To the students taking the

course Biochemistry

You don’t have to be

brilliant to survive
Biochemistry, but you
have to be willing to
work at it.
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8

What this module is all about?

This module will discuss and describe to you the metabolic pathways for
biomolecule. This module is good for three weeks (3 wks).
What do you expect to learn?
After completion of this module, it is anticipated that you should be able to:
1. explain that the energy needed by the body is provided by the oxidation
of CHOs and lipids
2. discuss that the primary objective of lipid digestion is to arrange the
lipids in a form that is water miscible
3. explain that ketone body production only occurs during conditions of
high circulating free fatty acids.

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8

Module 8 BIOCHEMISTRY
METABOLIC PATHWAYS
INTRODUCTION:

There are many metabolic pathways/cycles/processes/reactions that are involved in

the synthesis or degradation of carbohydrates and compounds formed from them.
Please note that most of these pathways aren’t specific to carbohydrates only.
Gluconeogenesis will be covered in the protein section, because amino acids are a
common substrate used for synthesizing glucose.

A. CARBOHYDRATE METABOLISM

Steps of cellular respiration
Cellular respiration is a metabolic pathway that breaks down glucose and produces
ATP. The stages of cellular respiration include glycolysis, pyruvate oxidation, the
citric acid or Krebs cycle, and oxidative phosphorylation.
Cellular respiration, the process by which organisms combine oxygen with
foodstuff molecules, diverting the chemical energy in these substances into life-
sustaining activities and discarding, as waste products, carbon dioxide and water.

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8
Introduction

Cellular respiration is one of the most elegant, majestic, and fascinating metabolic
pathways on earth. At the same time, it’s also one of the most complicated. When I
learned about it for the first time, I felt like I had tripped and fallen into a can of
organic-chemistry-flavored alphabet soup!Luckily, cellular respiration is not so scary
once you get to know it. Let's start by looking at cellular respiration at a high level,
walking through the four major stages and tracing how they connect up to one
another.
During cellular respiration, a glucose molecule is gradually broken down into carbon
dioxide and water. Along the way, some ATP is produced directly in the reactions
that transform glucose. Much more ATP, however, is produced later in a process
called oxidative phosphorylation. Oxidative phosphorylation is powered by the
movement of electrons through the electron transport chain, a series of proteins
embedded in the inner membrane of the mitochondrion.
THE FOUR STAGES OF CELLULAR RESPIRATION

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8

What is Glycolysis?
Definition: In glycolysis pathway glucose is converted to pyruvate
(aerobic condition) or lactate (anaerobic condition), along with production
of a small quantity of energy.
Site of reaction: All the reaction steps take place in the cytoplasm.
Importance of the glycolysis pathway:
 It is the only pathway that is taking place in all the cells of the
body.
 Glycolysis is the only source of energy in erythrocytes.
 In strenuous exercise, when muscle tissue lacks enough oxygen,
anaerobic glycolysis forms the major source of energy for muscles.
 The glycolytic pathway may be considered as the preliminary step
before complete oxidation.
 The glycolytic pathway provides carbon skeletons for synthesis of
nonessential amino acids as well as glycerol part of fat.
 Most of the reactions are reversible

Steps of glycolytic pathway

1. Glucose is phosphorylated to glucose -6-phosphate. The
enzyme is hexokinase, which splits ATP into ADP and the Pi is
added on to the glucose. The energy released by hydrolysis of
ATP is utilised for the forward reaction. Hexokinase is the key
glycolytic enzyme and the reaction is irreversible.

2. Glucose-6-phosphate is isomerised to fructose-6-phosphate by

phosphohexose isomerase.

3. Fructose-6-phosphate is further phosphorylated to fructose-1,6-

bisphosphate. The enzyme is phosphofructokinase, it is an
important key enzyme and the reaction is irreversible.

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8

4. Fructose-1, 6-bisphosphate is cleaved into two 3 carbon atoms;

one glyceraldehyde-3-phosphate and another molecule of
dihydroxyacetone phosphate. The enzyme is aldolase.
Dihydroxyacetone phosphate is isomerised to glyceraldehyde-3-
phosphate by the enzyme phophotriose isomerase.

