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Enzymes Inhibition | Reversible Inhibition | Irreversible Inhibition | Allosteric Inhibition

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This content explains the concept of enzyme inhibition, detailing how inhibitors decrease or block enzyme activity, and explores various types of inhibitors, their mechanisms, and their significant applications, particularly in drug development and medicine.

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so ladies and gentlemen you are all

welcome to my YouTube channel in today's

class we are going to look at the

concept of enzymes inhibition and uh

ladies and Gentlemen please if this is

the first time you are coming to my

YouTube Channel Please Subscribe and I

hope the class will actually

uh be of important to you and uh please

try to subscribe and join my YouTube

membership Community where you'll find a

lot of other interesting

videos and this PowerPoint as we can see

is not made by me it's made

Dr assistant

for so uh let's start with the lecture

so when we said an enzymes inhibitor

enzymes inhibitor so when you said

enzymes inhibitor we know that generally

enzymes is a molecules that

comvert the molecules that convert

substrate to product and enzymes is a

molecule that convert and enzy is a

molecule that convert a substrate so a

substrate here stand for S so enzymes

plus substrate will give partical and

enzymes substrate complex which will

later give us a free enzymes plus the

product so this is how enzymes catalyze

reaction so in a situation where you

have an inhibitor so an inhibitor is a

compound that usually decrease or uh

diminish the rate or velocity of an

enzyme catalyze reaction by infuencing

The Binding and O is turn over number so

generally enzymes inhibitor or an

inhibitor is a ules that when bind to an

enzymes is

decrease or block the activity of the

enzymes completely so it can either

decrease the activity that is the

velocity of the enzymes

or completely deactivate the enzymes

activity so that is what you call

enzymes inhibitor so it's a molecule or

it's a compound that when bind to the

enzymes it can either decrease or diminish

diminish

the velocity of the enzymes or the turn

over that is how speeds when you said

velocity it means house speeds the

enzymes is catalyzing the substrate to

product you can have the situation where

you can have an enzymes maybe

in one micro minute in one micro minute

maybe the enzyme is converting 100

substrate to product but in the presence

of an inhibitor the activity or the

velocity of the enzymes may be

decreased by maybe instead of converting

100 substrate to product it will end up

of converting maybe five substrates to

product so it means that the activity or

the turn over number of the enzymes is

decreased by the inhibitor so that is

what we call an inhibitor so this

inhibitor uh actually classified into

organic so it can be organic the

inhibitor can be organic or it can be in

organic so these are the actually class

of inhibitor it can be organic that is

maybe it's D from organic molecules or

it is an inorganic so

uh one very interesting things that we

should understand is that the enzymes

the enzymes can be sorry the inhibitor

can be trops like in so many cases in so

many cases most of the drugs that we

produce and the pharmacy IAL industry

there are Inhibitors of enzymes so uh

that is why understanding the knowledge

of uh inhibitor and enzymes is very very

essential in the area of Pharmacy and

medical Sciences because with the

knowledge of enzymes and enzyme

inhibition you can be able to develop a

new drugs for a particular disease and

also in addition so many drugs so many

drugs are enzyme inhibitor like for

example uh we have like Anin combating

enzymes it's an enzymes that produce

anint one unj tens two and anint tens

two is a constrictor so actually anint tensin

tensin

enzymes com enzy is an enzymes that is

associated with hypotension so if you

can get any mo that can block or that

can diminish or decrease the activity of

an converting enzy

to prevent conversion of an one to 2 it

means that the molecules can serve as

antihypertensive drugs so that is why

you need to understand that if you are

able to understand the enzymes they the

the the what the enzymes is actually

catalyzing and the products what are the

importance of the products that are

catalized by the particular in a system

is very very essential so if you're able

to do that if you are able to know that

them from there you will know whether

the enzymes is a very good Target in

terms of Dr design Discovery so it is

very very important to understand that

so many enzymes so many enzymes

Inhibitors there are drugs so that is

why as a student of medical Sciences you

need to understand the importance of the

Inhibitors try to understand how the

Inhibitors are what are they meant for

it is very very essential

and in addition some of these enzymes

they are some of these enzyme inhibits

they are antibiotics of course when you

said antibiotics remember there are

molecules that are actually involve in uh

killing microorganisms especially

bacteria so antibiotics are the

molecules that

kills microorganisms so it cure disease

that are ass assciated with the

infection and of course remember that

some of the bacteria they are classified

as positive and gr negative bacteria so

the major molecules that actually

protect the

microorganisms especially bacteria from

any AAL attack is the pepti glycon that

is found on the cell of the bacteria so

there are some enzymes that are imported

in actually biosynthesis of fog glycan

on the wall of the on the cell wall of

