BIOCHEMISTRY  

Instructor: LE HONG PHU  

Date of submission: September 6, 2022 

HOMEWORK 1  

Student's Information: 
Name  ID Student 

Mai Lê Chí Bảo  BTBTWE21068

TOPIC: 3 significant lessons that you can learn from the classes (31/8/22)
Homework: 
The first day that I became a sophomore was one of the most important events of my life. No
longer are those feelings of anxiety and nervousness of 1st-year students and not the busy feeling
of final-year students. For me, this is an extremely indescribable and truly unforgettable feeling.
As a person who loves science and coincidentally, my first day of school started with
Biochemistry. In class, I have the opportunity to expose a lot of new knowledge and more
specifically, there are 3 things that impressed me the most. The magic of Maslow's Hierarchy of
Needs, the logic of Bloom's taxonomy, and the true purpose of learning will be detailed in the
next paragraphs.

Perhaps Maslow's model is too familiar to everyone and especially those who learn about science
and psychology. Each person's needs will be different and Maslow's model was created with the
aim of generalizing those needs into specific areas. I still remember that in that class, Professor
Phu asked everyone a very special question "What are your needs". I was quite impressed with
that question because it will never have a specific and exact answer. And yes, the answers of the
students, including me, are different and very unique. Some of the students are interested in
knowledge, some are interested in health and some are interested in their beauty. After a series of
answers, he showed us the Maslow model and said that cognitive human needs are one of the
most common and important factors. And this step also plays an important role in distinguishing
between growth needs and deficiency needs. I was impressed with Professor Phu’s explanation
of this model. After we have passed the stages of basic needs, we will gradually think about
taking care and developing ourselves. And that is also the reason for the appearance of demand
groups like aesthetic needs, self-actualization, and transcendence. 

In addition, the logic of Bloom's taxonomy is the second thing that makes me feel very
impressed in this class. Through Professor Phu’s teachings, I realized that it is considered as a
scale of educational goals and is extremely widely used in the world, especially those related to
the field of education. The teacher explained to us at each level, what skills we will need to use
on this scale. Specifically, at the university level, we need to masterly apply 3 skills:
remembering, understanding, and applying. Applied skills are the skills that our students need to
pay the most attention to. We can remember and understand knowledge, but somehow, we have
to apply it in our daily lives to produce positive results. Professor Phu gave a very unique and
authentic example of the fact that Singapore has flourished under the hands of Ly Hien Long.
Moreover, Korea and Japan are the two strongest industries in Asia because they have applied
the knowledge they have learned to daily life and turned it into a huge advantage. Next,
Professor Phu also introduced to us that if students want to study well at the Master's level, they
must master 2 skills, respectively, analysis and evaluation. Professor Phu also gave an impressive
example to make students feel more clearly about these skills. That's an example of evaluating a
remote, he showed us the difference between the same remote when we look at it from different
angles. Each perspective will bring us a different analysis and evaluation. Furthermore, Professor
Phu introduced us to one of the indispensable skills of a PhD student, which is creativity.
Continuous creativity and innovation are important factors in the development of life and the
country. 

The final thing that makes me feel exceedingly impressed is the true purpose of the study. What
do we learn for? Why do we have to learn? And what are the learning outcomes? Various
questions are asked by Professor Phu and the response to these questions is a series of answers
from students. He also showed us four UNESCO standards for learning: To Know, To Do, To
Be, and To Live Together. Like the part mentioned above, it is extremely important to know and
understand something deeply, but having to apply those things in life to bring about real benefits
is a challenge. It won't make any meaning if we understand something but can't apply it to our
lives. Professor Phu also asked the challenge question “Which are the most important learning
outcomes: Knowledge, Skills, or Attitudes”. Perhaps this is an open-ended question and will not
have a specific answer. Some argue that knowledge and skills are extremely important if you
want to be successful. But others think that attitude outweighs skill. To increase the authenticity,
my teacher showed us recent surveys and the numbers helped us get a better view of this difficult
question. Through Professor Phu’s explanations, I realize what is my true purpose in learning
and why I have to learn very hard. Besides, Professor Phu also showed that the university
environment is not only a place to study and research but also a place for us to comprehensively
develop ourselves through sports activities, clubs, learning new languages, or even improving
our computer skills

To conclude, this is an unforgettable day in my life because in this day I not only have the
opportunity to interact with new knowledge but also learn valuable lessons from my lecturer -
Professor Le Hong Phu.

     BIOCHEMISTRY  
 Instructor: LE HONG PHU  

Date of submission: September 12, 2022 

HOMEWORK 2  

Student's Information: 
Name  ID Student 

Mai Lê Chí Bảo  BTBTWE21068

TOPIC: 3 significant lessons that you can learn from the classes (07/09/22)
Hw: 
Biochemistry is always one of the subjects that gives me a great feeling and excitement every
time I study. This course takes place every Wednesday and coincidentally it is also my first class
of the week. Every time I come to class, I am impressed by the enthusiasm of the lecturer, the
interest in the lesson, and so on. And last Wednesday was no exception, I was impressed with 3
main things: the photo in the opening slide of the first lesson, and the scientific process. These 3
things will be detailed in the paragraphs below. 

The first is about the related picture on the first slide and is also a general picture that represents
what I will learn and explore in the upcoming lessons. Based on this photo, the teacher asked us
an interesting question that was "What is most special when you look at this photo". There are
many answers given by the students. Each student has a different and very specific answer. Some
people think that this is an energy conversion process, and some people think that this is a
normal photosynthetic cycle. I really like questions like these because we will never find the
most precise and perfect answer to this interesting question. After a series of answers from the
students, the teacher also explained to us about this photo. Professor Phu said that this is really a
very comprehensive and general biological system. I was really impressed with the two terms
that he mentioned when explaining this picture: Open System and Closed System. This image is
an open system and also works on the principle of openness. He gave us many examples to help
us understand the definition of this word better, and one of the examples that I remember the
most is the system in the human body. And the second question that I am really impressed with
is whether the factors present in the image exist completely independently or not. The answer
made the students, including me, very surprised. It does not exist as a dependent and does not
exist as an independent, but it exists in a relatively independent form. This means that the
product of one will be the input of the other. And all have a dependent relationship or in other
words, if there is one, the other will exist. This process takes place within the cell and is highly
uniform in both structure and function. They complement each other very closely

