Enzymes C1.1
Metabolism:complex network of interdependent& interacting
chemical reactions occuring in living organisms
(majority being enzyme controlled)
Diffrent
classification chemical
of reactions in living organisms
Anabolic:enzyme bring the substrate molecule together to build a larger
molecule (condensation reactions)
Catabolic:enzyme active site affect
the bonds in substrate
so they break to smaller molecules (hydrolysis reaction
Enzymes:Biological catalyst, speed up metabolic reaction in living
cells being
without used themselves
globular proteins
Enzymes inrecentintheneces
Enzymes globular protein
-> with specifically active site
shaped
determined tertiary structure
by
Enzyme. Substrate specificity
-
Active site have specific shape due to tertiary structure of protein
change in shape of the protein affects shape of activesite & the
-
function the
of enzyme
Denaturation
reasons for denaturation =
S
+ extreme ph
+ extreme heat irriversible change
to a protein
+heavy metal
denaturation ->
destroys the tertiary or quaternary conformation a
of
protein
, minor
->
temperature increase possible
->
reversible denaturation
Enzyme & Temperature
If too
high temp too much vibration
hydrogen bonds
-
-
within the enzymes breaks.
Enzyme & Ph
extreme ph-4 denature enzyme by altering the three dimensional
structure of it's active site
Thermodynamics of Enzymes
-Enzyme reduce the activation energy for a reaction by forming
an enzyme-substrate complex
neededto
Activation
~
of
energy:amount energy a
start reaction
anabolic reaction
+ -the
enzyme holds the substrates close to
one another, reducing repulsion &
allowing
them to bondmore easily
catabolic into the active site
+ reactions -
fitting the substrate
puts strain on the bonds, making them
easier to break
Factors affecting rate of enzyme-catalysedreactions
-Substrate concentration
+
Enzyme Concentration
, How to Caculate rate of Reaction
formed
product or reactant
usedup
Rate of reaction =
time
Metabolic Pathway
+
any chain or cycle of linkedreaction catalysed by enzymes
transformation energy in metabolic 100%
+ of
pathways are never
efficient
Heat
is always lost, warm-bloodedanimals such as mammals &
+
birds use this heat to keep warm & maintain body
constant
temperature
Metabolic of
the amount
organism
neededby that in
rate -
energy
a given time period
Enzyme inhibitions
Competitive inhibition =
- similar shape to substrate
- Bind to active site of enzymes
if
+
the substrate concentration is increased,
will
it reduce the effectof inhibitors
substrate molecules presents the
+..
more
greater the chance finding
of active site,
leaving fewer to be by
occupied the
inhibitors
Non-competitive inhibitors:
+ these inhibitors binds to the
enzyme at a siteway
active site
away from the
+ alters the overall shape the
of enzyme molecules,
including the active site, in such a
way active site
can no
longe accommodate the substrate
+ rate reaction
of unaffectedby substrate
concentration
, End-product
inhibition
In order to control metabolic pathways the end product
-
ofthe pathway
can sometimes inhibitthe activity of the firstenzyme in the pathway
avoids
+
excessive production & buildup intermediate
of chemicals in
a pathway
Inactive precursors
Enzymes
+
are sometimes producedas inactive precursors, this prevents the
enzyme from damaging the cells
precursor
+
removedit
activates & enzymes starts to work
Mechanism-basedinhibition
- irreversible binding of inhibitor to the active site specific
of
enzyme through a covalent bond
creates inhibitor-enzyme complex permanently
>
stable is
enzyme
-
a
+
inactive
Drugs are examples of inhibitors:
+Clarithromycin (antibiotics)
↑
Tamoxifen (antibiotic)
ritonavir
+
(anti-HIV(
Metabolism:complex network of interdependent& interacting
chemical reactions occuring in living organisms
(majority being enzyme controlled)
Diffrent
classification chemical
of reactions in living organisms
Anabolic:enzyme bring the substrate molecule together to build a larger
molecule (condensation reactions)
Catabolic:enzyme active site affect
the bonds in substrate
so they break to smaller molecules (hydrolysis reaction
Enzymes:Biological catalyst, speed up metabolic reaction in living
cells being
without used themselves
globular proteins
Enzymes inrecentintheneces
Enzymes globular protein
-> with specifically active site
shaped
determined tertiary structure
by
Enzyme. Substrate specificity
-
Active site have specific shape due to tertiary structure of protein
change in shape of the protein affects shape of activesite & the
-
function the
of enzyme
Denaturation
reasons for denaturation =
S
+ extreme ph
+ extreme heat irriversible change
to a protein
+heavy metal
denaturation ->
destroys the tertiary or quaternary conformation a
of
protein
, minor
->
temperature increase possible
->
reversible denaturation
Enzyme & Temperature
If too
high temp too much vibration
hydrogen bonds
-
-
within the enzymes breaks.
Enzyme & Ph
extreme ph-4 denature enzyme by altering the three dimensional
structure of it's active site
Thermodynamics of Enzymes
-Enzyme reduce the activation energy for a reaction by forming
an enzyme-substrate complex
neededto
Activation
~
of
energy:amount energy a
start reaction
anabolic reaction
+ -the
enzyme holds the substrates close to
one another, reducing repulsion &
allowing
them to bondmore easily
catabolic into the active site
+ reactions -
fitting the substrate
puts strain on the bonds, making them
easier to break
Factors affecting rate of enzyme-catalysedreactions
-Substrate concentration
+
Enzyme Concentration
, How to Caculate rate of Reaction
formed
product or reactant
usedup
Rate of reaction =
time
Metabolic Pathway
+
any chain or cycle of linkedreaction catalysed by enzymes
transformation energy in metabolic 100%
+ of
pathways are never
efficient
Heat
is always lost, warm-bloodedanimals such as mammals &
+
birds use this heat to keep warm & maintain body
constant
temperature
Metabolic of
the amount
organism
neededby that in
rate -
energy
a given time period
Enzyme inhibitions
Competitive inhibition =
- similar shape to substrate
- Bind to active site of enzymes
if
+
the substrate concentration is increased,
will
it reduce the effectof inhibitors
substrate molecules presents the
+..
more
greater the chance finding
of active site,
leaving fewer to be by
occupied the
inhibitors
Non-competitive inhibitors:
+ these inhibitors binds to the
enzyme at a siteway
active site
away from the
+ alters the overall shape the
of enzyme molecules,
including the active site, in such a
way active site
can no
longe accommodate the substrate
+ rate reaction
of unaffectedby substrate
concentration
, End-product
inhibition
In order to control metabolic pathways the end product
-
ofthe pathway
can sometimes inhibitthe activity of the firstenzyme in the pathway
avoids
+
excessive production & buildup intermediate
of chemicals in
a pathway
Inactive precursors
Enzymes
+
are sometimes producedas inactive precursors, this prevents the
enzyme from damaging the cells
precursor
+
removedit
activates & enzymes starts to work
Mechanism-basedinhibition
- irreversible binding of inhibitor to the active site specific
of
enzyme through a covalent bond
creates inhibitor-enzyme complex permanently
>
stable is
enzyme
-
a
+
inactive
Drugs are examples of inhibitors:
+Clarithromycin (antibiotics)
↑
Tamoxifen (antibiotic)
ritonavir
+
(anti-HIV(
