what are
Ezylog
?
or enzymes
,
enzymes
d ↳ specialised proteins
&
-
Biocatalysts ↳ speed up the chemical reaction
Zu ↑ ↳largely predominate in
What is a
catalyst ? 2 inorganic
ions
of that
increase/decrease
Marietyatalysts
② catalyst The rate of reaction
but not all catals in
are
enzymes .
V
Differences Catalyst
Enzyme
-
#
&
-
I . -
organic
in nature Based on -Inorganic in nature
2.
High molecular notchemical low Molecular weight
-
-
Nature metal ions
gobular proteins
.
3 - Are "proteins" - Are Metal Ions/ enzyme
4 There
. are a types : Based on There are a types
1. Activationenzymes types
. 1 . Positive catalysts
2 .
Inhibitory enzymes .
2 Negative catalysts
.
.Gives
5 faster late of Based on
Gives slower rate of
reaction . Rate of R
. reaction
aged .
-largely remain
. Enzymes need
6 optimum Based on Catalysts do not need
temp pH soll
:
, they temperature any
,
optimum temp ph ,
are
specialised proteins PH came are stable at all
tery
S
.
,
act diff.
enence work
,
easily
PH .
(highes/lawer).
i e
.
secific denatures Anything !!I
.
7
Enzymes are more Based on Catalysts are less
specific specificity
.
specific comp. to enzym
, O catalysts
similarity of
enzymes
↓
⑧samsuddtiene
Both are not consumed in the
estion ?? entire course of reaction .
Approve / Disapprove :
1
II
All are
protein in
enzymes nature
No ,
I
disapprove
, Not "All" enzymes are
protein in nature
,
There's an
exception :
Ribozymes a made of
up
RNA
An consists of 2
portions parts /
enzyme
.
-
Apenzyme cofactor/coenzyme
-
↓
-
↓
-
d organic part
of non-protein
protein part I is
part a A is derived
from
↓ enzyme
an
metal ion
V
Vitamins"
My 44tca2+
+
But is an catalytic +
inactive portion . 2n
Wi no cofactor att to it
.
Agloenzyme what makes an catalytic enzyme
the way
,
↳
Catalytic active enz. it is ?
↳ makes the
i
.
capable of converting
e Presence of cofactor enzyme
the substrate to prod catalytic active . N
sout of an requirement for
a bounded
cofactors
&
catalytic active
.
to it
.
Move about cofactors
types
--
: Are vitamins ORGANIC IN ORGANIC
in nature
Vitamin B complex
6Coenzymes ↓ ↓
metalions
eg : Riboflavin
2/ help of &
These
coenzymes/lofactors are fightly bound
enzyme (Apoenzyme)
to the are are
COVALENTING termed as "Prosthetic groups"
, &
co-substrate is the one cofactor
A
Inon-protein
+
Apoenzyme
(protein part)
i. e not
rightly bounded to part) H
MOLOENZYME
·
the
enzyme
.
Lactive enzyme)
&
DIEF UNIIS TO MEASURE ENZYE
S ACTIVITY us rate of conversion of
-
substrate to
product
Enzymes
.
:
International Unit (IV] are biomassess -> The
change in
S helps us to
their levels (as
umol/min understand they are
protein)
↓ what's next to
Amt of
enzyme that catalyses come .
I mol of
the conversion of
substrate
per min under
->
Revised -
Kata
- a
katal of
I enzyme
Optimum conditions (pH temp
, ,
con!
activity converts (mol of
substrate per second .
1 IV 16 6 7 n katal i nmol/s
to
we know =
.
&
.
e
= 16 . 67
· 2I0=2x10 67 .
n Katal
= 43 34 .
n Katal
/
Activity Turnover number
Specific - -
of of substrate molecules
->
Activity an
enzyme per -> no
converted
mg of an total protein
. to
product per
↓ .
second
Units : mol of substrate converted
Inactive form of an
zymogen :
into product per min/mg enzyme
similar
under optimum condition
:
pepsinogen
d chymotrypsinogen .