5. Glyceraldehyde-3-phosphate is dehydrogenated and

simultaneously phosphorylated to 1,3-bis-phosphoglycerate with
the help of NAD+. The enzyme is glyceraldehyde-3-phosphate
dehydrogenase.

6. 1, 3-bis-phosphoglycerate is converted to 3-phosphoglycerate

by the enzyme 1, 3-bis-phosphoglycerate kinase. Here one
molecule of ATP is formed and this reaction is an example for
Substrate level phosphorylation.

7. 3-phosphoglycerate is isomerised to 2-phosphoglycerate by

shifting the phosphate group from 3rd to 2nd carbon atom. The
enzyme is phosphoglucomutase.

8. 2-phosphoglycerate is converted to phosphoenol pyruvate by

the enzyme enolase. One water molecule is removed. A high
energy phosphate bond is produced. This enzyme requires Mg+
+and inhibited by fluoride.

9. Phosphoenol pyruvate is dephosphorylated to pyruvate, by

pyruvate kinase. One molecule of ATP is generated. This step is
irreversible.

10. In anaerobic condition pyruvate is reduced to lactate by lactate

dehydrogenase.In aerobic conditions pyruvate enters citric acid
cycle for complete oxidation. The lactate from anaerobic cycle
enters cori’s cycle.

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8

Under aerobic conditions the end product of glycolysis is pyruvic acid. The next step
is the formation of acetyl coenzyme A (acetyl CoA) - this step is technically not a part
of the citric acid cycle, but is shown on the diagram on the top left.
Acetyl CoA, whether from glycolysis or the fatty acid spiral, is the initiator of the citric
acid cycle. In carbohydrate metabolism, acetyl CoA is the link between glycolysis
and the citric acid cycle. The initiating step of the citric acid cycle occurs when a four
carbon compound (oxaloacetic acid) condenses with acetyl CoA (2 carbons) to form
citric acid (6 carbons).
The whole purpose of a “turn” of the citric acid cycle is to produce two carbon dioxide
molecules. This general oxidation reaction is accompanied by the loss of hydrogen
and electrons at four specific places. These oxidations are connected to the electron
transport chain where many ATP are produced.

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8

Step 1
The acetic acid subunit of acetyl CoA is combined with oxaloacetate to
form a molecule of citrate. The acetyl coenzyme A acts only as a
transporter of acetic acid from one enzyme to another. After Step 1, the
coenzyme is released by hydrolysis so that it may combine with another
acetic acid molecule to begin the Krebs cycle again.
Step 2
The citric acid molecule undergoes an isomerization. A hydroxyl group
and a hydrogen molecule are removed from the citrate structure in the
form of water. The two carbons form a double bond until the water
molecule is added back. Only now, the hydroxyl group and hydrogen
molecule are reversed with respect to the original structure of the citrate
molecule. Thus, isocitrate is formed.
Step 3
In this step, the isocitrate molecule is oxidized by a NAD molecule. The
NAD molecule is reduced by the hydrogen atom and the hydroxyl group.
The NAD binds with a hydrogen atom and carries off the other hydrogen
atom leaving a carbonyl group. This structure is very unstable, so a
molecule of CO2 is released creating alpha-ketoglutarate.
Step 4
In this step, coenzyme A, returns to oxidize the alpha-ketoglutarate
molecule. A molecule of NAD is reduced again to form NADH and leaves
with another hydrogen. This instability causes a carbonyl group to be
released as carbon dioxide and a thioester bond is formed in its place
between the former alphaketoglutarate and coenzyme A to create a
molecule of succinyl-coenzyme A complex.

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8

Step 5
A water molecule sheds its hydrogen atoms to coenzyme A. Then, a
free-floating phosphate group displaces coenzyme A and forms a bond
with the succinyl complex. The phosphate is then transferred to a
molecule of GDP to produce an energy molecule of GTP. It leaves
behind a molecule of succinate.
Step 6
In this step, succinate is oxidized by a molecule of FAD (Flavin adenine
dinucleotide). The FAD removes two hydrogen atoms from the succinate
and forces a double bond to form between the two carbon atoms, thus
creating fumarate.