the bacteria so there are so many

antibiotics like for example fyin and

pin there are drugs that inhibit the

enzymes called

transas the transes is one of the key

enzymes and the synthesis of

plycon so of course pheline is an enzyme

that inites the activity of transes and

as a result of that glycine cannot be

produced so iFly cannot be produced it

means that the solell of the bacteria

will not be actually built you canot the

cell will not be produced as a result of

that the microorganisms will die so we

should understand that some of the

antibiotics that are available in the

market they are enzymes Inhibitors and

of course some of the Inhibitors they

are toxins at what stage or at what uh

State can we consider an enzymes to be S

an enzyme init to be a toxins maybe that

is a particular enzyme that is very very

important for the survival of human like

for example let's just let me just give

a s an example of let's say aalin aalin

is an enzymes that actually degradate

aalin asalin is a neurotransmitter that

help in the transmission of information

between other part of the body to the

brand so if you can get any molecules

that can inhibit the activity of AAL so

what will happen it means that estalin

cannot be actually degradated to produce

the product which actually help in the

uh transmission of information between

the body and the brain so if you are

able to actually or if there is any

component can inhibit the activity of

those enzymes it means that it is a

toxins because it blocks an enzymes that

is very essential to the survival

of living organisms of a human being so

that is where we should understand that

like in so in so many cases let me just

give our examples of uh of some of the

anti some of the

toxins like for

example there is what you call uh

uh incde some of the

insecticides they are toxic so if human

take them like for example like is a

insecto side that is called Pia so it's

an insecto side that if you take it it

will block the activity of some

important essential enzymes in human and

that is why it can lead to the death of

human so we should understand that some

of these Inhibitors they are

antibiotics then in addition the next

thing that we are going to look at is of

course some of these inhibitor they are

antimetabolites they are antimetabolites

what is antimetabolite when we said

metabolite there are molecules that are

involved in the metabolisms of

uh of some uh food product that we are

taking so you said antimetabolite it

means that there are molecules that

prevent the body to utiliz the metabol

that in the body some of them they are

natural products of enzymes reactions so

these are actually some of the

Inhibitors that are found in humans and

also their classical groups so some are

drugs some are antibiotics some are

antimetabolites some are natural

products so uh that is actually enzymes

Inhibitors enzymes Inhibitors it means

that there are molecules that prevent

the enzymes or that slow down the

activity of an enzymes or in some cases

it can even completely block the

activity of the

enzymes so then uh let's now look at the

types of enzymes Inhibitors so enzymes

Inhibitors are divided into three we

have one we have reversible inhibitor so

you said reversible Inhibitors it means

that it's a stage where or a types of

inhibitor where if the inhibitor is

removed from the enzymes the enzymes can

still continue with it activity like for

example if you have the inhibitor

let's say you have the inhibitor you now

have the enzymes plus the inhibitor so

when you have the

enzymes when you have the enzymes plus

the inhibitor to give us enzymes

inhibitor it means that at this point

when you have an enzyme inhibitor

complex it means that that is the the

substrate cannot bind so but in a

situation where the Inhibitors is

removed you will have your three enzymes

then plus the inhibitor then the enzymes

will actually uh go back and convert the

substrate so it means that it's a

reversible because when the Inhibitors

Inhibitors can be removed and the

activity of the enzymes will be restored

so that is

reversible enzymes inhibition and we

have two types of reversible enzymes

inhibition we have what we call

competitive inhibition we have non-c

compettive reversible enzymes init and

we have on

on competive

competive

enzymes inhibition so these are actually

three types of RS inhibition and then

the second other types of enzymes

Inhibitors we have a RS so you said

irreversible enzymes inhibition it means

that there are molecules that once they

bind to the enzymes then it means that

the enzymes will commit suicide the

enzymes will actually will not longer

reverse to not restore it is activity

because it is the Inhibitors is binded

to the enzymes using the calent process

but in the case of reversible

inhibitions why the enzymes actually

Resto it activity is because the binding

between the substrate and the inhibition

is using a noncovalent forces like

hydrogen bonding Bond force of

attraction and electrostatic so that is

why the Inhibitors can be removed and

then the enzymes can restore it is

activity but in the case of irreversible

because the inhibition between or The

Binding between the enzymes and the Inhibitors

Inhibitors

is using calent bonds so as a result of

that it is very very difficult it is

very very difficult to remove that types

of inhibitor from the enzyme so that is

why it is called suicide

Inhibitors and then the next time of

enzymes inhibition is allosteric so

generally enzymes they have other site

apart from the active site so we call it

aleric site so aleric site is a site

where the Inhibitors combin and

inactivate or activate the enzymes so