In addition, Professor Phu also introduced us to a very new concept that is the scientific process.
This stems from a lesson in intellectual skills. Whenever we encounter a problem that is very
difficult to solve, we should not give up, but go find the most correct and scientific answer.
Professor Phu reminded us that the action that is always associated with the scientific process is
observation. After observing, we will have different ways of thinking to answer the same
question. And in order to choose the most correct and comprehensive way of thinking, the next
step that the teacher guided us is to perform the test. Accompanying those tests are the methods
and these tests will be carried out in the form of outdoor or indoor depending on the nature of
each type. After performing the tests under the right conditions, we will get the results. There
will be some correct results and some false results. I was impressed here because most of the
students would stop here and use the results to write science-related articles. But Professor Phu
reminded us that it is not enough and we need to repeat the test at least 3 times to make sure that
the final result we use is the most perfect and accurate result. In addition, Professor Phu also
gave a very specific example to help us better visualize the scientific process. Professor Phu gave
the example of Edison - one of the geniuses of world science. Professor Phu said that Edison did
the experiment wrong 9999 times and for the 10000th time he succeeded in his experiment with
extraordinary perseverance and effort. Through Professor Phu’s example, I have learned a lesson
that false results are not something we should ignore and throw away. Take it as a lesson and try
for the next time, be persistent and keep trying. 

And the last thing that impressed me the most in the class on 9/9/22 was the knowledge we must
have at the end of this course and with it the course description. Professor Phu told us that the
two most important parts of this course are the Enzyme section and the Metabolism section. We
need to remember, understand, and apply the knowledge in practice. Professor Phu reminded us
that a huge amount of knowledge will emerge. And we understand that it will be difficult to
remember them all. Knowing this, Professor Phu suggested to us an extremely effective learning
method that is to memorize important keywords and especially to carefully remember the
principles of enzymes and in the process of metabolism. He emphasized that principles are the
key to all problems. Although there are many different variations in operation and
implementation, in general, they still follow a pre-established principle. 

Above are 3 things that I was really impressed with when studying Biochemistry on September
7th. And really, today's class has given me a lot of valuable knowledge lessons and I very
appreciate when learning this lesson.

BIOCHEMISTRY  

Instructor: LE HONG PHU  

 Date of submission: September 20, 2022 

                                                             HOMEWORK 3  

Student's Information: 
Name  ID Student 

Mai Lê Chí Bảo  BTBTWE21068

TOPIC: 3 significant lessons that you can learn from the classes and explain the statement
“Enzyme has complex structure so it can be regulated” (14/9/22)
Hw: 
Every day when I go to the university, I receive extremely useful and interesting knowledge
lessons and today is no exception. I learned about enzymes - one of the most important things
that happen in the living world. There are 3 things that impressed me about today's class: the
overview of enzymes, the origin of enzymes and the processes in which enzymes are present. All
of them will be detailed in the paragraphs below. In addition, I will also explain the question
"Why do enzymes need complex structures to be able to regulate easily?"

As for the overview of enzymes, we will first have to answer the “Wh questions” such as What,
Where, Why, What for, and so on. With these questions, we can easily determine what enzymes
are, their special properties and even what functions they have. Then I was surprised when
Professor Phu asked, "Are enzymes a form of helper molecules?". This question was
immediately answered by the students that helper molecules include coenzymes, cofactors and
these are considered friends of enzymes. When talking about something in chemistry or biology,
we will always refer to its structure because the structure will play an important role in
determining its function. And this is no exception with enzymes, Mr. Phu asked us about the
special structure of enzymes. The answer is given a lot by the students, but in conclusion, the
main structure of the enzyme will include active site, allosteric site, allosteric activators
(positive), allosteric inhibitors (negative), and allosteric binding sites. Furthermore, one question
type that is no less important than the “Wh question” is the question that begins with the word
“How”. How do enzymes work? What is the working mechanism of enzymes in different
reactions? And these things will be explored in detail later in the lesson. Next, as we know
enzymes are extremely diverse and there will be many different types. Therefore, enzymes'
classification and classification criteria will also be extremely important. In addition, the role of
enzymes as biological catalysts in reactions will also be explored through their kinetic energy in
different reactions where enzymes are present. Enzymes are so perfect, what applications will
they have in reactions in particular and the life of humans and organisms in general. This will be
answered through questions that begin with "what for?". Imagine what would happen if one day
the enzyme disappeared from our body and it would no longer exist in the living world. From
there we can recognize and draw conclusions about the importance of enzymes. 
The second thing that I can learn in today's class is the diversity of enzyme origins. It can appear
anywhere and at any level of the body. In this section, Professor Phu gave us a small activity in
class that is which each student will have 5 minutes to find out the name of the enzyme and its
origin. After 5 minutes, the students had many different and different answers for themselves
such as protease from bovine and pancreas, pepsin from the porcine stomach, etc. However, the
enzymes that students described all have one thing in common, which is that they all appear in
organs. However, the origin of enzymes is much more diverse, they not only occur at the organ
level, but they are also found at the organelles and cellular levels such as the enzyme catalase
found in peroxisomes, rubisco found in chloroplasts, and other enzymes found in mitochondria.
In addition, Professor Phu further informed us that enzymes can also appear and be found on
membranes. And enzymes like these are called immobilized enzymes. In addition, it is also
called an embedded protein but its essence is still an enzyme. Besides, Professor Phu also
introduced us to a very special way of working of enzymes that is, enzymes are born inside, but
the main place of enzyme activity is outside. And from this, we can conclude that there are two
types of enzymes: endogenous and exogenous. Through the knowledge presented above, we can
draw a simple conclusion that: Where there is a living world, there will be enzymes. In the air
there will also be enzymes because the air has dust particles, those dust particles will have a lot
of microorganisms on it and enzymes are also found a lot from different microorganisms.

The third thing I learned in class on 9/14/22 is about the processes that enzymes can be involved
in. As mentioned above, enzymes will appear anywhere as long as there is a living world. The
processes that our bodies perform every day are the breathing process, also known as the
respiratory process. This process requires the presence and catalysis of enzymes. For a long time,
we have always wondered how cells will interact with each other. And it wouldn't be too
surprising to say that cells interact with each other with the help of enzymes. They will create a
large amount of energy source ATP and this energy source plays an extremely important and
indispensable role in the processes taking place in the human body. Thus, the enzyme acts as a
biological agent in low-temperature reactions and after the reaction, it will still retain its catalytic
properties. In addition, most enzymes are derived from proteins and a few are derived from
RNA. 