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8

Step 7
An enzyme adds water to the fumarate molecule to form malate. The
malate is created by adding one hydrogen atom to a carbon atom and
then adding a hydroxyl group to a carbon next to a terminal carbonyl
group.
Step 8
In this final step, the malate molecule is oxidized by a NAD molecule.
The carbon that carried the hydroxyl group is now converted into a
carbonyl group. The end product is oxaloacetate which can then
combine with acetyl-coenzyme A and begin the Krebs cycle all over
again.
Summary of Krebs Cycle
In summary, three major events occur during the Krebs cycle. One GTP
(guanosine triphosphate) is produced which eventually donates a
phosphate group to ADP to form one ATP; three molecules of NAD are
reduced; and one molecule of FAD is reduced. Although one molecule of
GTP leads to the production of one ATP, the production of the reduced
NAD and FAD are far more significant in the cell’s energy-generating
process. This is because NADH and FADH2 donate their electrons to an
electron transport system that generates large amounts of energy by
forming many molecules of ATP.
Yield of ATP
At this point the yield of ATP is 4 moles per mole of Glucose as it passes
through the Krebs cycle.
 This is not much more than the 2 moles which would have been
produced from glycolysis.
 However, NADH and FADH2 are energy rich molecules
 Their oxidation is highly exergonic and is coupled with the
production of ATP from ADP z Oxidation of 1 mole NADH
produces 3 moles ATP
 Oxidation of 1 mole FADH2 produces 2 moles ATP
 Thus total ATP yield = (10 × 3) + (2 × 2) + 4 = 38 moles ATP per
mole Glucose

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8

Biosynthesis of Glycogen
The goal of glycolysis, glycogenolysis, and the citric acid cycle is to conserve energy
as ATP from the catabolism of carbohydrates. If the cells have sufficient supplies of
ATP, then these pathways and cycles are inhibited. Under these conditions of
excess ATP, the liver will attempt to convert a variety of excess molecules into
glucose and/or glycogen.
Glycogenesis
Glycogenesis is the formation of glycogen from glucose. Glycogen is synthesized
depending on the demand for glucose and ATP (energy). If both are present in
relatively high amounts, then the excess of insulin promotes the glucose conversion
into glycogen for storage in liver and muscle cells. In the synthesis of glycogen, one
ATP is required per glucose incorporated into the polymeric branched structure of
glycogen. actually, glucose-6-phosphate is the cross-roads compound. Glucose-6-
phosphate is synthesized directly from glucose or as the end product of
gluconeogenesis.

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8

Glycogenolysis
In glycogenolysis, glycogen stored in the liver and muscles, is converted first to
glucose-1- phosphate and then into glucose-6-phosphate. Two hormones which
control glycogenolysis are a peptide, glucagon from the pancreas and epinephrine
from the adrenal glands.
Glucagon is released from the pancreas in response to low blood glucose and
epinephrine is released in response to a threat or stress. Both hormones act upon
enzymes to stimulate glycogen phosphorylase to begin glycogenolysis and inhibit
glycogen synthetase (to stop glycogenesis).
Glycogen is a highly branched polymeric structure containing glucose as the basic
monomer. First individual glucose molecules are hydrolyzed from the chain, followed
by the addition of a phosphate group at C-1. In the next step the phosphate is moved
to the C-6 position to give glucose 6-phosphate, a cross road compound.
Glucose-6-phosphate is the first step of the glycolysis pathway if glycogen is the
carbohydrate source and further energy is needed. If energy is not immediately
needed, the glucose-6-phosphate is converted to glucose for distribution in the blood
to various cells such as brain cells.

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8

Gluconeogenesis
Gluconeogenesis is a metabolic pathway that results in the generation of
glucose from non-carbohydrate carbon substrates such as pyruvate,
lactate, glycerol, and glucogenic amino acids. The vast majority of
gluconeogenesis takes place in the liver and, to a smaller extent, in the
cortex of kidneys. This process occurs during periods of fasting,
starvation, or intense exercise and is highly endergonic.
Gluconeogenesis is often associated with ketosis.
Entering the pathway
Several non-carbohydrate carbon substrates can enter the
gluconeogenesis pathway. One common substrate is lactic acid, formed
during anaerobic respiration in skeletal muscle. Lactate is transported
back to the liver where it is converted into pyruvate by the Cori cycle
using the enzyme lactated hydrogenase. Pyruvate, the first designated
substrate of the gluconeogenic pathway, can then be used to generate
glucose. All citric acid cycle intermediates, through conversion to
oxaloacetate, amino acids other than lysine or leucine, and glycerol can
also function as substrates for gluconeogenesis. Amino acids must have
their amino group removed by transamination or deamination before
entering the cycle directly (as pyruvate or oxaloacetate), or indirectly via
the citric acid cycle.

