In Km Allosteric Inhibition
binding
shape
change that
affinity of the
for the substrate ine
Weaver
lines intersect left from
he
axis Allosteric
→ conformational
change that (4)
oncompetitive inhibitors are
inhibitors
no change in km
an enzyme
④ inhibitor
( t
Enzyme Non
Competitive Inhibition End product inhibition
☒
Rtd 2 ¥ substrate inhibitor substrate
Inhibitor §vsubstrate binding binding 5 μg iq site site site binding Less
enzyme
substrate Allosteric Ste The
and substrate ⑨D⑨d site _ substrate Ggg
€64b Ind
" %g% , substrate
binds for
""""" ②"
G-
chemical
"nd
at
s shape ; compete reaction 1 ⑨ LA
" " " " °
Z
binding
Completing reaction
fits e- ɧ . 1% More active enzyme ⑥ enzyme
um,,ma
,,na , g,,,
"
by inhibition end
[ 1% to
substrate reaction IS g| ⑨ Binding of ↓ not carried instead Of too much end product inhibitor causes
Inhibitor. _ excess binds to the
site ① substrate
ward to change shape : without inhibitor can bind
Is allosteric site :
carried out/
the shape of the substrate causes
bind site ; substrate
not carried out reaction -10 be carried
no longer binds ; stops out
produced metabolic pathway
"""" " ,
-c+Ty-------_ R state ¥¥
→
! Allosteric Regulation kinetics ;
_s[g]gmK%
Menten