BIOCHEMISTRY  

Instructor: LE HONG PHU  

Date of submission: September 28, 2022 

HOMEWORK 4  

Student's Information: 
Name  ID Student 

Mai Lê Chí Bảo  BTBTWE21068

Every day I go to the university, every day I receive different and extremely useful knowledge.
And the subject of Biochemistry is not an exception, the knowledge is very complicated but
equally attractive to the students of the International University. One of the 3 things that
impressed me most in the Biochemistry class was: The structure of Enzymes, Coenzymes, and
especially the question about the specific difference between functional foods and drugs.

What impressed me most was none other than the interestingness and complexity of the
enzyme's structure and mechanism of action. Regarding the structure of the enzyme, one of the
most indispensable parts of the enzyme is the active site. Regarding the active site, it is only
very small in size compared to the total area. Professor Phu told us that "If the active site is
present then everything will remain, and if the active site disappears there will not be any
possible reaction". The active site is found in the tertiary structure and for this reason, there are
many different types of chemical bonds found in it. In addition, it also has a cleft and this cleft
plays a very important role in the formation of the structure and function of the active site.
Imagine if its structure was not a cleft but a surface structure, what would happen? The
possibility of being affected by external factors such as the environment will be very high. And if
they are designed in cleft form, it will be one of the favorable conditions for the substrate to
enter to create a micro-field, so that the substrate will be in the best state and the reactions will
take place in a great condition. Based on the importance of the active site, Professor Phu gave
us an extremely difficult question "Why do we need several hundred or even many amino acids
to create an enzyme containing an active site that is very small?". Based on the importance of
the active site, Professor Phu gave us an extremely difficult question "Why do we need several
hundred or even many amino acids to create an enzyme containing an active site of the same
size? very small" We spent a lot of time thinking about the answer to this question. He then
explained that to be able to harmonize, they need a complex structure to be flexible in all
different environmental conditions. And although they have repair mechanisms, they will not be
able to correct 100% of errors and the presence of hundreds of amino acids plays a very
important role in internal and external protection. Furthermore, the substrate will attach to the
enzyme by weak bonds. The question is "Why don't they link with just one strong link but need a
lot of weak links?". The answer is very simple that they cannot depend on just one strong link, it
needs many weak links. The substrate will be bound to the enzyme through the Induce Fit
mechanism. At the high school or middle school levels, this mechanism is called another name,
"Locks and Keys". However, this name will not fully show how Induce Fit works. One thing that
we need to keep in mind is that the Active site and substrate are compatible but not exactly the
same. It means that when the enzymes and substrate meet together, there is a shift in the
enzyme’s structure to suit the substrate and maximize the enzyme’s ability. Right after that, our
teaching assistant in the class that day introduced us to the allosteric site. And she gave us a
very interesting question, which is "How do allosteric sites affect the active site?" The answer is
when an allosteric inhibitor binds to an enzyme, all active sites on the protein subunits change
slightly such that they bind their substrates with less efficiency. It will change according to the
type of chain (in other words, it will change in different spaces).

The second thing that I felt very impressed in the class that day was the knowledge about
Coenzyme and Cofactor. First, we were introduced to zymogen - which is a pro-enzyme. The
precursor of the enzymes can't be active. They need the change in biochemistry to become
activated. The activation can be self-regulated or by some protease. Hydrolysis reaction will cut
one or some bonding at the end -N of zymogen to activate the zymogen. This cutting process
will take place in the tertiary structure. Right after that, the teaching assistant provided us with
knowledge about coenzymes and cofactors. Many enzymes can work individually if they do not
bound to the other specific non-protein helper molecules. In contrast, if they cannot bind to the
ionic or hydrogen bonds or stronger covalent bonds, they are often called Co-enzymes and
Cofactors. When they bind to the helper molecules, they can promote the function of the
respective enzymes. Cofactors are inorganic ions such as iron (Fe ++) and magnesium (Mg ++).
They play an important role in building DNA polymerase because this process needs Zn ++ to
function. Coenzymes are organic helper molecules. The source of coenzymes is dietary
vitamins. Some coenzymes can be seen as coenzymes and can act directly as coenzymes.
Depending on the type of coenzyme that plays a different role in the reaction. There are 2 types:
Used for redox and Transport of functional groups. 

What impressed me in the Biochemistry class was the question of how to distinguish the
difference between drugs and supplements. And why when we go to the doctor and get a
prescription from the doctor, that prescription always comes with different vitamins? This
question was asked by Professor Phu at the beginning of the lesson, but the time to find out for
the seemingly simple question was very long. But the answer will become very simple after we
learn through the Enzyme lesson today. As we all know, the source of coenzymes is from
everyday vitamins like vitamin A, vitamin B1, vitamin B2, etc. And in the presence of
coenzymes, it will act as a catalyst for the highest enzyme activity so that the drug's functions
will be maximized. From this information, we can distinguish between functional foods or
supplements and drugs easily. This is an extremely interesting question because it combines
the knowledge in the lesson and practical applications in the life of each person. From that, we
can see that the relationship between science and daily life is extremely close.