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8
Fatty acids cannot be converted into glucose in animals, the exception being odd
chain fatty acids which yield propionyl CoA, a precursor forsuccinyl CoA. In plants,
specifically in seedlings, the glyoxylate cycle can be used to convert fatty acids
(acetate) into the primary carbon source of the organism. The glyoxylate cycle
produces four-carbon dicarboxylic acids that can enter gluconeogenesis. Glycerol,
which is a part of alltriacylglycerols, can also be used in gluconeogenesis. In
organisms in which glycerol is derived from glucose (e.g., humans and other
mammals), glycerol is sometimes not considered a true gluconeogenic substrate, as
it cannot be used to generate new glucose.
Gluconeogenesis is a pathway consisting of eleven enzyme-catalyzed reactions. The
pathway can begin in the mitochondria or cytoplasm, depending on the substrate
being used. Many of the reactions are reversible steps found in glycolysis.
Gluconeogenesis begins in the mitochondria with the formation of oxaloacetate
through carboxylation of pyruvate at the expense of one molecule of ATP. This
reaction is catalyzed by pyruvate carboxylase, which is stimulated by high levels of
acetyl-CoA(when fatty acid oxidation is high in the liver) and inhibited by high levels
of ADP. Oxaloacetate must then be reduced into malate using NADH in order to be
transported out of the mitochondria.
In the cytoplasm, malate is oxidized to oxaloacetate using NAD+, where the
remaining steps of gluconeogenesis occur. Oxaloacetate is then decarboxylated and
phosphorylated to produce phosphoenolpyruvate by phosphoenolpyruvate
carboxykinase. One molecule of GTP is hydrolyzed to GDP in the course of this
reaction.
The next steps in the reaction are the same as reversed glycolysis. However,
fructose-1,6-bisphosphatase converts fructose-1,6-bisphosphate to fructose-6-
phosphate. The purpose of this reaction is to overcome the large negative ΔG.
Glucose-6-phosphate is formed from fructose-6-phosphate by phospho
glucoisomerase. Glucose-6-phosphate can then be used for glucose generation or in
other metabolic pathways. Free glucose is not generated automatically because
glucose, unlike glucose-6-phosphate, tends to freely diffuse out of the cell.
The final reaction of gluconeogenesis, the formation of glucose, is carried out in the
lumen of the endoplasmic reticulum. Glucose-6-phosphate is hydrolyzed by glucose-
6-phosphatase to produce glucose. Glucose is then shuttled into the cytosol by
glucose transporters located in the membrane of the endoplasmic reticulum.
Regulation
While most steps in gluconeogenesis are the reverse of those found inglycolysis,
three regulated and strongly exergonic reactions are replaced with more kinetically
favorable reactions. Hexokinase/glucokinase, phosphofructokinase, and pyruvate
kinase enzymes of glycolysis are replaced with glucose-6- phosphatase, fructose-
1,6-bisphosphatase, and PEP carboxykinase. This system of reciprocal control allow
glycolysis and gluconeogenesis to inhibit each other and prevent the formation of
afutile cycle.

