ENZYME

By. Yasmine Hadiastriani, S.Si.

 DEFINITION AND CHARACTERISTICS
• Enzyme is a BIOLOGICAL CATALYST to catalyzed substrate and
producing product as the new formed substance
• Enzyme catalyze reaction by speeding up the reaction time and
lowering the ACTIVATION ENERGY
• Enzyme consists of GLOBULAR PROTEIN
• They are SPECIFIC – one enzyme will catalyze one substrate, in
their TERTIARY STRUCTURE
• The site of the reaction occurs in an specific (made up of the same
arrangement of amino acids) area and shape on the surface of the
protein called the ACTIVE SITE.
• Their specificity characteristic based on the LOCK-KEY MODEL and
INDUCED FIT MODEL
• Enzyme has some FACTORS that affecting the rate of enzyme-
catalyzed reactions
 BIOLOGICAL CATALYST
• Catalyst is substance that speeds up a chemical
reaction without being used up in the reaction
itself.
• Enzyme catalyze metabolic reaction in
intracellular (within cells) or extracellular
(outside cells), e.g. blood or digestive system
 ACTIVATION ENERGY
• A certain amount energy needs to be
supplied to the chemicals before the
reaction will start, e.g. heat.
• With the lower amount of activation
energy cause the lower temperature
of the reaction and it will speed up
the rate of reaction
• The lower activation energy happens
because :
1.Enzyme help to hold two substance
close together and it reduce any
repulsion, so those two molecules
can bond more easily.
2.Enzyme help to fit a strain and a
substrate into a bonds in an active
site, so the substrate molecules
break up more easily
 GLOBULAR PROTEIN
• Has molecules that
fold in a spherical 3D
shape, e.g. Insulin,
haemoglobin,
and enzyme
• More or less soluble
• (semi-polar) in
aqueous solution
and physiologically
active
• Involved in metabolic reaction
 SPECIFIC IN TERTIARY STRUCTURE
• Enzyme is very specific – one enzyme for one reaction
• Only one substrate will fit
• The active site’s shape is determined by the enzyme’s
tertiary structure (which is determined by the enzyme’s
primary structure)
• Different enzyme, different tertiary structure, and
different shaped active site
• If the tertiary structure of a protein is altered, it will
change the active site and substrate won’t fit again
• The alter can be pH or temperature
• The primary structure of a protein is determined by a
gene. So, mutation can change the structure of enzyme
 LOCK and KEY MODEL
• Model where the substrate fits into the enzyme in the same way
that a key fits into a lock.

• But scientist find the new evidence showed that the enzyme
substrate complex change shape slightly to complete the fit.
• This locks the substrate more tightly to the enzyme
• This theory known as INDUCED FIT
 INDUCED FIT
• Substrate not only have to be the right shape to
fit the active site, it also makes the active site
change shape
 FACTORS THAT AFFECTING THE RATE OF REACTION
• Temperature
• pH
• Substrate Concentration
• Enzyme Concentration
• Enzyme Inhibitor : molecules that bind to the
enzyme that they inhibit
A. COMPETITIVE INHIBITOR
B. NON-COMPETITIVE INHIBITOR
 COMPETITIVE INHIBITOR
• Have a similar shape to that of
substrate molecules
• Compete with the substrate
molecules to bind to the active
site, but no reaction takes place
• No substrate molecules can fit
in it
• How much the enzyme is
inhibited depends on the
relative concentration of the
inhibitor and substrate
• High concentration of the
inhibitor take up nearly all the
active site
 NON-COMPETITIVE INHIBITOR
• Bind to the enzyme away
from its active site
• It will make the active site
change shape so the
substrate molecules can no
longer bind to it.
• Don’t compete with the
substrate molecules to the
active site
• Increasing the
concentration of substrate
won’t make any difference –
enzyme will still be inhibited
 CLASS DISCUSSION AND PRESENTATION
Find :
1. The effect of temperature on rate of an enzyme catalysed
reaction (other variables controlled) e.g. the catalase
experiment.
2. Carry out an investigation into the effect of pH on rate of an
enzyme catalysed reaction (other variables controlled) e.g.
trypsin digesting protein in a suspension of milk powder
3. Impact of rate of collisions at optimal temperatures, in relation
to concentration of enzyme and substrate at low substrate
concentrations)
4. Hydrogen bonding, tertiary structure, shape of active site and
complementary fit of substrate (e.g. at high temperatures and in
relation to pH)
5. Effect of cofactors and coenzymes in enzyme work