but in this case we are thinking about

Inhibitors so enzymes have aleric side

where the Inhibitors bind and then

decrease or block the activity of the

enzymes so uh this is actually these are

the types of the enzymes inhibition so

now we are going to look at them one

after the other so starting with actually

actually

reversible inhibition so in IR

reversible inhibition here the inhibitor bind

bind

noncovalently so that's why it is the

Inhibitors find noncovalent so you said

noncovalently it means that the

interaction is a weak interaction so

noncovalent interaction as I said from

the previous slide it can be hydrogen

bonding it can be Bond because of

Attraction it can be electrostatic force

of attraction so the Inhibitors V

noncovalently with the enzymes so if the

inhibitor is removed then the action of

the enzymes will be fully restored so

when the enzymes when the Inhibitors are

removed then it means that the activity

of the enzymes will be fully restored

to so generally an equilibrium is

established between the free inhibitor

and enzyme substrate and enzymes

inhibition complex and is defined by an

equilibrium constant and the equilibrium

constant is Ki which is called

inhibition constant so we have enzymes

plus substrate then we have enzy

substrate complex so generally an

equilibrium is established between the

uh the the free Inhibitors and the

enzymes of complex and of course the

activity of the enzymes is fully

restored on removing the Inhibitors by

dialysis so with just a simple dialysis

you can remove the inhibitor from the

enzymes active side because the

direction is very weak so

um so now let's look at of course the

types of enzymes inhibition so the types

the types of reversible enzymes

inhibition so we are starting with

competive so from the the word

competition it means that of course

there is a competition and of course the

competition in the case of this reverse

gr enzymes oh sorry competative

inhibition is between the inhibitor and

the substrate because the substrate and

the inhibitor they look alike like for

example now let's look at this this is

the enzymes this is the enzymes and this

is the substrate so look at the

substrate here

look at the inhibitor so if you look at

it clearly here you can see that the

enzymes and Inhibitors they look alike

so therefore the enzymes if the enzymes

is binded with the substrate then of

course the enzymes substrate complex

will be produced which is this and then

of course the free enzymes will be

generated and then finally the product

will be form but in the case of uh this

inhibitor when inhibitor bind to the

enzymes so there will be no catalysis or

it may actually decrease the catalysis

of the enzy and one very interesting

thing that we should understand that

inhibitor bind

reversibly the same site that the

substrate bind to so the inhibitor is

bind to the active side where the

substrate bind to and compete with the

substrate for The Binding so the

inhibitor is actually a substrate analog

it closely resembles the

substrates so it can be actually

reversed by increasing the concentration

of the substrate so uh one very

interesting things that we should

understand in these types of compettive

inhibition this if you have the

substrate and the inhibitor in the same

in the same

same

environment so

what will

determine whether the substrate will be

the one to find or the inhibitor so at

that point actually the concentration

matters if the concentration of the

Inhibitors is higher than the

concentration of the substrate then the

inhibitor will bind to the active

sides but if the concentration of the

substrate is higher than the

concentration of the inhibitor then the

substrate will B and then catalysis will take

take

so that is what happen

so of course this one is another example

so this is the inhibitor this is uh look

at it here this is an e this is the

substrate and this is the competive

inhibitor so you see in this case the competive

competive

inhibitor bite but of course here

increasing the concentration of the

substrate here by looking at how the

concentration of the substrate increase

here look at it here we have one

inhibitor one substrate so that is where

the inhibitor B but in this case we have

the concentration of the Inhibitors to

be very high so after increasing the

concentration of the inhibitor then the

sorry the concentration of the substrate

then the substrate will now removed it

will now remove the subst the inhibitor

and then the substrate will bind so that

is what happen that is how the

inhibition revers is is actually

reversed by increasing the concentration

of the substrate so of course here after

increasing the concentration of the

substrate then the inhibitor was

actually removed and then the substrate

pil so the degree of inhibition depend

on the concentration of the

substrate depend on the concentration of

the substrates and on the relative

affinities of the enzymes for

substrate and the inhibitor so you

should understand that actually in this

point or in this uh in the case of this

competitive inhibition concentration

matters a lot concentration matters a

lot if the concentration of inhibitor is

higher than that of the substrate then

the inhibitor will B but in the case

where the concentration of the substrate

is higher than that of the uh of the uh

of the the inhibitor and the substrate

will now bind so uh that is this so This

is actually a brief discussion on the compettive

compettive

inhibition so now let's look at how the

compettive inhibition work so you see in

this point we have an Appo enzymes which

is an active enzymes so we have the

substrate and we have the inhibitor so

substrates with B to the enzymes and of