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8

The majority of the enzymes responsible for gluconeogenesis are found in the
cytoplasm; the exceptions are mitochondrial pyruvate carboxylase, and, in animals,
phosphoenol-pyruvate carboxykinase. The latter exists as an isozyme located in
both the mitochondrion and the cytosol. As there is no known mechanism to
transport phosphoenolpyruvate from the mitochondrion into the cytosol, the cytosolic
enzyme is believed to be the isozyme important for gluconeogenesis. The rate of
gluconeogenesis is ultimately controlled by the action of a key enzyme, fructose-1,6-
bisphosphatase, which is also regulated through signal ransduction bycAMP and its
phosphorylation.
Most factors that regulate the activity of the gluconeogenesis pathway do so by
inhibiting the activity or expression of key enzymes. However, both acetyl CoA and
citrate activate gluconeogenesis enzymes (pyruvate carboxylase and fructose-1,6-
bisphosphatase, respectively). Due to the reciprocal control of the cycle, acetyl-CoA
and citrate also have inhibitory roles in the activity of pyruvate kinase.
Insulin and Glucagon:
Control of Blood Glucose One of the most important and tightly regulated responses
in the human body is the concentration of blood glucose (blood sugar). Glucose is
the major breakdown product of cellular metabolism. As such, it is required both as
an energy source and as a source of carbon for making organic molecules. Blood
glucose concentrations are regulated by negative feedback pathways that are
modulated by two separate hormones: insulin and glucagon. Both of these hormones
are produced in special cells called islet cells, or islets of Langerhans – are found in
clusters throughout the pancreas. Islet cells make up a very small percentage of the
pancreas (about 1-2%); the remainder of the organ is an exocrine gland producing
digestive enzymes and bicarbonate ion. This tiny number of endocrine cells is
exceedingly important. Each islet contains two kinds of cells: alpha cells, which
produce glucagon, and beta cells, which produce insulin.
Insulin vs. Glucagon
Normally, blood glucose concentrations in human blood should range between 70-
110 milligrams (mg/ml). Insulin and glucagon operate in an antagonistic (opposing)
manner. The result is a precise control of blood glucose levels within this range.
The insulin pathway is activated when blood glucose levels are too high. High blood
glucose levels (e.g., occurring after the stomach has digested a food high in sugar)
stimulate beta cells in the pancreas to release insulin. Insulin causes an increased
uptake of glucose from the blood; promotes conversion of glucose into triglycerides
in the liver, fat and muscle cells; and increases the cellular rate of glycolysis –
breaking glucose into smaller components that can be used for synthesis of other
compounds.
The glucagon pathway is activated when blood glucose levels are too low. Low blood
glucose levels (e.g., due to exercise combined with not eating for several hours)
TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS
Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8
stimulate the alpha cells in the pancreas to produce glucagon. Glucagon causes the
liver to convert stored glycogen into glucose, then release the glucose into the blood
(a process called glycogenolysis). The two hormones, insulin and glucagon, each
regulate the other. A decrease in insulin (as well as low glucose levels) stimulates
the secretion of glucagon, while an increase in insulin (as well as an increase in
blood glucose) suppresses glucagon secretion. This results in a continuous cycle,
with insulin and glucagon constantly monitoring blood glucose levels and regulating
their secretion to maintain these levels as nearly constant as possible.
The main function of insulin is removal of excess blood glucose. Because all cells
use glucose as an energy source and as a raw material for making other organic
compounds, all cells except brain cells are targets for insulin. Since the function of
glucagon is opposite that of insulin, it stimulates the addition of glucose to the
bloodstream. Thus, it targets cells with high concentrations of energy stored as
glycogen, including the liver and skeletal muscles. It also stimulates glucose
production from fats, so adipose tissue cells are another target of glucagon.
Lactose intolerance
Lactose intolerance is a common digestive problem where the body is unable to
digest lactose, a type of sugar mainly found in milk and dairy products. The body
digests lactose by using an enzyme called lactase to break down lactose into two
simpler sugars called glucose and galactose, which can then be easily absorbed into
the bloodstream. Enzymes are proteins that cause chemical reactions to occur.
In cases of lactose intolerance, the body does not produce enough of the lactase
enzyme so lactose stays in the digestive system, where it is fermented by bacteria
(in the same way that yeast is fermented to produce beer). It’s this fermentation
process that causes the symptoms associated with lactose intolerance.
Levels of lactase often fall as people grow older and some health conditions can also
reduce the production of lactase.
Symptoms of lactose intolerance include
 a bloated stomach
 flatulence (wind)
 Diarrhoea
Treating lactose intolerance
Limiting intake of food and drink containing lactose is the main treatment for lactose
intolerance.
Depending on a person’s levels of intolerance, they may also require additional
calcium and vitamin D supplements to keep the bones strong and healthy.
Advice from a dietitian may sometimes be helpful in determining the best diet for a
person. Lactase substitutes are also available. These are drops that you can add to
your meals or drinks to improve your digestion of lactose.

