MAURICIO, Krizzia Anne C.

August 10, 2018

CHE 503 – Biochemical Engineering Engr. Sy
HOMEWORK

LOCK AND KEY MODEL VS. INDUCED FIT MODEL

The lock-and-key model and the induced-fit are two potential models for how substrates may bind in
the active site of an enzyme.

The lock-and-key model suggests that the substrate is completely complementary in shape to the
active site, so that it fits in 'perfectly' - i.e. the way a key (the substrate) fits into a lock (the enzyme). Thus
only the correctly shaped key (substrates) opens a particular lock (enzyme). There is no change in shape of
the active site when the substrate binds.

It's important to remember that the induced-fit model is similar to the lock-and-key model, but
tweaked slightly. It says that the substrate and active site are not completely complementary, but there is still
some complementarity. This is like a glove (the enzyme and its active site) and a hand (the substrate) -
they're a similar shape but not an exact match. When the hand goes into the glove, the glove changes shape
slightly and molds itself around the hand so that it fits snugly. In the same way, the active site changes shape
to tightly bind the substrate. At the moment, this model is supported by a lot of evidence. For example, some
enzymes can catalyze reactions with more than one substrate, but these different substrates are still similar
in shape. This is much like how a single glove can fit different hands (as hands are generally similarly
shaped!).
MICHAELIS – MENTEN OR RAPID EQUILIBRIUM APPOACH
The Michaelis-Menten model (1) is the one of the simplest and best-known approaches to enzyme
kinetics. It takes the form of an equation relating reaction velocity to substrate concentration for a system
where a substrate S binds reversibly to an enzyme E to form an enzyme-substrate complex ES, which then
reacts irreversibly to generate a product P and to regenerate the free enzyme E. This system can be
represented schematically as follows:

The Michaelis-Menten equation for this system is:

Here, Vmax represents the maximum velocity achieved by the system, at maximum (saturating)
substrate concentrations. KM (the Michaelis constant; sometimes represented as KS instead) is the substrate
concentration at which the reaction velocity is 50% of the Vmax. [S] is the concentration of the substrate S.

BRIGGS – HALDANE OR QUASI STEADY STATE APPROACH

In 1925, G. E. Briggs and J.B.S. Haldane derives a new interpretation of the enzyme kinetics law
described by Victor Henri in 1903, different from the 1913 Michaelis Menten equation. Leonor Michaelis and
Maud Menten assumed that enzyme (catalyst) and substrate (reactant) are in fast equilibrium with their
complex, which then dissociates to yield product and free enzyme. The Briggs – Haldane equation was of
the same algebraic form, but their derivation is based on the quasi steady state approximation, that is the
concentration(s) of intermediate complex(es) do(es) not change. As a result, the microscopic meaning of the
“Michaelis Constant” (Km) is different. Although commonly referring it as Michaelis – Menten kinetics, most
of the current models actually use the Briggs – Haldane derivation.
SUCRASE – ISOMALTASE
Sucrase – isomaltase is a type of sucrase (enzyme) that converts sucrose hydrolysis into simple
sugars like glucose and fructose. This enzyme is helpful in digesting food. It breaks down the food and
enables the absorption of healthy nutrients. It can also eliminates viruses like gastrointestinal flu viruses and
may also break down particular damaged tissues. These processes enhance tissue growth and reduce
inflammation.
STRUCTURE
Sucrase is the largest identified polypeptide chain successfully translated. It contains more than one
active site, making it multifunctional. Sucrase has 4867 atoms per unit, which includes 558 residues. The
surA gene encodes the information for the sucrase.
METABOLIC PATHWAY
Sucrase has an active site specific to sucrose. Once sucrose enters the enzyme’s active site, the
joint structure is referred to as enzyme substrate complex. The two components undergo a chemical reaction
in which the substrate is broken down, and in this case 2 monosaccharides are produced.

USES
o Detoxifying the body
o Breaking down fats
o Reducing cholesterol
o Losing weight
o Fighting against aging
o Treatment of ulcers
o Natural antiseptic
o Natural immune booster
o Reduces inflammation and thus make people relieved.
3D STRUCTURE
AMINO ACIDS FOUND IN ACTIVE SITE OF SUCRASE – ISOMALTASE

The pink ones are the active site of the enzyme.

The amino acids in the active site of the enzyme
are the following:
o TRP, Tryptophan
o LEU, Leucine
o ASN, Asparagine
o HIS, Histidine
o ASP, Aspartic Acid
o MET, Methionine
o ILE, Isoleucine

ASN328 & ASP355 & TRP327

HIS629 & ASN630

ASP472 & MET473

LEU569 & TRP568

ASP355 & ILE356

LEU393 & ILE392

ILE471 & TRP470