course there will be an enzymes product

formation where the product will be

generated but now here look at it here

we now have inhibitor so the inhibitor will

will

now bind so if the inhibitor bind to the

of course active site then it means that

there will be no catalysis so this is

another example this a compettive

inhibitor and this is the prod and this

cells so we should understand that in

the presence of inhibitor because the

enzymes and the substrate are sorry the

enzymes and the inhibitor are conf for

the same poet or the same active SES so

this is actually what happen so the concentration

matters so now what happened if you have

a competative inhibition what happened

to the kinetic par parameters what

happen to the kinetic parameters so

generally in the presence of compettive

Inhibitors velocity generally

decrease the velocity generally decrease

you see this is the velocity decrease

therefore the effective concentration of

enzymes is

reduce and of course the km is increase

so remember that ladies and

gentlemen the lower the km the higher

the inity of enzymes toward the

substrate so if the km value increased

it means that the uh activity or the

Affinity of the enzymes toward the

substrate also decrease so this is what

happens so because km is increased then

the Affinity of the enzymes toward the

substrate is apparently decreased in the

presence of the inhibitor but V Max is

not affected so you should understand

that the kinetic parameters

in enzymology is KM and Vmax so in the

case of compettive inhibition Vmax

doesn't change it doesn't affect the

Vmax that is the maximum velocity but km

is affected by increasing it is

concentration so this is actually a

graphical presentation of

uh a graphical presentation of competive

inhibition so you see here this is using my

M you have the parabolic shaped

shaped

graph so this one no Inhibitors and this

inhibitor so it doesn't affect the V

Max but of course look at the km so the

km in the absence in of Inhibitors look

at it here it's very low but in the

presence of the inhibitor is increased

so this is the new km when the

substrates when the Inhibitors fine when

the absence of inhibitor is low so the

lower the concentration of course the

higher the Affinity of the m so but of

course we know that we this is a line w

box representation of the competitive

inhibitor of course in the presence of

inhibitor look at what happened but look

at the point where we have the P Marx

nothing ch

there is nothing change also here look

at it nothing change so that is the V

Marx it doesn't affect it here also look

at it where there is inhibitor and no

Inhibitors they still meet at the same

point so V Marx it doesn't affect it but

of course look at it here in the absence

of inhibitor look at the VX here sorry

km and also in the France of in look at the

the

K so you should understand that the Vmax

it doesn't change in the case of

competive Inhibitors but the

velocity of the Vmax sorry the km it is

actually increased thereby decreasing

the activity of the enzymes toward the substrat

substrat

so let's look at example here this is

malonate so malonate is a competive

inhibitor of su de hydrogenous

enzymes so we have of course the enzyme

is an enzyme that is an enzymes in

citric acid cycle

where the enzymes combat Sate to ferate

so the malonate here is an example of

competitive inhibitor

of suat so look at it the only look at

the structure of the subate and M and and

and

Bon it they looks similar they look very

similar so in the presence of this

inhibitor it will block the activity of

the suin the hydrogenous therefore the

suin will not be converted into

fate so look at actually this is

the enzymes so the enzymes is

here and this is the substrate and of

course we have subate enzymes complex

and then we have fumate was the but in

the presence of melanoid

melanoid

malonate the enzymes B to the malonate

and of course the activity of the

enzymes will be blocked therefore there

product to be produced so that is in the

inhibition so Al this is another example

antibiotic action of sulf drugs that is

sulfonamides it has a structural analog with

with

FL FL that is para

see the the enzymes

called teroid synes is an enzymes That

comat Power Plus 78

dihydro dihydro teric acids produce

folic acid and you know the importance

of folic acid it is very very

important in uh in developing baby during

during

Francy so the major enzymes in in the

par synthesis of folic acid and that is why

why

sometime because folic acid is very very

important especially during Francy so

generally you see that fragant wom in

some cases they are supplemented with

folic acid because it is needed for the

growing babies

so this power

power

plus 78

dihydro acid is converted into folic

acid in the presence of theid

entities but in the presence of the sulf

that is sulf it is having a structural

analog with the fiber with the F that is

amzo acids so it will now

bind with

the enzymes

therefore it will now inhibit the

bacterial enzymes so this is actually in

bacteria in bacteria the synthesis of

folic acid is in bacteria so but it's

not to humans human cannot synthesize

folic acid so generally human in human

we cannot synthesize folic acids so we

don't have these enzymes but if you want

to kill bacteria you can use the

sulphonamides to inhibit these enzymes

who can prevent the synthesis of folic

acid so as a result of that it will kill

hum so soorry it will kill the bacteria

so because we in humans we like these

enzymes that is why the sulfur drugs

will not affect us it will not affect us

because we don't have

enzymes and then so these are the

example of clinically