In the next section, I will explain why the more complex the enzyme, the easier it is to regulate.
As we all know most enzymes are of protein origin. And the hierarchical structure of the protein
answers this question. In the primary structure, amino acids are linked together via peptide bonds
and form a polypeptide chain. This is followed by a secondary structure, which contains not only
peptide bonds, but where the hydrogen bonds form between the oxygen atom in the carbonyl
group in one amino acid and another amino acid which is four amino acids farther along the
chain. After completing the secondary structure, the tertiary structure gradually began to be
revealed. Parallel to the formation of tertiary structure is the formation of bonds. In addition to
the indispensable presence of hydrogen bonds, there are also contributions of hydrophobic
interactions, weak bonds such as ionic bonds, and disulfide linkages. The final structure of the
protein is the quaternary structure. In the quaternary structure, all the types of bonds mentioned
in the primary, secondary, and tertiary structures are present in the quaternary structure. There is
also a very important link which is the van der Waals interaction. When proteins reach the
quaternary structure, they are now considered an enzyme. With the complete quaternary
structure, we can conclude that the enzyme has an extremely complex structure. And with such a
complex structure, when enzymes exist in different environments, they will be able to
dynamically change shape to match the temperature and pH conditions that the environment
requires. Therefore, through the above reasons, we can conclude that “Enzyme has the complex
structures so it can be regulated”
      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. 

     BIOCHEMISTRY  

Instructor: LE HONG PHU  

Date of submission: October 5, 2022 

HOMEWORK 5  
Student's Information: 
Name  ID Student 

Mai Lê Chí Bảo  BTBTWE21068

Biochemistry is always one of the subjects that gives me not only valuable lessons and
knowledge but also a source of energy for me every week. In every Biochemistry class, we learn
many things and 28/09/22 was no exception. I was impressed with 3 things: the source of the
enzyme, the variety of different enzymes, and the last thing that impressed me was the diversity
and specificity of the oxidoreductase subclasses.

At first, I was impressed with the diverse source of enzymes. As we all know, enzymes are very
widely distributed in nature and the 3 sources where we can find enzymes most easily are
animals, plants, and microorganisms. And to help us understand the lesson better, Professor Phu
gave us some time to find and think about where enzymes can be found in animals, plants, and
microorganisms. And after thinking for a while, there were many different answers given by the
students and all of them were correct. And I am no exception, I have prepared myself with very
specific answers. For example, animal sources are mainly from the pancreas, liver, and porcine.
Furthermore, the application of these sources is concerning to the digestive system. Especially,
alkaline phosphatase can be used in diagnostic. The sources from plants are mainly applied in
anti-inflammatory agents. And periodase can be used in diagnostics. The sources from microbes
are mainly applied in breaking down something or degrading something. Especially, alcohol
dehydrogenase can be used in diagnosis and L-asparaginase can be used in Leukemia treatment.
Through this knowledge, I understand more deeply that enzymes are extremely diverse in nature
and in our daily lives.

The next part is the one that I think is the most important, which is the classification of enzymes.
Because of the diversity of enzymes, they will also have many types carrying different functions.
Since this is one of the most important parts of the enzyme, Professor Phu advised us to
memorize this part carefully. At that time, Professor Phu gave us 5 minutes to memorize all the
names of 5 different groups of enzymes: Oxidoreductase, Transferase, Lyases, Isomerases, and
Ligases. And after that 5 minutes, Professor Phu randomly called a student to be able to test that
student's ability to remember the different enzymes mentioned above. Not only stopping at
memorization but remembering in order is extremely necessary and important. We are required
to remember them in a certain order, not in an unsystematic way.

As mentioned above, enzymes are extremely diverse and are classified into many different
groups such as Oxidoreductases, Transferase, Lyases, Isomerases, and Ligases. And if we take a
closer look, there are many different enzymes in Oxidoreductase. In general, the enzyme
Oxidoreductase is involved in catalyzing oxidation-reduction reactions. There are 2 components,
containing the co-enzyme such as NAD+, NADP+, FAD, and FMN. And along with that are 4
subclasses in this type of enzyme: Dehydrogenase, Reductase, Oxygenase, and Peroxidase. Let's
start with Dehydrogenase, they take part in the reaction that H+ from the substrate is transferred
to the oxidized coenzyme such as NAD+; NADP+, FAD, and FMN. It is for this reason that they
can easily occur in the glycolysis or CAC (Krebs cycle). In addition, they also took part in the
reverse reaction that H+ from reduced co-enzyme (NADH; NADPH, FADH2, FMNH2) is
transferred to the substrate. And they can easily occur in the synthesis reactions. Furthermore,
they have a wide range of applications, such as in the production of wine and beer through the
alcohol dehydrogenase reaction. They can also help nitrogen transfer from the soil to the plant
and this can help the plant absorb it further. They also help microorganisms absorb NH3. Next,
we learned about the enzyme reductase. They can catalyze the reaction in which electrons can be
transferred to oxygen. So, oxygen can have the ability to combine with protons. The third
enzyme in the oxidoreductase family is Oxygenase. They play an important role in taking part in
the oxidation reaction in which oxygen can combine with the substrate to become a part of
functional groups such as OH; COOH. The last of the Oxidoreductases that I learned about is
Peroxidase. There are 2 main types: Peroxidase and Catalase. They also include co-enzyme:
HEM. Peroxidase also catalyzes the oxidation reactions of organic molecules with the presence
of H2O2. 

Today's lesson has helped me better understand the importance and diversity of enzymes in life.
The 3 things that I learned in this lesson are invaluable sources of knowledge that cannot be
replaced

BIOCHEMISTRY

Instructor: LE HONG PHU

Date of submission: October 12, 2022

HOMEWORK 6

Student's Information: 
Name  ID Student 

Mai Lê Chí Bảo  BTBTWE21068

TOPIC: The significant lessons that you can learn from the classes (05/10/22)
Hw: 
Enzymes are one of our important lessons this semester 1. Towards the end, the amount of
knowledge as well as the lesson will increase in difficulty. And last Wednesday was also a very
special and important day because we learned one of the most difficult parts of enzymes which is
kinetics.

In my opinion, Kinetics has always been one of the most challenging things to visualize because
it is so abstract. We always ask ourselves what is kinetics and how it will play an important role
in our body. More specifically, what is the profound relationship between kinetics and enzymes,
and does that relationship have a major influence on most biochemical reactions? Because this is
one of the extremely difficult parts of the Enzyme chapter, Professor Phu has given many
examples to help students easily imagine and understand. After a series of examples about
biochemical reactions and the effect of rate factors on biochemical reactions, Professor Phu
helped us understand how Kinetics is defined. We can derive basic kinetic properties such as the
study of kinetics focuses on the speeds of chemical processes. Furthermore, thermodynamics
may be used to determine whether a reaction will happen spontaneously for any system that is
responding. The reaction's kinetics show how quickly it actually proceeds. As mentioned in
previous lessons, most biochemical reactions take place at the cellular level of living organisms.
Moreover, the enzyme acts as a catalyst that can help the reaction achieve the highest efficiency.
And we also remember that catalysts significantly speed up a reaction's pace while maintaining
equilibrium.

