GPGCM ATD

ROLL NO: 127125

ASSIGNMENT NO: 3
SUBMITTED TO: MAM SHUMAILA
SUBMITTED BY: WAQAR UN NISA
DATE: 16/6/2016

Enzymes:
Enzymes are very efficient catalysts for biochemical reactions. They speed up
reactions by providing an alternative reaction pathway of lower activation energy.
Like all catalysts, enzymes take part in the reaction - that is how they provide an
alternative reaction pathway. But they do not undergo permanent changes and so
remain unchanged at the end of the reaction. They can only alter the rate of
reaction, not the position of the equilibrium.Most chemical catalysts catalyse a wide
range of reactions. They are not usually very selective. In contrast enzymes are
usually highly selective, catalysing specific reactions only. This specificity is due to
the shapes of the enzyme molecules.

Enzyme performance:
An enzymatic reaction is the conversion of one molecule into another; a chemical
reaction catalyzed at the reactive sites on the enzyme. Considering the complex
nature of the enzyme itself, it is not unreasonable to expect that many parameters
will affect the rate of this catalytic activity. Enzyme activity can be influenced by:
Spacing (steric hindrance)
pH
Temperature
Substrate Concentration (Michaelis-Menten Kinetics)

Spacing:
Any groups that separate the enzyme from the support (or backbone) are referred
to as spacing groups. For an enzyme only one spacing group away, it would be very
difficult for a substrate to find the active site. The backbone interferes sterically. But
with more than one CH2 (or other spacing groups), the enzyme can whip around
and twist so that the active site is much more accessible. Usually, spacers that
provide as much distance as six CH2 groups are enough.

Effect of pH Change:
Since enzymes are proteins, they are very sensitive to changes in pH. Each
enzyme has its own optimum range for pH where it will be most active. This is the
result of the effect of pH on a combination of factors: (1) the binding of the enzyme
to substrate, (2) the catalytic activity of the enzyme, (3) the ionization of the
substrate, and (4) the variation of protein structure. The initial rates for many
enzymatic reactions exhibit bell-shaped curves as a function of pH as shown in the

example

below.

Effect of Temperature Change

As temperature increases, the rate of reaction also increases, as
is observed in many chemical reactions. However, the stability of the
protein also decreases due to thermal degradation. Holding the
enzyme at a high enough temperature for a long period of time may
cook the enzyme
Effect of Substrate Concentration
Enzymes are not passive surfaces on which reactions take place
but rather, are complex molecular machines that operate through a
great diversity of chemical mechanisms.
According to MichaelisMenten kinetics, enzyme-substrate reactions are actually comprised of
two elementary reactions. The first is the when the substrate forms a
complex with the enzyme and then in the second, the complex
decomposes to product and enzyme.
k1
k2
Enzyme + Substrate <----> Complex ----> Products +
Enzyme
k-1
According to this model, when the substrate concentration
becomes high enough to entirely convert all of the enzyme to the
complex form, the second step of the reaction becomes the ratelimiting step. Therefore, the overall conversion to product becomes
insensitive to further increases in substrate concentration. The general
expression for the rate of this reaction (velocity) becomes:
v = d[P]/dt = k2*[complex]