useful compettive Inhibitors that are

for disase treatment for example we

have STS an example of this St we have

example of this St we have

have

aob we have

have

Simas so they actually the Inhibitors

they are compettive Inhibitors that's

Target an enzymes called HMG Co reducts

and they are trtic use they actually

have to decrease plasma cholesterol

level and also it has antiy liid

agents so it reduce

the so another examples of uh this uh

Inhibitors we have uh

alool so we have

alool which also inhib which Target an

enzyme antin

oxidase so of course this alol because

stin Ox is one of the enzymes that

involve in the degradation of uh U uh

and the degradation of nucc acid to

produce uh uric acid and you know that

theout disease is associated due to

accumulation of uh due to accumulation

of uric acid which is the end product of

nucleic acid so using alool is a

competive inhibitor ofin oxidation that

use in the treatment of C disease and

you also have metet which is also a

competive inhibitor of dihydrofolate

reductors which also used in the

treatment of cancer and there is also

cup we have C we have C we have cup C to

and and and AF which is also uh a

competitive Inhibitors in Anin

converting enzyme so it inhibit Anin

converting enzymes which is used in the

treatment of high blood prev that is

hypertension remember that actually from

uh the previous slide we I actually

discuss about this so and combating

enzymes foru V constrictor which is an 2

so these are some of the Inhibitors or

drugs that are used to inhibit the

activity of the enzymes which actually

have lowering lowering blood frion we

have we have diomal which is also uh

init vitamin K epoxide redu enzymes and

used in the treatment of

anti-coagulant ser as

anti-coagulant so uh

this is actually examples of some drugs

that are comput Inhibitors and the

enzyme that they are targeting and their importance

importance

in the D in disease

treatment so um the next thing that we

are going to look at is a non-c

compitative inhibition so in the case of

non-c compitative Inhibitors in this

case the enzymes is not actually binding

to the active site the Inhibitors bind

at a side older than the active side of

the enzyme so it's not binding at the

to so in this case in the case of this

uh non-c compitative

inhibition the inhibitor it has no

structural resemblance to the substrate

so there is no structural resemblance

between the uh substrate and the

inhibitor so no comp competition for

binding so in this case there is no

competition for binding and of course

increasing the concentration of the

substrate it doesn't

relieve this inhibition it doesn't

relieve the inhibitor from Bing the

active side so the inhibitor and the

substrate bind at different sides and

therefore in this case the enzymes

combind to the substrate and as well as

the inhibitor to produce enzymes

inhibitor substrate complex so it's

possible to produce both enzymes in hio

complex and enzymes in hibo substrate

complex it is possible to produce both

the two so the enzymes inhibition

inhibito substrate complex

forms product at a slower rate than

enzyme substrate complex so therefore it

will slow the reaction very low

therefore the rate will be very low when

the inhibitors

to the sub string so the reaction is

slot but not Haled it usually not heed

it usually not block the reaction

completely rather it slow it it's it

slow the reaction very well so you see

this is actually the other site where

the Inhibitors bind and this is the site

where the substrate will

bind so therefore there is no

competition in terms of the ACT side

between the inhibitor and the

enzymes so uh then the next thing is of

course still under inhibitor so you see

this is the enzymes and this is the this

is where we have the inhibit this is the

inhibitor this is the substrate so this

is the enzymes active sides this is the

inhibition binding s so of course here

we can the substrate combined to produce

an enzyme substrate complex and will now

have the product but a situation the

enzymes substrate complex you can have

the enzyme substrate complex and then

the inhibitor at the same time bind to

produce the

enzymes substrate inhibition complex so

the product is formed at a slower rate

but not halted and you can also have a

situation where the Inhibitors will B

PRS like this and Then followed by the

substrate so you can have the two

cases so you can either have the

Inhibitors first bind to the substrate

or the substrate will first bind before

the inhibitor bind so you can have the two

scenario so what happened to the kinetic parameters

parameters

so in the case of KM the km remain

unchange so if the km remain onchange

then it means that the inhibitor do not

interfere with The Binding of the

substrate to the enzymes and the Vmax

decreases therefore the inhibitor cannot

be overcome by increasing the

concentration of the substrate so this

is what actually

using the

mement graph that is hyperbolic you see

this is the km this is the km so the km

it doesn't affect it the km doesn't

affect it and of course the V Marx

change loc at here it changed so as you

have as you have the Inhibitors the Vmax

change in the case of nonc competive

Inhibitors look at also using the line r

box plots you see that the km remain the

same it remain the same look at it here

and then the V marks change with the

inhibitor and with no inhibitor the V

Marx change so that is what happened in

the case

inhibitor so non comp example of non-competitive

non-competitive

Inhibitors we have heavy metals like for example

example

silver ion merury ion and Lead ion and

cile

sh of the enzymes that is in the the [Music]

[Music]