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8
Diabetes Mellitus
Diabetes mellitus (often referred to simply as diabetes) is a group of metabolic
diseases characterized by high blood glucose levels. The term comes from two
Greek words: “diabetes” comes from a verb that means “to pass through” and refers
to the frequent, copious urination that is a characteristic of the disease; the word
“meli” is Greek for “honey” so the term “mellitus” refers to the presence of high levels
of glucose (sugar) in the blood. In addition to urination, other classic symptoms of
diabetes are increased thirst and hunger. The diabetic’s blood contains more
glucose than can be taken up by the cells so this excess glusose is therefore
released in the urine (a diagnostic characteristic of diabetes is sugar in the urine).
The presence of sugar results in more water being drawn into the urine to balance
the osmotic pressure, leading to copious urination.

WHAT HAVE YOU LEARNT

 In glycolysis pathway glucose is converted to pyruvate in aerobic condition or
lactate in anaerobic condition. All the reaction steps take place in the
cytoplasm.
 Glycolysis is the only pathway that is taking place in all the cells of the body
and is the only source of energy in erythrocytes.
 In Glycolyis, Aerobic conditions yields 8 ATPs and in Anaerobic conditions
yields 2 ATPs per glucose molecule
 Citric acid cycle produces two carbon dioxide molecules. And oxidations are
connected to the electron transport chain where many ATP are produced.
 A total of 38 moles ATP per mole Glucose is yielded in Krebs Cycle
 Glycogenesis is the formation of glycogen from glucose. Glycogen is
synthesized depending on the demand for glucose and ATP (energy).
 In glycogenolysis, glycogen stored in the liver and muscles, is converted first
to glucose-1- phosphate and then into glucose-6-phosphate.
 Two hormones which control glycogenolysis are a peptide, glucagon from the
pancreas and epinephrine from the adrenal glands.
 Gluconeogenesis is a metabolic pathway that results in the generation of
glucose from non-carbohydrate carbon substrates such as pyruvate, lactate,
glycerol, and glucogenic amino acids.
 Blood glucose concentrations in human blood should range between 70-110
milligrams per milliliter (mg/mL). Insulin and glucagon operate in an
antagonistic (opposing) manner.

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8

QUESTIONS :
1. In glycolysis pathway glucose is aerobically converted to .................. and
anaerobically ..................

2. All the reaction steps take place in ..................

3. Glycolysis is the only source of energy in .................. cells

4. Number of ATPs gained per glucose molecule in Aerobic conditions of glycolysis

is ..................

5. Number of ATPs gained per glucose molecule in Anaerobic conditions of

glycolysis is ..................

6. Krebs Cycle yield .................. ATP per mole Glucose.

TERMINAL QUESTIONS
1. Explain glycolysis
2. Explain krebs cycle
3. Explain glycogenesis
4. What is the hormone control of blood sugar.

PROTEIN SYNTHESIS

This amazing artwork shows a

process that takes place in
the cells of all living things: the
production of proteins. This
process is
called protein synthesis, and it actually consists of two processes
— transcription and translation. In eukaryotic cells, transcription takes
place in the nucleus. During transcription, DNA is used as a template to
make a molecule of messenger RNA (mRNA). The molecule
of mRNA then leaves the nucleus and goes to a ribosome in
the cytoplasm, where translation occurs. During translation,
the genetic code in mRNA is read and used to make a protein. These
two processes are summed up by
the central dogma of molecular biology: DNA → RNA → Protein. 

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
56
Cervantes Campus
MODULE 8
Transcription

Transcription is the first part of the central dogma of molecular biology: DNA

→ RNA. It is the transfer of genetic instructions in DNA to mRNA. During
transcription, a strand of mRNA is made to complement a strand of DNA. You can
see how this happens in the diagram below.

Overview of Transcription. Transcription uses the sequence of bases in a strand of DNA to make a
complementary strand of mRNA. Triplets are groups of three successive nucleotide bases in DNA. Codons are
complementary groups of bases in mRNA.

Steps of Transcription

Transcription takes place in three steps: initiation, elongation, and termination. The

steps are illustrated in the figure below.

1. Initiation is the beginning of transcription. It occurs when

the enzyme RNA polymerase binds to a region of a gene called the promoter.
This signals the DNA to unwind so the enzyme can “read” the bases in one of the
DNA strands. The enzyme is ready to make a strand of mRNA with a
complementary sequence of bases.