Going deeper into the lesson, what impressed and overwhelmed me was the complexity of the
formulas. It is very flexibly modified from the original formula and to form each such formula
requires a lot of complicated experiments to be performed. One of the formulas that Professor
Phu introduced and explained very carefully to our class is the “Michaelis-Menten equation”. 

In this formula, we will focus mainly on 2 main quantities, which are Vmax and KM. When the
substrate has saturated all enzyme sites, the maximum reaction velocity, or Vmax, is attained.
This will occur when [S] >> KM, bringing [S]/([S] + KM]) closer to 1. Moreover, KM is equal
to the substrate concentration at which the reaction rate is half its maximum value. In other
words, if an enzyme has a small value of KM, it achieves its maximum catalytic efficiency at
low substrate concentrations. Thus, the smaller the value of KM, the more efficient is the
catalyst. The value of KM for an enzyme depends on the particular substrate. It also depends on
the pH of the solution and the temperature at which the reaction is carried out. For most
enzymes, KM lies between 10^-1 and 10^-7 M.

This is really one of the lessons that I find difficult and highly challenging. This is a lesson that
plays an extremely important role in the Enzyme chapter in particular and semester 1 in general.
The formulas used for the calculations are extremely complicated and the mechanics of the
increase and decrease are very complex and this makes me even more excited to learn more
about these things.

BIOCHEMISTRY  

Instructor: LE HONG PHU  

Date of submission: October 19, 2022 

HOMEWORK 7  

Student's Information: 
Name  ID Student 

Mai Lê Chí Bảo  BTBTWE21068

Biochemistry is a highly diverse subject in terms of knowledge. It will include all biochemical
reactions occurring in the human body in particular and the species in general. Indeed, on
Wednesday (October 12, 222) we were introduced to a whole new chapter, no longer about
catalyzed reactions or enzyme applications but rather about metabolism processes in the body of
people. 

Since the knowledge of this metabolic chapter is so vast and varied, we were asked in the first
session only to be able to distinguish between catabolism and anabolism. Also, we need to
understand how to control a complete pathway. To distinguish between anabolism and
catabolism, we first need to understand the definition of metabolism. There are many different
definitions but we just need to remember that metabolism is a process of chemical changes that
convert nutrients into energy and the complex finished products of cells. Next, Professor Phu
told us about the function of metabolism. We had to answer a simple question that plays an
important role in metabolism: "Where does the energy that metabolism needs come from?".
After a series of answers given by students, Professor Phu concluded that sunlight and fuel
molecules are the two main energy sources of metabolism. In addition, metabolism has another
extremely important function in the body, which is converting nutrients into the precursor of cell
components. In addition, metabolism is capable of synthesizing energy-using precursors into
cellular components. Once we can clearly understand the definition and what is metabolism, this
is the stepping stone to the classification of metabolic processes that will become easier to
remember. Metabolism is divided into two main processes: catabolism and anabolism. Professor
Phu reminded us that students often make a mistake when distinguishing and comparing these
two processes. Because of this, it is very important to know the knowledge of each process.
Next, we will go into details of each process and the first is the process of catabolism. To
facilitate the process of memorization I have listed a few bullet points and these bullet points will
cover the main contents of the catabolism process.
  Catabolism: Degradative 
 Oxidative 
 Many → Few 
 Degradative pathways 
 Saving energy. 
 Decomposition of large molecules into lots of small molecules 
Along with the process of catabolism, the process of anabolism also plays a very important role.
And just like above, to facilitate memorization, I also used bullet points. 
 Anabolism: Biosynthetic 
 Reductive 
 Few → Large 
 Biosynthetic pathways
 Enrergy requirement. 
 Large molecules will be synthesized by lots of small molecules 
Next, Professor Phu showed us a diagram of the biochemical reactions that take place directly in
our human body. The number of reactions occurring is extremely large and has a very close
relationship with each other. The relationships between reactions are represented by a straight
line connecting the reactions. It is because of this that Professor Phu compared this diagram to a
complex electrical circuit that students of the Department of Electronics and
Telecommunications often learn. Through the diagram that Professor Phu showed us, we can
make the observation that acetyl CoA is at the heart of many different biochemical reactions.
And one of the main routes is from the Glycogen -> CAC cycle. Next, we learned about
substances that play an important role in metabolism. One of the indispensable things is ATP,
which is considered as an energy currency in most reactions. In addition, NADPH and NADH
are the two substances that we were acquainted with in the Enzyme chapter, which also play a
very important role in this metabolism. For example, NADH (related to form drugs) and NADPH
(related to lipids). 

In the later part of the class, we studied with the teacher's assistant sister. The part we studied
involved quite a lot of calculations and this part was extremely difficult so it required us to
concentrate. First, we are reminded of the definition and importance of Km. It has a very close
relationship to the place where it exists. For example, the low Km: the mitochondrial form, and
high Km: the cytoplasmic form. Next, we have to answer a question that is also considered a
challenge which is "What happens to enzyme activity if the normal concentration of substrate
changes". A series of answers were given by the students and in the end, the main answer was:
 Changing a little substrate concentration, it is also very sensitive, but it still has little
activity.
 Its activity is very high but it will not be sensitive.
 Activity and sensitivity are both at a sufficient level.
Moreover, we are introduced to different applicable formulas, and we also have the opportunity
to apply those formulas to solve problems.

The class that day was extremely interesting but equally challenging for math and formulas.
However, I feel that this is an interesting subject and the knowledge is very closely linked from
chapter to chapter.
 BIOCHEMISTRY  

Instructor: LE HONG PHU  

Date of submission: November 16, 2022 

HOMEWORK 8  

Student's Information: 
Name  ID Student 

Mai Lê Chí Bảo  BTBTWE21068

Biochemistry is a subject that is not only extremely interesting but also very important because
its knowledge can not only be read in books but can also be applied to our daily lives in general
and our bodies in particular. There are so many different reactions and processes going on in our
body every second, every hour and every day. And among them glycolysis is one of the
processes I learned in Biochemistry class last Wednesday. So what is Glycolysis? The answer í
that Glycolysis is the process by which glucose is broken down to provide energy is known as
glycolysis. It generates two pyruvate molecules, ATP, NADH, and water. There is no need for
oxygen throughout the process, which occurs in the cytoplasm of a cell. Both aerobic and
anaerobic creatures experience it. The first stage of cellular respiration, which takes place in all
organisms, is called glycolysis. The Krebs cycle comes after glycolysis during aerobic
respiration. Small amounts of ATP are produced by the cells in the absence of oxygen as
fermentation follows glycolysis. Next, we will move to the pathway of glycolysis. The glycolysis
pathway occurs in the following stages:

Stage 1:

- Hexokinase, an enzyme, adds a phosphate group to glucose in the cytoplasm of the cell.
- This involves the transfer of a phosphate group from ATP to glucose to create glucose,6-
phosphate.