Sile T grow of the enzymes and then we

also have P which also

in which actually non competively

inhibits fsin we have inhibitor we have

ethanol or narcotic drugs that

inhibits acid

phosporus nonc

competively so this is actually what

happened in the case of non-competitive

inhibition so the next one is

uncompetitive inhibition so what

happened in the case of uncompetitive

inhibition in this case the inhibitor

bind only to the enzyme substrate

complex not to threee enzymes but you

see in the case of non-competitive

Inhibitors the inhibitor can bind to the

free enzymes and it can also bind to

enzyme substrate complex but in this

case uncompetitive

inhibition the Inhibitors usually V to

enzymes of complex not the free enzyme

and the inhibitor cause structural tion

it change the structure of the active

side of the enzymes so therefore the

enzymes become catalytically inactive

then the inhibitor can't be revised by

increasing the substrate concentrations

since the inhibitor doesn't compete with

the substrate for the same binding SES

so the inhibition of like for example

the inhibition of placental alkaline

phosp that

is call it enzymes

enzymes

by Alin so look at it this is an enzymes

so first the enzymes bind with the

substrates and then the substrate will

now bind soon so the inhibitor will now

bind to enzyme substrate complex so that

is why it is called uncom ination so

after the inhibitor B then it will now

distort it will now change the structure

of the enzymes active

sites so this is what happened you see

this is an enzymes so we have an enzymes

and the substrate so the enzymes first

look at it here the enzymes first but

the substrate then we now have enzyme

substrate complex and then we now have

the inhibitor and then the inhibitor

will now binds so after

that we now

have enzyme sub inhibition inhibitor

complex so in this case we have enzy

substrate and then we have enzy

substrate complex from the inhibitor

then we now have enzyme sub inhibition

complex so in this case the Vmax

decrease the km decrease then inhibitor

has no affinity for free enzymes it

doesn't have Affinity to free enzymes so

you see the km change both in the line w

box and the M menting graph the

km the km change and the VX change so

both the two change so that is what

Inhibitors so then the next thing that

we are going to look at is the

irreversible inhibition so irreversible

inhibition is the types of inhibition in

which the Inhibitors Vine covalently

with the enzymes so it is usually a

reversal so it can it can't dissociate

from the free enzymes it cannot

dissociate from the enzymes after

binding to the uh to the enzymes because

the bonding is very strong so the

inhibitor cause confirmational change at

the Active side of the enzymes

destroying their capacity to function as

a catalyst so once they inhibitor once

the reversible inhibitor B to the

enzymes cently it will now change the

conation of the enzyme active side

thereby it will now completely destroy

the enzymatic activity of the enzyme so

the catalysis of the enzy will be

completely dissociate and the enzy

activity is not reg as

dialysis or by increasing the substrate

concentration and of course a variety of

poisons such as

iodoacetate Organo prosate poisoning and

oxidizing agent act as a

inhibition so let's look at what happen

in the case of irreversible inhibition

in terms of the kinetics irreversible

irreversible

irreversible is similar to non compitative

compitative

inhibition where the V Marx decrease and

then the km no change there is no change

in km so you

see the km here Remains the Same but in

the presence of inhibitor look at what

happened in the absence of inhibitor the

Vmax change so Vmax change in the

presence of the

inhibit so these are the examples

of the irreversible Inhibitors we have

dium which actually uh

inhibits alides de hydrogenous and is

used in the treatment of

alcoholism we have cite which actually

uh inhibit cytochrome oxides and this

one it inhibit respiratory change so

when that is where we have cide

poisoning cide poisoning can even lead

to the dates a particular individual

because it affects cytochrome oxid which

is a key enzymes in respiratory so once

this enzymes is inhibited there will be

more energy no energy would be generated

and of course as a result that if

the care is not taking a person will die

there is a fuite also inhibit an and an

is the key enzymes in glycolysis so

therefore the glycolysis will be

inhibited so we have so many of them

here we have the iso profile

fluorophosphates which actually

inhibites serin protasis and acetal

estal acalin EST

and they are Ser as enough gas so these

are actually some of the example of

inors they are

function so then the next one of course

is suicide inhibition so it's a

specialized form of a with inhibition

also known as mechanism based Activation

so it make use of enzymes on reaction

mechanism to

inactivates to inactivate it so in this

case the inhibitor of a structural

analog a structural analog is converted

to a more effective Inhibitors with the

help of the enzymes to be inhibited so

the enzymes literally commit suicide

they utilize normal enzymes reaction

mechanisms to inactivate the

enzymes that is in the case of Sude is a

specialized form of irreversible

inhibition but in this case the

inhibitor use the course the enzyme's

own reaction mechanisms to activate the enzyme

enzyme

itself and of [Music]

[Music]

