SE *
CLASS
HOTLILy
S = Es E P
Hydrolases
-
E
+
+
-
Use H20 Ligases (join
mostly protein . Transferases
/ mol -
> 2 mol -
1 + 1 -
71
structure
-
release product after rxth
transfer of f(x) group
.
-
-
-
H20 get into molecules -
require energy
substrate
Glycerokinase
S
- eg :
-
active site
- ↓
~ V Oxidoreductase
[
P
from tertiary ?
+
-
quaternary protein . -
-
oxi b reduction .
OXI red Isomerases Lyases
inorganic (ion)
&talticactor
-
02 - -
movement of f(x) gp .
-
+ /-
&
enzyMC
non-protein
xenz or X
+ It t
sis trans
-
- -
coenzyme =
organic (vitamin e- - t
me : Inactive form ON t -
Holoenzyme
/measured
by turnover number/molecular activity
no of substrate >
-
product
-
unit time
Catalytic activity
& Mechanism
& turnover
depends
no varies
on condition
in diff enzyme
(
* Lock key model
reversible
Induced fit
:
-most are
model
Reversibility <eg (X reversible
denatures .
: Grease
Before :
undergo confirmational change
-
S
37 %
⑤
sensitivity/ Opt
temp
becoming complementary
: -
both
Heat
E ↓ activity at ↓ temp
·
& ↑ temp , enzyme
Before
- diff enzyme varies After
:
GE
&
PH sensitivity -
↓/ & pH can disrupt structure
E
1 substrate
substrate
11 rx +h After
Specificity substrate that have similar bond
⑮
Bond
Geometrical & eg : peptide bond
optical cofactor rather
X specific
-
Group- co-factor
L wout cofactor ,
enzyme will not be activate
>
-
↑ s overcomes I
-
compete for
site
active
&
↑
competitive (X)
INHIBITORS As ,
& inhibition of E
↑
mice()
S I = Es
/
- E + S -
E + P
Uncompetitive
+
I
lindnes
E +
SF ES - E
I
reta turnover I
non-competitive (v (
&
·
of
I mentum enzym
I
↑ S to I Rate
S
,
graph :
a E SFES - E P complex
ot
+
burkPlot
+
(C)
I
-
once it bind ,
S
unchanged
ab
1/ Vo Vmax
graph -
S-EN
-
I blocked
ar e
a
-
km & (X-intercept s will be
linewe
El leaving
al/Vo
+
& & [s]
from
-1/Vmax active site
-
:
need
reach V max substrate
rateut
to
> 1/[S] I km
1/km graph ↑ affinity ,
al/Vo > 1/S
timate
1/km
-
competitive
I
-good ?
Reversible -
-
uncompetite
noncompetitive 1Vmax
vmax
it S
- bind strongly to enzym <
// [S]
Irriversible
↓ E+I - El
- to no of active
, nerve covalentbon n Vmaxt() ↓ f(x) enzyme km Ability of substrate
:
site
-
eg : aspirin
one
a to bind to the active site e.
km
pencilin
unchanged substrate
.
-
↳ (X intercept doesn't enzyme substrate
problem to bind
to active site. Affinity :
have
CLASS
HOTLILy
S = Es E P
Hydrolases
-
E
+
+
-
Use H20 Ligases (join
mostly protein . Transferases
/ mol -
> 2 mol -
1 + 1 -
71
structure
-
release product after rxth
transfer of f(x) group
.
-
-
-
H20 get into molecules -
require energy
substrate
Glycerokinase
S
- eg :
-
active site
- ↓
~ V Oxidoreductase
[
P
from tertiary ?
+
-
quaternary protein . -
-
oxi b reduction .
OXI red Isomerases Lyases
inorganic (ion)
&talticactor
-
02 - -
movement of f(x) gp .
-
+ /-
&
enzyMC
non-protein
xenz or X
+ It t
sis trans
-
- -
coenzyme =
organic (vitamin e- - t
me : Inactive form ON t -
Holoenzyme
/measured
by turnover number/molecular activity
no of substrate >
-
product
-
unit time
Catalytic activity
& Mechanism
& turnover
depends
no varies
on condition
in diff enzyme
(
* Lock key model
reversible
Induced fit
:
-most are
model
Reversibility <eg (X reversible
denatures .
: Grease
Before :
undergo confirmational change
-
S
37 %
⑤
sensitivity/ Opt
temp
becoming complementary
: -
both
Heat
E ↓ activity at ↓ temp
·
& ↑ temp , enzyme
Before
- diff enzyme varies After
:
GE
&
PH sensitivity -
↓/ & pH can disrupt structure
E
1 substrate
substrate
11 rx +h After
Specificity substrate that have similar bond
⑮
Bond
Geometrical & eg : peptide bond
optical cofactor rather
X specific
-
Group- co-factor
L wout cofactor ,
enzyme will not be activate
>
-
↑ s overcomes I
-
compete for
site
active
&
↑
competitive (X)
INHIBITORS As ,
& inhibition of E
↑
mice()
S I = Es
/
- E + S -
E + P
Uncompetitive
+
I
lindnes
E +
SF ES - E
I
reta turnover I
non-competitive (v (
&
·
of
I mentum enzym
I
↑ S to I Rate
S
,
graph :
a E SFES - E P complex
ot
+
burkPlot
+
(C)
I
-
once it bind ,
S
unchanged
ab
1/ Vo Vmax
graph -
S-EN
-
I blocked
ar e
a
-
km & (X-intercept s will be
linewe
El leaving
al/Vo
+
& & [s]
from
-1/Vmax active site
-
:
need
reach V max substrate
rateut
to
> 1/[S] I km
1/km graph ↑ affinity ,
al/Vo > 1/S
timate
1/km
-
competitive
I
-good ?
Reversible -
-
uncompetite
noncompetitive 1Vmax
vmax
it S
- bind strongly to enzym <
// [S]
Irriversible
↓ E+I - El
- to no of active
, nerve covalentbon n Vmaxt() ↓ f(x) enzyme km Ability of substrate
:
site
-
eg : aspirin
one
a to bind to the active site e.
km
pencilin
unchanged substrate
.
-
↳ (X intercept doesn't enzyme substrate
problem to bind
to active site. Affinity :
have