Stage 2:
The enzyme phosphoglucomutase isomerizes glucose-6-phosphate into fructose,6-phosphate..

Stage 3:
The other ATP molecule uses the enzyme phosphofructokinase to transform fructose 6-
phosphate into fructose 1,6-bisphosphate by adding a phosphate group to it.
Stage 4:

Fructose 1,6-bisphosphate is transformed by the enzyme aldolase into the isomers

glyceraldehyde 3-phosphate and dihydroxyacetone phosphate.
Stage 5:

Dihydroxyacetone phosphate is transformed into glyceraldehyde 3-phosphate by triose-

phosphate isomerase, which serves as the substrate for the following stage of glycolysis.

Stage 6:
This step undergoes two reactions:

• The glyceraldehyde 3-phosphate dehydrogenase enzyme converts nicotinamide adenine

dinucleotide to NADH + H+ by transferring one hydrogen molecule from glyceraldehyde
phosphate.

• To create 1,3-bisphosphoglycerate, glyceraldehyde 3-phosphate dehydrogenase adds a

phosphate to the oxidized glyceraldehyde phosphate.

Stage 7:

With the aid of phosphoglycerokinase, phosphate is transferred from 1,3-bisphosphoglycerate to

ADP to create ATP. At the conclusion of this reaction, two molecules each of phosphoglycerate
and ATP are produced.

Stage 8:

The enzyme phosphoglyceromutase moves the phosphate of both phosphoglycerate molecules

from the third to the second carbon to produce two molecules of 2-phosphoglycerate.

Stage 9:

To create phosphoenolpyruvate, the enzyme enolase takes a water molecule out of 2-

phosphoglycerate.

Stage 10:

Pyruvate kinase transfers a phosphate from phosphoenolpyruvate to ADP to produce pyruvate

and ATP. The final products are two molecules of pyruvate and ATP.

Hence, we can conclude about the key Points of Glycolysis

• It is the procedure by which a glucose molecule is split into two pyruvate molecules.
• Animal and plant cells' cytoplasms are where the process occurs.
• The process involves six enzymes.
• The reaction produces two molecules of pyruvate, two of ATP, and two of NADH.
 BIOCHEMISTRY  

Instructor: LE HONG PHU  

Date of submission: November 23, 2022 

HOMEWORK 9  

Student's Information: 
Name  ID Student 

Mai Lê Chí Bảo  BTBTWE21068

TOPIC: The significant lessons that you can learn from the classes
CAC is a fundamental metabolic pathway as well as the most important metabolic pathway for
energy supply to the body. CAC operates under aerobic condition only and oxidizes 2 carbons
Acetyl group in Acetyl CoA and Carbon dioxide. CAC also produces reduced Coenzyme
NADH, FADH2, ATP. CAC occurs in the mitochondria matrix. This is the second step in
aerobic cellular respiration.
The series of chemical reactions used by all aerobic organisms to generate:
a. Energy through the oxidation of Acetate (derived from carbohydrates, fats and proteins).
b. Chemical energy in the form of ATP
Pyruvate produced in cytoplasm enter mitochondrial matrix. Pyruvate is converted into acetyl
coA by pyruvate hydrogenase complex. Pyruvate hydrogenase complex consists of 3 enzymes
and 5 coenzymes.
Step 1: Acetyl CoA + Oxaloacetate Citrate
- Enzyme: Citrate synthase
- Oxaloacetate bind to the enzyme citrate synthase Acetyl coA binds to the enzyme Acetyl coA
is enolized Changed acetyl coA binds to oxaloacetate, Citryl CoA is formed Citryl-coA is
separated into citrate and coA.
Step 2:
- Enzyme catalyze: Aconitate
- Aconitate active cluster [Fe4S4] 2+ converts to inactive form [Fe3S4] + One H2O molecule is
removed from citrate Formation of cis-Aconitate The inactive form change to active form One
water molecule is added to cis-Aconitate Isocitrate is formed
Step 3:
- Enzyme catalyze: Isocitrate dehydrogenase
- NAD+ is reduced to NADH, oxidation of isocitrate creates oxalosuccinate The decarboxylation
of oxalosuccinate produces α-Ketoglutarate and CO2
Step 4:
- Enzyme catalyze: α-Ketoglutorase dehydrogenase
- Decarboxylation of α-Ketoglutarate Reduction of NAD+ to NADH CoA binds to the
subsequence Succinyl CoA
Step 5:
- Enzyme catalyze: Succinyl coA synthetase
- Phosphate displace CoA from bound succinyl-CoA molecule Phosphoryl group transfers to His
residue of enzyme Succinate released Phosphoryl group transferred to GDP (or ADP)
Step 6:
- Enzyme catalyze: Succinate dehydrogenase
- Oxidization of Succinate, Reduction of FAD
Step 7:
- Enzyme catalyze: Furmarase
- Trans addition of water to the double bond of Fumarate.
Step 8:
- Enzyme catalyze: Malate dehydrogenase
- Malate is oxidized to form Oxaloacetate
Fatty Acids:
When a cell’s metabolic needs increase, free fatty acids enter the mitochondrion where the
degradative reactions called b oxidation. A fatty acid shortened by two carbon atoms plus a free
acetyl-CoA molecule results from each round of b oxidation. Acetyl-CoA initiates the citric acid
cycle.
Amino Acids
The remaining carbon skeleton is broken down to acetyl-CoA or to pyruvate, which is then
converted to acetyl-CoA. Alternatively, a citric acid cycle intermediate such as a-ketoglutarate
may result. In all cases, the citric acid cycle plays a large role in breaking down the amino acid
skeleton to carbon dioxide. For example, catabolism of lysine yields carbon dioxide and acetyl-
CoA, while glutamate breaks down to a-ketoglutarate, carbon dioxide, and acetyl-CoA. Acetyl-
CoA initiates the citric acid cycle.
Monosaccharides
In the cytosol, glucose is broken down to two, 3-carbon molecules during glycolysis. The
resulting three-carbon molecules are called pyruvate. Pyruvate is transported across the
mitochondrial membrane where it is broken down to a 2-carbon compound called acetyl - CoA
plus carbon dioxide. Acetyl-CoA initiates the citric acid cycle