course in this case the enzymes

literally commit suicide

suicide

because they utilize normal enzymes

reaction mechanisms to inactivate the

enzymes these are the examples of the uh

suicide inhibitors

aspirin al alool

alool

Five Ur and of course these are the

products and these are the enzymes that

they targeted and these are the

example the suicide Inhibitors the help

in the treatment of

chosis also non

nonsteroidal and inflammatory drugs

cancer and

gouts so then the next thing is altic

inhibition so what is aleric inhibition

so generally enzymes have old

sides apart from the active SI so that

other site we call it Al aleric sight so

you see some enzymes possess additional

site other than the active site and the

site is called an aleric site e site

that is AIC side of our enzymes and they

are unique on o molecule so these aleric

effectors they are the substances that b

the aleric side and regulat the enzyme's

activity so in this case we can have a

positive althetic

effectors so if the positive althetic

effectors in this case the enzy

activities is increase so once the

molecule bind to the aleric side will

increase the activity of the enzymes but

we have a negative allosteric activators

or effectors what they are doing is when

this negative allosteric effectors B to

the active site then it will now inhibit

the activity or it will now decrease the

enzym activity and in the case of aleric

enzymes when the

altic uh molecules bind to the altic

side of the enzymes then the Shi of the

graph will change from the normal

molic Shi graph to give sigid C graph so

this is actually what happened in the

case where the inhibitor is not a

substrate analog and it is a Fally

reversible so when excess when excess

substrate is added then it will now

reverse The Binding and then the km is

usually increased and then V Max is

decreased in the case of aleric

Regulation so when an Inhibitors B to

the aleric site the configuration of the

active side is modified such as such

that the such that the substrate cannot

bind properly and as a result of that we

will now get a sigmoidal shift that is

how the sigmoidal shift of the

enzymes is

generated so you see km is increased and

V Marx is reduced you see the km here if

you look at the km

here you see in the absence of the

inhibitor and in the presence of

inhibitor look at how ites and then the

V Marx also decrease in the presence of the

the

inhibitor so

that is what happened in the case of

at how it works so we have active SES we

have the enzymes and we have the aleric

site so these the enzymes in the enzymes

we have active site and we have

allosteric site so when the allosteric

inhibitor bind to the active side bind

to the aleric side then it now distorts

the configuration of the active side of

the enzymes and as a result of that this

is the distorted active site then of

course the substrate will now bite so

the molecules can be altic regulators

and can be altic inhibitor so you see in

this case this is where we have

allosteric inhibitor so once the

inhibitor bind then it will now distort

the active side of the enzy so as a

result of that the activity of the

decase so these are the examples

of the

aleric examples of the allosteric

molecules you see here in this case we

have glycolysis the fat we have

glycolysis TC in the glycolysis we have

phosphorus one and the inhibitor that

bind to the aleric side of the one

a TP and citrate and the activator is a

positive aleric activator is so this is

how we have the Inhibitors and the

activators the enzymes they actually

activate or deactivate and the

pathway so let's look at the example you

see this is a phosphate where it's converted

converted

toose Six B phosphate is an enzym

callus one so you see uh the enzymes

here this is the catalytic subunit of

the enzymes and this is the Bing side

and this is the

inory subunit of the enzymes and this is

the EMP binding site so you see

here ATP is a

negativity and then m is

POS so the P of pfk is quary protein and

has two alic regulator side and a active

side so the two altic Regulators one is

for the activating and one for

inhibiting so you see here ATP in it is

regulatory binding side you once it CL

then it is this is a in inhibitory sub

unit and this is the activating sub unit

so The Binding side for the substrate

presently and impossible pit to the

catalytic activity has been lost because

