Serine Proteases

Serine Proteases


N
&
~
SUBSTRATES, TRANSPON STATE, Product An COMPLEX MCLUdES THE Enzyme
Enzym
:




- Often THE

- -
of
Enzyme's
Brodig
- -
And THE SUBSTRATE THAT Brods a The ActresMe .




*

-- 17-
-

/
Y

Y ENEYME'S ACTIE INDUCES CONFORMATIONAL



Y
THE SUBSTRATE

CHANGES
AS THE




3- i
SME

-
F /




:
/ ~ " / YI
7

IS
-




foreton of
S
iW Bonding
In The SoBSTRATE Due MERACTroms This Results




i·
&-
To . no




j
S - S
u
u




G i
Bond


Y&
: Products ARE RELEASED AFTER
deAnge
TRANSPON STRE

O
A
I S/ .
.




y
--




Y
-




- > Energy Required
& THE ES
CENEymE SuBSTRATE) COMPLEX
&
LOWERS THE REACH THE



*
To

! -




-six
H




&
& - * TRANSARON STATE . M IS ONE Kid of INTERMEdNATE . ANOTHER B THE
EP(Enzyme-
-
- ↳
= -
-

V Product) complex Intermedies fre local
energy diagram
/ . THESE maint ou ano .
(-
-
of
j
11
Types Catalysis
SS
y . Acid-BASE
1

CATAlySeS : Residues N THE
Enzyme ACTIE SME DONATE (Acid CrAlySrS)


* SUSTRATE Binding POCKETS OR ACCEPT (BASE CATALysis) A proton


TyR, CYS , Lys , His ARE PROTEN
2
Chymorypso Trypsm ELASTASE
Spe
.
Content Catalysts : Ser ,

groups
They Serve As


Apitoic
2
ES Content THIS duE THE
PRESENCE of LOVE PARRS i n Content
Catalysis
CATAlySTS . TS TO .




BECOME DEPROTONATED AND ACT AS
NUCLEOPHIES ATTACK ELECTRON
THEY
THE

GROUPS
THR .




Gl Gly Gly t Gl
VI deferent Toms On Sustrates To form COVALENT intermediates .
CHyMoTRIPSON USES
-
SER
SER Asp
ACTRATED SERNE ALKOxide ION TO Attack The pepTrdE Bond .




THE
CATALYTIC
TRAAD


CHyMOTRIPSiN : is A
Type
of Serve PROTEASE That
Hydrolizes peperde
THE ACTNE SME of
cymOTRipso · His 57
HOSTINE
① ⑨
Is So REACTIE DUE TO BASE
Bowds . If A RESTOUE frIS INTO ChyMORPSM's ACTIVE SME , THE ENEymE clEAVES THE
⑨
Astr ⑨
· ⑧
I
⑬
of A Serve
-----
"
Residue ⑨
pepTrdE Bond Immediately After REsrdUE Catalysts ⑧ - ⑨



...
CHAN As The THAT - -
-
& ⑨
7
⑧
-
·
.




=
To form A SERENE ALKOxidE
Acid
Bulky Hydrophore
RECOgnrtES
Ammo WoH Enter
CymasRipsmo ,
Asp 102
Pz This done Aspartic
Acid
Or Aromare Side CHAMS 1 =
zon . Is
By Aspiot
Pi


1.
* 1

And His 57 . THE HIS 57 TAKES SER 195
1
Trp
SERNE
AGz

PHE
A ProTo from SER195-oH THE .
Asp1OT
2 .
AG
~


intermediate
---
,




G E-Pz STABrLtES THE HAS57 And THE SERIE AlkosidE FON CAN ACT As A
3 .
TyR -
.........
V

REACTANTS
for THE of Deparde Bounds
CLEAGE
armen
4
. MET CrazyS y .




products
>


E
EtS ES -
E -

12
Acy1 EntymE INTERMEdNTE MORE V
-

is
TETRAGECRA
Pz
STABLE THAN THE
INTERMEdNATE -




THE Brods THE Substrate forms A INTERMEdrE
CHyMoRySm REACTION MECHANIM : Enzyme As ES , THEN Content W i THE SUBSTREt
Consequently

Depende Bond
Hydrazing
THE The
process product PLIS RELEASEd (FAST) Pe REMANS Bound THE ACTIVE SNE As E-P2 THEN Pe RELEASEd
n . one WARE
TEMPORARiy In . is




from THE ACTIE SME (Slow) ChyMOTRypSN LOWERS ACTMAron
ENERGY
.




=
3
.
His Has 57
PolypEPTNCE SUBSTRATE Brds Don ES A ProTon
.
1
2 . 57 REMOVES A PROTON


o
TO
ENtyME ACTIVE SME from SERISS WHICH Allows To AMNO of Sustrate, o
group
.




157



D
TETRAHEGRAL

oh
Bowd
Resurrogan peptide
A ATTACK INTERMEONE
vocleopHriC By 2

XF
WESTABLE
Meregh stetric

timin
says
: Rz
gen
-
NH
H" m


SN
H ↓
N-
CH - L
c




"
Carbon of peptide Fragment RELEASED As P1 I
CH -
c
N-
CH
-

O
J
G ....
O
G-
It CHz
#
2
CH
-
M N
N

4. 5 HiS DONATES C BEFORE N
WHER ENTERS ACTIVE 57 A
.

PROTON

His 57
SME .
DEPROTONATES TO SER 195 To clEAVE
Acyl- I
HOLE :
Oxyarrow
SER19S - Gly 193
OH A
WATER
RESULTING NTERMEONE
is N TERM.
.

EnzymE .




WCEOPHME ATTACKS CARBONyL RELEASED As P
Is
CATAlyTic
ot
.




it
A
. C TERM
a RELEASED rTRIAG
o REGENERATES n