     BIOCHEMISTRY  

Instructor: LE HONG PHU  

Date of submission: November 30, 2022 

HOMEWORK 10  

Student's Information: 
Name  ID Student 

Mai Lê Chí Bảo  BTBTWE21068

Oxidative phosphorylation is the process in which ATP is formed as a result of the transfer of
electrons from NADH or FADH2 to O2 by a series of electron carriers. This process takes place
in the mitochondria inner membrane in eukaryotes and in the cytoplasm in prokaryotes.
Electron transport chain is used for extracting energy from sunlight (photosynthesis) and from
redox reactions such as the oxidation of sugar (respiration). The electron transport chain shuttles
electrons down a series of redox reactions that release energy used to make ATP. Creation of an
electrochemical proton gradient over the inner mitochondrial membrane, which powers oxidative
phosphorylation. The NADH and FADH2 formed in glycolysis, fatty acid oxidation, and the
citric acid cycle are energy-rich molecules because having a high transfer potential. When these
electrons are used to reduce molecular oxygen to water, a large amount of free energy is
liberated, which can be used to generate ATP. The citric acid cycle is a series of redox and
decarboxylation reactions that remove high-energy electrons and carbon dioxide. The electrons
temporarily stored in molecules of NADH and FADH2 are used to generate ATP. We can see
these reactions thorough these formulas below
• NADH → NAD+ + H+ + 2 e-
• FADH2 → FAD + 2 H+ + 2 e-
The need of human beings for the optimal functions of the oxidative phosphorylation:
Almost all aerobic organisms (organisms that require oxygen to live) including humans use
oxidative phosphorylation, in one way or another, to produce the basic energy currency of the
cell needs to function: ATP (adenosine triphosphate). Oxidative phosphorylation is the fourth
step of cellular respiration and produces most of the energy in cellular respiration.
For example, glycolysis produced 2 molecules of pyruvate and 2 ATPs; the TCA cycle produces
2 ATPs from two acetyl-CoA molecules.
On the other hand, oxidative phosphorylation generates about 30-34 ATPs; which accounts for
more than 80% of ATPs that are formed when glucose is completely oxidized to CO2 and H2O
What would happen if the oxidative phosphorylation would not work properly?
If oxidative phosphorylation will not work properly then, protons will not be pumped outside and
electrons won't flow into the cell, resulting in concentration gradient generation. In the absence
of a concentration gradient, ATP production will be inhibited. For example, antimycin A can
inhibit succinate - cytochrome c reductase in the electron transport chain to block NADH
oxidation & ATP synthesis.
Defective oxidative phosphorylation functions result in disease. MItochondrial diseases are the
most common form of inherited metabolic disorders. The pathophysiology of mitochondrial
diseases is complex and involves genetic mutations in mtDNA or DNA. Patients with mtDNA
mutations can often lead to a mixture of mutated and wild-type genomes, called heteroplasmy.
Mitochondrial diseases can also involve any organ or tissue and characteristically involve
multiple systems, typically affecting organs that are highly dependent on aerobic metabolism and
are often relentlessly progressive with high morbidity and mortality.

     BIOCHEMISTRY  

Instructor: LE HONG PHU  

Date of submission: December 7, 2022 

HOMEWORK 11  

Student's Information: 
Name  ID Student 

Mai Lê Chí Bảo  BTBTWE21068

The pentose phosphate pathway (also called the phosphogluconate pathway and the hexose
monophosphate shunt) is a metabolic pathway parallel to glycolysis. It generates NADPH and
pentoses (5 - carbon sugars) as well as ribose 5-phosphate, a precursor for the synthesis of
nucleotides.
There are two distinct phases in the pathway. The first is the oxidative phase, in which NADPH
is generated, and the second is the non-oxidative synthesis of 5-carbon sugars.
Oxidative phase:
Oxidation is the breakdown of a molecule as it loses at least one of its electrons. This phase is
made up of 2 irreversible steps:
- Glucose-6-phosphate is oxidized to form lactone. NADPH is produced as a byproduct of this
reaction as NADP+ is reduced as glucose-6-phosphate is oxidized. Following the oxidation of
glucose-6-phosphate, another reaction, catalyzed by a different enzyme, uses water to form 6-
phosphogluconate, the linear product.
NADPH is similar in structure and function to the high energy electron shuttle, NADH,
mentioned in the cellular respiration articles. NADPH has an added phosphate group and is used
in the cell to donate its electrons, just like NADH. Once NADPH has donated its electrons it is
said to be oxidized (oxidation = loss of electrons) and is now symbolized as, NADP+. NADPH is
often used in reactions that build molecules and occurs in a high concentration in the cell so that
it is readily available for these types of reactions.
- Next, a carbon is removed (cleaved) and CO2 is released. Once again, the electrons released
from this cleavage is used to reduce NADP+ to NADPH. This new 5-carbon molecule is called
ribulose-5- phosphate.
The overall reaction for this process is:
Glucose 6-phosphate + 2 NADP+ + H2O ribulose 5-phosphate + 2 NADPH + 2 H+ + CO2
Non-oxidative phase:
The non-oxidative phase is really handy because these reactions are reversible. This allows
different molecules to enter the pentose phosphate pathway in different areas of the non-
oxidative phase and be transformed up until the first molecule of the non-oxidative phase
(ribulose-5-phosphate). Ribulose-5- phosphate is the precursor to the sugar that makes up DNA
and RNA, and is also a product of the oxidative stage.
- Ribulose-5-phosphate can be converted into two different 5-carbon molecules. One is the sugar
used to make up DNA and RNA called, ribose-5-phosphate and this is the molecule we will
focus on. Ribulose - 5-phosphate isn’t being divided because the carbon count is the same in the
next step.
- The rest of the cycle is now made up of different options that depend on the cell’s needs. The
ribose - 5-phosphate from step 3 is combined with another molecule of ribose-5-phosphate to
make one, 10-carbon molecule. Excess ribose-5-phosphate, which may not be needed for
nucleotide biosynthesis, is converted into other sugars that can be used by the cell for
metabolism.
The 10-carbon molecule is interconverted to create a 3-carbon molecule and a 7-carbon
molecule. The 3-carbon product can be shipped over to glycolysis if it needs. That being said,
recall that we can also work our way back up to another molecule in this phase. So that 3-carbon
molecule could also be shipped over from glycolysis and transformed into ribose-5-phosphate for
DNA and RNA production.
- The 3-carbon molecule and the 7-carbon molecule, from the interconversion above in step 4,
interconvert again to make a new 4-carbon molecule and 6-carbon molecule. The 4-carbon
molecule is a precursor for amino acids, while the 6-carbon molecule can be used in glycolysis.
The same reversal of steps in option 4 can happen here as well.
The pentose phosphate pathway takes place in the cytosol of the cell, the same location as
glycolysis. The two most important products from this process are the ribose-5-phosphate sugar
used to make DNA and RNA, and the NADPH molecules which help with building other
molecules.