once this ATP is actually binded then of

course the active side of the enzymes is

distorted so nothing the subet cannot

bind so it means that we lose the

activity of the enzy so now let's look

at this in this case look at it when we

have EMP bind so you see The Binding

side for the substrate presently and

excellent pamp form an excellent pit

when B and of course there will

be full catalytic ability of the

enzymes so that is actually for the

allosteric sit and then we also have

what you call uh feedback negative

feedback inhibition and end

product inhibition so there a

specialized type of aleric inhibition

and this is ired to control the

metabolic fat ways for efficient

cellular function so you said end

product of a metabolic reaction produced

in excess so when the end product of a

particular metabolic reaction is

produced in excess so it inhibit the

first regulatory enzymes in the Su so in

the end product inhibition we have a

situation where the Cod of a particular

like for example in glycolysis the end

product of glycolysis is ATP so when

this ATP is built off at the end then it

will now come back inhibit the first

enzymes of the glycolysis like for

example in glycolysis we have 10 enzymes

and the end product is ATV so when ATV

is producing enough enough it will now

come back to inhibit

the face enzymes or the regulatory

enzymes like for example in glycolysis

we have three regulatory enzymes so if

the n product of glycolysis which is ATP

inhibit the activity

of the enzymes the first enzymes or the

regulatory enzymes so that is described

as n product inhibition or negative feedback

feedback

inhibition so like for example let's

look at this

so in the negative feedback let's say

this D is the end

product and you see because it is the

end product now it's built up then it

now come back and actually inhibit the

face enzyme so that is what happen in

inhibition so these are actually

that end product ination we have him

which is the end product and the enzymes

to be inhibited we have all synthes and

the part is him synthesis we have

cholesterol which is the n product and

it meet HMG Co do which is the first

enzymes or the key enzymes in

cholesterol biosynthesis and the f Way

the pathway is cholesterol synthesis so

these are the some of the example of end

product that it repeats the face enzymes

or regulatory enzymes and the part way

are so this is actually uh some basic

comparism between all the

tree so all the form all form of the

Inhibitors all the form Inhibitors this

is just the summary so you can just look

at the summary and understand what how

one differ from one another as we

explained like for example in the

compettive inhibition the structural

similarity there's a structural

similarity between the inhibitor and the

substrates but in the case of nonmutated

inhibitor there is no structural

similarity and of course in the case of

irreversible inhibition the inhibitor

bind tightly to the enzymes by calent

Bond then in the case of althetic the

inhibitor B to the althetic side of the

enzymes and then the for the suicide

inhibition then the inhibitor make use

of the enzymes on reaction mechanisms to

inactivate it but for the end product

inition then the end product inhibit the

earlier enzymes of the fat so this is

just the differences between

them so now let's look at the importance

of enzymes in evion number one it's

helpful understanding the regulatory or

the regulation of

enzyme activity within the living C with

the living cells and it is also usable

in elucidating the cellular metabolic

fats by causing accumulation of enti

also it help in identification of the

catalytic or the functional GRS and the

active side of enzymes it also provide

information about substrate specificity

of enzymes it is also useful in to study

the mechanisms of of catalytic activity

and the enzymes Inhibitors after a f

application so DRS useful in medicine I

feel to be I feel punction by inhibiting

a certain en so most drugs are competitive

competitive

Inhibitors are competitive or suicide

Inhibitors so ladies and Gentlemen

please if you didn't join to my YouTube

Channel please try and join to my

YouTube channel and I hope this video

would be of help and please subscribe

thank you thank you for

attending this lecture Please Subscribe

and join my YouTube Community for more videos

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