|
  |

] Greatly increase the rate of reaction

] Catalyse at milder condition
] Are highly specific, only catalyse one particular
reaction
] Reaction takes place at active site where its shape
matches substrate¶s shape
] Active sites recognize and hold substrate in place
] Nature of R-groups of amino acid located at the active
site determines the enzyme¶s specificity
] Remain unchanged at the end of reaction, can be
reused
Enzymes speed up reaction by
providing an alternative route of
lower activation energy.

More molecules possess

sufficient energy to overcome
activation energy (minimum energy
required for a reaction to occur)
 aock-and-Key Model
½
 



 
  
(a) Temperature
VAt low T, molecules have low kinetic
E, they do not collide frequently & do
not posses minimum activation E, rate
of reaction is very low
Vaocks and keys are complementary
structures; VAs T increases(0-40C), molecules
Vthe enzyme is highly specific have increasing kinetic E, frequency of
VOnly 1 substrate fits into the active site at collision increase, more molecules
once have energy greater than activation
energy, rate of reaction increase

VAs T increase further(40C-..),

thermal motion of polypeptide chain
causing disruption of the force
maintaining shape of enzyme, shape
of active site change, enzyme is
denatured, rate of reaction decrease
(b) pH


  
Extremes of pH will denature
enzyme by disrupting precise 3D
structure of the protein chain
Even small changes around neutral
pH can affect ionization of amino acid
side-chains in the active site
Each enzyme has its own distinct
optimum pH value:
]Pepsin works in acidic condition
]Amylase works in neutral pH
]Trypsin works in alkaline condition
g

Vaoss of biochemical activity through
structural change
VDenaturation destroys enzyme irreversibly
VIsolated enzyme extracted from tissue can
be denatured by changes in chemical
condition.
‡high [salt] disrupt ionic interaction btw
different region of the chain
‡urea disrupt hydrogen bonds
VChemical inhibitors inactivate enzyme
‡DFP : reagent that binds to serine
residue in enzyme to show importance of
serine in the active site ; function as
nerve gas
 Enzyme Inhibition
What is inhibitors?
Small molecules that bind to enzyme and reduce the rate of enzyme
reaction.
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 Cofactors
Non-protein group that is necessary for the enzyme to function as catalysts.
Without the cofactors, no enzyme activity will occur.
They must present to for the enzyme to work .

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