   

  BIOCHEMISTRY  

Instructor: LE HONG PHU  

Date of submission: December 14, 2022 

HOMEWORK 12  

Student's Information: 
Name  ID Student 

Mai Lê Chí Bảo  BTBTWE21068

In humans the main gluconeogenic precursors lactate, glycerol, alanine and glutamine.
Lactate produced by active skeletal muscle and erythrocytes. Erythrocytes lack mitochondria and
can never oxidize glucose completely. In contracting skeletal muscle, the rate at which glycolysis
produces pyruvate exceeds the rate at which the citric acid cycle oxidizes it. Under these
conditions, moreover, the rate of formation of NADH by glycolysis is greater than the rate of its
oxidation by aerobic metabolism.
The accumulation of both NADH and pyruvate is reversed by lactate dehydrogenase, which
oxidizes NADH to NAD+ as it reduces pyruvate to lactate. However, lactate is a dead end in
metabolism. It must be converted back into pyruvate before it can be metabolized.
The only purpose of the reduction of pyruvate to lactate is to regenerate NAD+ so that glycolysis
can proceed in active skeletal muscle and erythrocytes. The formation of lactate buys time and
shifts part of the metabolic burden from muscle to other organs. Lactate and pyruvate both are
substances diffuse out of active skeletal muscle into the blood and are carried to the liver. Much
more lactate than pyruvate is transported out because the high NADH/NAD+ ratio in contracting
skeletal muscle favors the conversion of pyruvate into lactate. The lactate that enters the liver is
oxidized to pyruvate. Pyruvate in the liver is converted into glucose by the gluconeogenic
pathway. Glucose then enters the blood and is taken up by skeletal muscle.
Thus, the liver furnishes glucose to contracting skeletal muscle, which derives ATP from the
glycolytic conversion of glucose into lactate. Contracting skeletal muscle supplies lactate to the
liver, which uses it to synthesize glucose

   

  BIOCHEMISTRY  

Instructor: LE HONG PHU  

Date of submission: December 21, 2022 

HOMEWORK 13  

Student's Information: 
Name  ID Student 

Mai Lê Chí Bảo  BTBTWE21068

Glycogenesis
1) Synthesis of UDP-glucose
* UDP-glucose: an activated form of glucose and the building block for glycogen synthesis and
glycogenolysis
* Process
- Glucokinase converts glucose + ATP → glucose-6-P + ADP
- Phosphoglucomutase (an isomerase) converts glucose-6-P → glucose-1-P
- UDP-glucose pyrophosphorylase converts glucose-1-P + UTP → UDP-glucose + PPi
(pyrophosphate)
2) Initial chain formation
Glycogen
An enzyme comprised of a homodimer protein that is at the core of each glycogen unit and is the
starting point of glycogen synthesis
Catalyzes the formation of short glycogen chains by polymerizing a few UDP-glucose molecules
3) Chain elongation
Glycogen synthase
- A key regulatory enzyme that binds UDP-glucose molecules to the growing glycogen chain
- Catalyzes the formation of α-1,4-glycosidic bonds between UDP-glucose and the hydroxyl
group of the C4 atom at the free end of the glycogen chain
4) Branching of glycogen chains
Branching enzyme: an enzyme with glucosyltransferase activity that introduces branches to the
glycogen chain to allow for further chain elongation at multiple sites within the glycogen
complex
- Catalyzes the formation of α-1,6-glycosidic bonds: hydrolyzes a chain of 6 glucose units off the
original chain → attachment of molecules to C6 atom of another glucose unit within the original
chain
- Branches are introduced at least 4 glucose units apart from one another.
Glycogenolysis
1) Release of glucose
* Cleavage of α-1,4-glycosidic bonds: glycogen phosphorylase (cofactor vitamin B6) cleaves off
glucose-1-P; through a phosphoric reaction until 4 terminal glucose residues remain on a branch
(referred to as limit dextrin).
* Cleavage of α-1,6-glycosidic bonds
- Debranching enzymes: an enzyme that has glycosyltransferase as well as glucosidase activity
+ First step: glycosyltransferase; (or 4-α-D-glucanotransferase): transfers 3 out of the 4
remaining glucose residues of the branch to a nearby branch
+ Second step: glucosidase (or amylo-α-1,6-glucosidase): cleaves off remaining glucose unit
(alpha-1,6 linkage) from the branch; through a hydrolytic reaction → release of
nonphosphorylated, free glucose molecules and a linear chain of glycogen
2) Glucose utilization
After glycogenolysis, the phosphoglucomutase (isomerase) transducers glucose-1-P into glucose
6-P
- In muscle
+ The instant metabolization of glucose-6-P during exercise (glycolysis)
+ Hexokinase: converts free glucose to glucose-6-P
- In liver: Glucose-6-phosphatase: glucose-6-P → free glucose → release into systemic
circulation → increase in serum glucose levels
Regulation related to insulin, glucagon & epinephrine (adrenalin).
Insulin
Insulin is an anabolic peptide hormone that is produced and secreted from β cells located in the
islets of Langerhans of the pancreas. By modulating glucose absorption from the blood, insulin
lowers blood glucose levels. Further important metabolic functions of insulin include the
promotion of carbohydrate, amino acid, and fat storage in the liver, skeletal muscle, and adipose
tissues. There are several insulin analogues (e.g., insulin glargine) with a different molecular
structure but similar properties to human insulin, with differences mainly in the onset, peak, and
duration of action. Insulin therapy is an important part of treatment for individuals with no or
insufficient insulin production (e.g., diabetes mellitus, gestational diabetes). It is crucial that
patients receiving insulin therapy undergo in-depth training to prevent potentially life-threatening
conditions such as hypoglycemia as a result of an insulin overdose or drug interactions.
Glucagon
Glucagon binds to the glucagon receptor, a G protein-coupled receptor, located in the plasma
membrane of the cell. The conformation change in the receptor activates G proteins, a
heterotrimeric protein with α, β, and γ subunits. When the G protein interacts with the receptor, it
undergoes a conformational change that results in the replacement of the GDP molecule that was
bound to the α subunit with a GTP molecule. This substitution results in the release of the α
subunit from the β and γ subunits. The alpha subunit specifically activates the next enzyme in the
cascade, adenylate cyclase.
Epinephrine
As a hormone, adrenaline acts on nearly all body tissues by binding to adrenergic receptors. Its
effects on various tissues depend on the type of tissue and the expression of specific forms of
adrenergic receptors.
Adrenaline is a nonselective agonist of all adrenergic receptors, including the major subtypes α1,
α2, β1, β2, and β3. Adrenaline's binding to these receptors triggers a number of metabolic
changes. Binding to α-adrenergic receptors inhibits insulin secretion by the pancreas, stimulates
glycogenolysis in the liver and muscle, and stimulates glycolysis and inhibits insulin-mediated
glycogenesis in muscle. β adrenergic receptor binding triggers glucagon secretion in the
pancreas, increased adrenocorticotropic hormone (ACTH) secretion by the pituitary gland, and
increased lipolysis by adipose tissue. Together, these effects lead to increased blood glucose and
fatty acids, providing substrates for energy production within cells throughout the body.
Adrenaline causes liver cells to release glucose into the blood, acting through both alpha and
beta-adrenergic receptors to stimulate glycogenolysis. Adrenaline binds to β2 receptors on liver
cells, which changes conformation and helps Gs, a heterotrimeric G protein, exchange GDP to
GTP. This trimeric G protein dissociates to Gs alpha and Gs beta/gamma subunits. Gs alpha
stimulates adenylyl cyclase, thus converting adenosine triphosphate into cyclic adenosine
monophosphate (AMP). Cyclic AMP activates protein kinase A. Protein kinase A
phosphorylates and partially activates phosphorylase kinase. Adrenaline also binds to α1
adrenergic receptors, causing an increase in inositol trisphosphate, inducing calcium ions to enter
the cytoplasm. Calcium ions bind to calmodulin, which leads to further activation of
phosphorylase kinase. Phosphorylase kinase phosphorylates glycogen phosphorylase, which then
breaks down glycogen leading to the production of glucose.