: . mol of substrate/min/mg
impo d
↳
use
Ezylog
?
or enzymes
,
enzymes
d ↳ specialised proteins
&
-
Biocatalysts ↳ speed up the chemical reaction
Zu ↑ ↳largely predominate in
What is a
catalyst ? 2 inorganic
ions
of that
increase/decrease
Marietyatalysts
② catalyst The rate of reaction
but not all catals in
are
enzymes .
V
Differences Catalyst
Enzyme
-
#
&
-
I . -
organic
in nature Based on -Inorganic in nature
2.
High molecular notchemical low Molecular weight
-
-
Nature metal ions
gobular proteins
.
3 - Are "proteins" - Are Metal Ions/ enzyme
4 There
. are a types : Based on There are a types
1. Activationenzymes types
. 1 . Positive catalysts
2 .
Inhibitory enzymes .
2 Negative catalysts
.
.Gives
5 faster late of Based on
Gives slower rate of
reaction . Rate of R
. reaction
aged .
-largely remain
. Enzymes need
6 optimum Based on Catalysts do not need
temp pH soll
:
, they temperature any
,
optimum temp ph ,
are
specialised proteins PH came are stable at all
tery
S
.
,
act diff.
enence work
,
easily
PH .
(highes/lawer).
i e
.
secific denatures Anything !!I
.
7
Enzymes are more Based on Catalysts are less
specific specificity
.
specific comp. to enzym
, O catalysts
similarity of
enzymes
↓
⑧samsuddtiene
Both are not consumed in the
estion ?? entire course of reaction .
Approve / Disapprove :
1
II
All are
protein in
enzymes nature
No ,
I
disapprove
, Not "All" enzymes are
protein in nature
,
There's an
exception :
Ribozymes a made of
up
RNA
An consists of 2
portions parts /
enzyme
.
-
Apenzyme cofactor/coenzyme
-
↓
-
↓
-
d organic part
of non-protein
protein part I is
part a A is derived
from
↓ enzyme
an
metal ion
V
Vitamins"
My 44tca2+
+
But is an catalytic +
inactive portion . 2n
Wi no cofactor att to it
.
Agloenzyme what makes an catalytic enzyme
the way
,
↳
Catalytic active enz. it is ?
↳ makes the
i
.
capable of converting
e Presence of cofactor enzyme
the substrate to prod catalytic active . N
sout of an requirement for
a bounded
cofactors
&
catalytic active
.
to it
.
Move about cofactors
types
--
: Are vitamins ORGANIC IN ORGANIC
in nature
Vitamin B complex
6Coenzymes ↓ ↓
metalions
eg : Riboflavin
2/ help of &
These
coenzymes/lofactors are fightly bound
enzyme (Apoenzyme)
to the are are
COVALENTING termed as "Prosthetic groups"
, &
co-substrate is the one cofactor
A
Inon-protein
+
Apoenzyme
(protein part)
i. e not
rightly bounded to part) H
MOLOENZYME
·
the
enzyme
.
Lactive enzyme)
&
DIEF UNIIS TO MEASURE ENZYE
S ACTIVITY us rate of conversion of
-
substrate to
product
Enzymes
.
:
International Unit (IV] are biomassess -> The
change in
S helps us to
their levels (as
umol/min understand they are
protein)
↓ what's next to
Amt of
enzyme that catalyses come .
I mol of
the conversion of
substrate
per min under
->
Revised -
Kata
- a
katal of
I enzyme
Optimum conditions (pH temp
, ,
con!
activity converts (mol of
substrate per second .
1 IV 16 6 7 n katal i nmol/s
to
we know =
.
&
.
e
= 16 . 67
· 2I0=2x10 67 .
n Katal
= 43 34 .
n Katal
/
Activity Turnover number
Specific - -
of of substrate molecules
->
Activity an
enzyme per -> no
converted
mg of an total protein
. to
product per
↓ .
second
Units : mol of substrate converted
Inactive form of an
zymogen :
into product per min/mg enzyme
similar
under optimum condition
:
pepsinogen
d chymotrypsinogen .
: . mol of substrate/min/mg
impo d
↳
use