2. Elongation is the addition of nucleotides to the mRNA strand.

3. Termination i
s the ending of
transcription.
The mRNA
strand is
complete, and
it detaches
from DNA.

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Steps of Transcription. Transcription occurs in three steps: initiation, elongation, and termination.

Processing mRNA

In eukaryotes, the new mRNA is not yet ready for translation. At this stage, it is
called pre-mRNA, and it must go through more processing before it leaves the
nucleus as mature mRNA. The processing may include splicing, editing,
and polyadenylation. These processes modify the mRNA in various ways. Such
modifications allow a single gene to be used to make more than one protein.

 Splicing removes introns from mRNA, as shown in the

diagram below. Introns are regions that do not code for the protein. The
remaining mRNA consists only of regions called exons that do code for the
protein. The ribonucleoproteins in the diagram are small proteins in the nucleus
that contain RNA and are needed for the splicing process.
 Editing changes some of the nucleotides in mRNA. For example, a human
protein called APOB, which helps transport lipids in the blood, has two different
forms because of editing. One form is smaller than the other because editing
adds an earlier stop signal in mRNA.
 Polyadenylation adds a “tail” to the mRNA. The tail consists of a string of As
(adenine bases). It signals the end of mRNA. It is also involved in exporting
mRNA from the nucleus, and it protects mRNA from enzymes that might break it
down.

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Proteins are made up of amino acids that are arrainged in orderly fashion. Discover
how the cell organizes protein synthesis with the help of the RNAs. You’re more than
welcome to join us in our Forum discussion: What does mRNA do in protein
synthesis?

TRANSLATION

Translation is the second part of the central dogma of molecular biology: RNA →

Protein. It is the process in which the genetic code in mRNA is read to make a
protein. Translation is illustrated in the diagram below. After mRNA leaves the
nucleus, it moves to a ribosome, which consists of rRNA and proteins. The ribosome
reads the sequence of codons in mRNA, and molecules
of tRNA bring amino acids to the ribosome in the correct sequence.

To understand the role of tRNA, you need to know more about its structure. Each
tRNA molecule has an anticodon for the amino acid it carries. An anticodon is
complementary to the codon for an amino acid. For example, the amino acid lysine
has the codon AAG, so the anticodon is UUC. Therefore, lysine would be carried by
a tRNA molecule with the anticodon UUC. Wherever the codon AAG appears in
mRNA, a UUC anticodon of tRNA temporarily binds. While bound to mRNA, tRNA
gives up its amino acid. With the help of rRNA, bonds form between the amino acids
as they are brought one by one to the ribosome, creating a polypeptide chain. The
chain of amino acids keeps growing until a stop codon is reached.

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Translation. Translation of the codons in mRNA to a chain of amino acids occurs at a ribosome. Find the different
types of RNA in the diagram. What are their roles in translation?

What Happens Next?

After a polypeptide chain is synthesized, it may undergo additional processes. For

example, it may assume a folded shape due to interactions between its amino acids.
It may also bind with other polypeptides or with different types of molecules, such as
lipids or carbohydrates. Many proteins travel to the Golgi apparatus within the
cytoplasm to be modified for the specific job they will do.

Summary

 Protein synthesis is the process in which cells make proteins. It occurs in two
stages: transcription and translation.
 Transcription is the transfer of genetic instructions in DNA to mRNA in the
nucleus. It includes three steps: initiation, elongation, and termination. After the
mRNA is processed, it carries the instructions to a ribosome in the cytoplasm.
 Translation occurs at the ribosome, which consists of rRNA and proteins. In
translation, the instructions in mRNA are read, and tRNA brings the correct
sequence of amino acids to the ribosome. Then, rRNA helps bonds form between
the amino acids, producing a polypeptide chain.
 After a polypeptide chain is synthesized, it may undergo additional processing to
form the finished protein.

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Protein synthesis – schematic diagram

In biology, a codon refers to the trinucleotides that specify for a particular amino acid. For
example, Guanine-Cytosine-Cytosine (GCC) codes for the amino acid alanine. The
Guanine-Uracil-Uracil (GUU) codes for valine. Uracil-Adenine-Adenine (UAA) is a stop
codon. The codon of the mRNA complements the trinucleotide (called anticodon) in the
tRNA.

