Class notes

Serine Proteases

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Course
MBB 222 (MBB222)

Institution
Simon Fraser University (SFU )

Condensed class notes for lectures about serine proteases. Mainly focused on Chymotrypsin. Includes substrate binding pockets, chymotrypsin reaction mechanism, and the catalytic triad.

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Uploaded on January 18, 2024
Number of pages 1
Written in 2023/2024
Type Class notes
Professor(s) Dustin king
Contains Class 12 to 13

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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

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