    
 BIOCHEMISTRY  

Instructor: LE HONG PHU  

Date of submission: December 28, 2022 

HOMEWORK 14  

Student's Information: 
Name  ID Student 

Mai Lê Chí Bảo  BTBTWE21068

Beta-oxidation Steps:
- In the first step, acyl-CoA is oxidized by the enzyme acyl CoA dehydrogenase. A double bond
is formed between the second and third carbons (C2 and C3) of the acyl-CoA chain entering the
beta oxidation cycle; the end product of this reaction is trans-Δ2-enoyl-CoA (trans-delta 2-enoyl
CoA). This step uses FAD and produces FADH2, which will enter the citric acid cycle and form
ATP to be used as energy.
- In the second step, the double bond between C2 and C3 of trans-Δ2-enoyl-CoA is hydrated,
forming the end product L-β-hydroxyacyl CoA, which has a hydroxyl group (OH) in C2, in place
of the double bond. This reaction is catalyzed by another enzyme: enoyl CoA hydratase. This
step requires water.
- In the third step, the hydroxyl group in C2 of L-β-hydroxyacyl CoA is oxidized by NAD+ in a
reaction that is catalyzed by 3-hydroxyacyl-CoA dehydrogenase. The end products are β-
ketoacyl CoA and NADH + H. NADH will enter the citric acid cycle and produce ATP that will
be used as energy.
- Finally, in the fourth step, β-ketoacyl CoA is cleaved by a thiol group (SH) of another CoA
molecule (CoA-SH). The enzyme that catalyzes this reaction is β-ketothiolase. The cleavage
takes place between C2 and C3; therefore, the end products are an acetyl-CoA molecule with the
original two first carbons (C1 and C2), and an acyl-CoA chain two carbons shorter than the
original acyl-CoA chain that entered the beta oxidation cycle.
Energy yield:
Each beta oxidation cycle yields 1 FADH2, 1 NADH and 1 acetyl-CoA, which in terms of
energy is equivalent to 17 ATP molecules:
1 FADH2 (x 2 ATP) = 2 ATP
1 NADH (x 3 ATP) = 3 ATP
1 acetyl-CoA (x 12 ATP) = 12 ATP
Total = 2 + 3 + 12 = 17 ATP
However, the theoretical ATP yield is higher than the real ATP yield. In reality, the equivalent of
about 12 to 16 ATPs is produced in each beta oxidation cycle.

     BIOCHEMISTRY  

Instructor: LE HONG PHU  

Date of submission: January 4, 2022 

HOMEWORK 15  

Student's Information: 
 Name  ID Student 

Mai Lê Chí Bảo  BTBTWE21068

Urea cycle for NH3 deamination

Urea is the major end product of nitrogen metabolism in humans and mammals. The urea cycle
describes the conversion reactions of ammonia into urea for excretion. Ammonia, the product of
oxidative deamination reactions, is toxic in even small amounts and must be removed from the
body.
Location of urea cycle: in the liver, in particular the series of reactions that are distributed
between the mitochondrial matrix and the cytosol; then the urea is then transported to the
kidneys where it is excreted. The overall urea formation reaction is:
NH3 + CO2 + Aspartate + 3 ATP + 2 H2O → Urea + Fumarate + 2 ADP + 2 Pi + AMP + PPi
Ste Reactant Product Enzyme Location
p
1 2 ATP + HCO3 - + NH4+ Carbamoyl phosphate + CPS I Carbamoyl Mitochondria
2ADP + Pi phosphate synthase I
2 Carbamoyl phosphate + ornithine citrulline + Pi OTC Ornithine Mitochondria
transcarbamoylase
3 Citrulline + aspartate + ATP argininosuccinate + AMP + ASS Argininosuccinate Cytosol
PPi synthetase
4 Argininosuccinate Arg + fumarate ASL Argininosuccinate Cytosol
lyase
5 Arg + H2O Ornithine + urea ARG 1 Arginase 1 Cytosol

Regulation of urea cycle:

Enzymes involved in urea cycle are synthesized at higher level when proteins are utilized for
energy production (starvation, or availability of fat and carbohydrate-free diet)
The carbamoyl phosphate synthase is allosterically activated by N-acetylglutamate.