catalyst speeds : Intracellular
Enzymes : COFACTORS :
be present
up the rate a reaction each metabolic
pathway substance that has to to ensure
·
*
in
withoutbeing
active
used a a
series 2
living cell is
consecutive
one a2 that an
enzyme catalysed reaction takes
covalent
place
permanently bound by bonds
·
-
reactions -
enzyme-subtrate complex enzyme and :
⑳
· -
substrate ·
various reactants < subtrate
-
intermediates act as
molecules bind
together temporarily
.
subtrates for specific
enzymes. LOCK < KEY COENZYMES :
L reactants < intermediates and small non-protein
organic
·
·
⑳ ·
enzyme products are known as that bind
metabolites.
molecules temporarily
to the active site & enzyme
* product : Molecule produced ·
each catabolic (metabolic molecule s
from an
enzyme catalysed pathway) are broken down.
Enzyme Enzy me ·
chemically changed during
reaction . ·
anabolic (other pathways subtrate product the reaction
* metabolism : chemical reactions
.
use
energy to synthesise complex complex need to be
recycled into
cells .
that takes place in
larger molecules. their
original states
·
Active site is complemen tay
Active site : to the subtrate molecule .
·
consists of a few amino acids.
is crucial INDUCED FIT
tertiary
↳ structure active site not
is a
rigid
·
altered temprature structure
↳ can be
by ⑳
DH in the presence 2 the
⑧ ⑤
·
denatured 4
I
optimum 2 .
sustrate it induces
>
-
·
its
M
moud
ENZYMES itself -
shape. to
Active still
Lowering
Activation
·
site
the
has a
subtrate
complementary
molecule .
to the
snape 2
-
8 Energy
- - - - - -
·
subtle
changes of side chains (R-groups) 2 the
acids
-
n
with out amino .
" ----------enzymes bonds attractions van der was
ionic
& ·
with
·
Hydrogen
<
,
interactions bind the
S
temprature ------------enzymes forces
subtrate
hydrophobic
the active site.
to
-
Extracellular V
E + S - E P
Enzymes maltose ESC EPC
: + +
B
· > >
-
enzymes secreted the from
CONCENTRATION
celld where
They are made giucose
&
SUBTRATE
and act on their subtracte reaction INHIBITORS if subtrate concentration is
!
n enzym
nation
-
increased rate will increase .
*
competitive inhibitors : inhibitor E S ,
ii
5 is limiting
Temprature :
enzyme is Molecule has similar snape to
a factor Fixed concentration
denatured that of the subtrate molecule. and 2 enzy me concentration
&
sustrate
for the active site. Blocks is no
longer limiting factor
>
- competes
the active site. S
* non-competitive inhibition competitor concentration of enzyme
:
Molecule attaches to an more cule
(not active site)
enzyme POISONS MEDICAL DRUGS
rate-time
1 which
changes snape
-
take to reach end pita site (no inhibits aerobic
of the active longer complementary Cyanide :
respiration
·
.
.
Venom inhibits
:
acetylcholinesterase .
·
&
·
Aspirin prevents formation
:
of prostaglandis.
Qo = rate of reaction at (T + 10) ATPase Inhibitors : cardiac
·
glycosides .
rate of reaction at ToC . ·
ACE inhibitors : inhibit antigotensin .
Enzymes : COFACTORS :
be present
up the rate a reaction each metabolic
pathway substance that has to to ensure
·
*
in
withoutbeing
active
used a a
series 2
living cell is
consecutive
one a2 that an
enzyme catalysed reaction takes
covalent
place
permanently bound by bonds
·
-
reactions -
enzyme-subtrate complex enzyme and :
⑳
· -
substrate ·
various reactants < subtrate
-
intermediates act as
molecules bind
together temporarily
.
subtrates for specific
enzymes. LOCK < KEY COENZYMES :
L reactants < intermediates and small non-protein
organic
·
·
⑳ ·
enzyme products are known as that bind
metabolites.
molecules temporarily
to the active site & enzyme
* product : Molecule produced ·
each catabolic (metabolic molecule s
from an
enzyme catalysed pathway) are broken down.
Enzyme Enzy me ·
chemically changed during
reaction . ·
anabolic (other pathways subtrate product the reaction
* metabolism : chemical reactions
.
use
energy to synthesise complex complex need to be
recycled into
cells .
that takes place in
larger molecules. their
original states
·
Active site is complemen tay
Active site : to the subtrate molecule .
·
consists of a few amino acids.
is crucial INDUCED FIT
tertiary
↳ structure active site not
is a
rigid
·
altered temprature structure
↳ can be
by ⑳
DH in the presence 2 the
⑧ ⑤
·
denatured 4
I
optimum 2 .
sustrate it induces
>
-
·
its
M
moud
ENZYMES itself -
shape. to
Active still
Lowering
Activation
·
site
the
has a
subtrate
complementary
molecule .
to the
snape 2
-
8 Energy
- - - - - -
·
subtle
changes of side chains (R-groups) 2 the
acids
-
n
with out amino .
" ----------enzymes bonds attractions van der was
ionic
& ·
with
·
Hydrogen
<
,
interactions bind the
S
temprature ------------enzymes forces
subtrate
hydrophobic
the active site.
to
-
Extracellular V
E + S - E P
Enzymes maltose ESC EPC
: + +
B
· > >
-
enzymes secreted the from
CONCENTRATION
celld where
They are made giucose
&
SUBTRATE
and act on their subtracte reaction INHIBITORS if subtrate concentration is
!
n enzym
nation
-
increased rate will increase .
*
competitive inhibitors : inhibitor E S ,
ii
5 is limiting
Temprature :
enzyme is Molecule has similar snape to
a factor Fixed concentration
denatured that of the subtrate molecule. and 2 enzy me concentration
&
sustrate
for the active site. Blocks is no
longer limiting factor
>
- competes
the active site. S
* non-competitive inhibition competitor concentration of enzyme
:
Molecule attaches to an more cule
(not active site)
enzyme POISONS MEDICAL DRUGS
rate-time
1 which
changes snape
-
take to reach end pita site (no inhibits aerobic
of the active longer complementary Cyanide :
respiration
·
.
.
Venom inhibits
:
acetylcholinesterase .
·
&
·
Aspirin prevents formation
:
of prostaglandis.
Qo = rate of reaction at (T + 10) ATPase Inhibitors : cardiac
·
glycosides .
rate of reaction at ToC . ·
ACE inhibitors : inhibit antigotensin .
