Enzyme Structure
BIOLOGICAL CATALYST that accelerates metabolic reactions
Enrymes are all tertiary globular proteins
Each engine has its unique sequence of amino acids
plastto
Ghagest
breakdown
the structures are held together with hydrogen bonds ionic bonds Sdisulphide bridges
They reduce the activation energy needed for a chemical reaction to
take place
They are ANABOLIC Engines bring substrate molecules together
canalso be CATABOLIC weaker bonds in substratesbreak it down
All have a uniqueSspecificactive site
Usually specific to only one reaction
When a reaction involving an euryme areas a substrate is turned into a product
the active site of an enzyme is complementary to the substrate it catalyses
Examples ATP ase break downof ATP into ADP producing energy
Lactose breaks down lactose into glucose Sgalactose
ENZYME WORKING MODELS
Lock and key model
This is a hypothesis of how engines catalyse substrate reactions
It states that theactive site of engines are exactly complimentary te the shape of the substrate
When a substrate molecule collides with an engine whos active site shape is complimentary the substrat
will fit intothe active site
This willform an Enryme substrate Complex
The engine will catalyse the reaction S the products together with the enzyme forms Euryme
product compies
TfReactions may possibly be
revirsible
Induced fit Hypothesis
, Induced El Hypotheses
this is more recent model backed evidence and is
a upby widely accepted by everyone
it sneaks thatthe shapeofactive sites are notexactly complimentary but changeshape inthe presence of a
b become complimentary
specific substrate
when a substrate molecule couides with an anyone if its composition is specifically correct
the shape of the eurymes active site will change so the substrate fits into
it
The R groupspointing out ofthe active site form interactions with the
substrate molecule
An engine substrate complex is formed
when the product leaves the enzyme the active site reverts back to its
inactive state
FACTORS AFFECTING ENZYMES
Concentration
of Enryme
i
As the concentration
of the engine is increasedthevelocity of the reaction proportionately
increases
This is because it means that more substrates can be catalysed at once
concentration
of Substrate
The rate of enzymatic reaction increases as substrate concentration increases
until a limiting rate is reached after which further increase produces no
significant change in the rate of reaction
this is when an engine molecules are saturated with substrate the excess substrate
cannot react until the products leave the complex
Temperature
The nature
f to
of energies makes them extremely sensitive thermal charges
Each engine has a certain optimum temperature that differs depending on
the organism
In manuals the optimum temperature is usually between 37 400
Effect of PH
BIOLOGICAL CATALYST that accelerates metabolic reactions
Enrymes are all tertiary globular proteins
Each engine has its unique sequence of amino acids
plastto
Ghagest
breakdown
the structures are held together with hydrogen bonds ionic bonds Sdisulphide bridges
They reduce the activation energy needed for a chemical reaction to
take place
They are ANABOLIC Engines bring substrate molecules together
canalso be CATABOLIC weaker bonds in substratesbreak it down
All have a uniqueSspecificactive site
Usually specific to only one reaction
When a reaction involving an euryme areas a substrate is turned into a product
the active site of an enzyme is complementary to the substrate it catalyses
Examples ATP ase break downof ATP into ADP producing energy
Lactose breaks down lactose into glucose Sgalactose
ENZYME WORKING MODELS
Lock and key model
This is a hypothesis of how engines catalyse substrate reactions
It states that theactive site of engines are exactly complimentary te the shape of the substrate
When a substrate molecule collides with an engine whos active site shape is complimentary the substrat
will fit intothe active site
This willform an Enryme substrate Complex
The engine will catalyse the reaction S the products together with the enzyme forms Euryme
product compies
TfReactions may possibly be
revirsible
Induced fit Hypothesis
, Induced El Hypotheses
this is more recent model backed evidence and is
a upby widely accepted by everyone
it sneaks thatthe shapeofactive sites are notexactly complimentary but changeshape inthe presence of a
b become complimentary
specific substrate
when a substrate molecule couides with an anyone if its composition is specifically correct
the shape of the eurymes active site will change so the substrate fits into
it
The R groupspointing out ofthe active site form interactions with the
substrate molecule
An engine substrate complex is formed
when the product leaves the enzyme the active site reverts back to its
inactive state
FACTORS AFFECTING ENZYMES
Concentration
of Enryme
i
As the concentration
of the engine is increasedthevelocity of the reaction proportionately
increases
This is because it means that more substrates can be catalysed at once
concentration
of Substrate
The rate of enzymatic reaction increases as substrate concentration increases
until a limiting rate is reached after which further increase produces no
significant change in the rate of reaction
this is when an engine molecules are saturated with substrate the excess substrate
cannot react until the products leave the complex
Temperature
The nature
f to
of energies makes them extremely sensitive thermal charges
Each engine has a certain optimum temperature that differs depending on
the organism
In manuals the optimum temperature is usually between 37 400
Effect of PH