What is the Genetic Code? “The genetic code is the system that combines
different components of protein synthesis, like DNA, mRNA, tRNA…” More
FAQ answered by our biology expert in the Forum: What does mRNA do in
protein synthesis? Come join us now!

mRNA, tRNA, and rRNA

mRNA, tRNA, and rRNA are the three major types of RNA involved in protein
synthesis. The mRNA (or messenger RNA) carries the code for making a protein. In
eukaryotes, it is formed inside the nucleus and consists of a 5′ cap, 5’UTR region,
coding region, 3’UTR region, and poly(A) tail. The copy of a DNA segment for gene
expression is located in its coding region. It begins with a start codon at 5’end and
a stop codon at the 3′ end.

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tRNA (or transfer RNA), as the name implies, transfers the specific amino acid to the
ribosome to be added to the growing chain of amino acid. It consists of two major
sites: (1) anticodon arm and (2) acceptor stem. The anticodon arm contains the
anticodon that complementary base pairs with the codon of the mRNA. The acceptor
stem is the site where a specific amino acid is attached (in this case, the tRNA with
amino acid is called aminoacyl-tRNA). A peptidyl-tRNA is the tRNA that holds the
growing polypeptide chain.

Unlike the first two, rRNA (or ribosomal RNA) does not carry genetic information.
Rather, it serves as one of the components of the ribosome. The ribosome is a
cytoplasmic structure in cells of prokaryotes and eukaryotes that are known for
serving as a site of protein synthesis. The ribosomes can be used to determine a
prokaryote from a eukaryote. Prokaryotes have 70S ribosomes whereas eukaryotes
have 80S ribosomes. Both types, though, are each made up of two subunits of
differing sizes. The larger subunit serves as the ribozyme that catalyzes the peptide
bond formation between amino acids. rRNA has three binding sites: A, P, and E
sites. The A (aminoacyl) site is where aminoacyl-tRNA docks. The P (peptidyl) site is
where peptidyl-tRNA binds. The E (exit) site is where the tRNA leaves the ribosome.

Review

1. Relate protein synthesis and its two major phases to the central dogma of
molecular biology.
2. Identify the steps of transcription, and summarize what happens during each step.
3. Explain how mRNA is processed before it leaves the nucleus.
4. Describe what happens during the translation phase of protein synthesis.
5. What additional processes might a polypeptide chain undergo after it is
synthesized?
6. Where does transcription take place in eukaryotes?
7. Where does translation take place?
8. Which type of RNA (mRNA, rRNA, or tRNA) best fits each of the statements
below? Choose only one type for each.
a. contains the codons
b. contains the anticodons
c. makes up the ribosome, along with proteins
9. If the DNA has a triplet code of CAG in one strand (the strand used as a template
for transcription)...
a. What is the complementary sequence on the other DNA strand?

b. What is the complementary sequence in the mRNA? What is this sequence

called?

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c. What is the resulting sequence in the tRNA? What is this sequence called? What
do you notice about this sequence compared to the original DNA triplet on the
template strand?

10. The promoter is a region located in the:

a. DNA
b. mRNA
c. tRNA
d. both A and B

11. True or False: Introns in mRNA bind to tRNA at the ribosome.

12. True or False: tRNAs can be thought of as the link between amino acids and
codons in the mRNA.

NUCLEIC ACID SYNTHESIS

Nucleic acids are targets of many important drugs, including several
anticancer agents. There are two types of nucleic acids: deoxyribonucleic
acid (DNA) and ribonucleic acid (RNA). DNA encodes the hereditary details
and controls the growth and division of the cells. The genetic information
stored in DNA is then transcribed into RNA, and the details in RNA are then
translated for the synthesis of the proteins.
Nucleotide synthesis is an anabolic mechanism generally involving the chemical
reaction of phosphate, pentose sugar, and a nitrogenous base. Destruction of
nucleic acid is a catabolic reaction. Additionally, parts of the nucleotides or
nucleobases can be salvaged to recreate new nucleotides.

Nucleosides and Nucleotides

• Nucleic acids are chains of five membered ring sugars linked by phosphate
groups (Figure 1). The anomeric carbon of each sugar is bonded to a nitrogen
of heterocyclic amine in a β-glycosidic linkage. In RNA, the five membered
sugar is D-ribose. In DNA, the five membered sugar is 2’deoxy-D-ribose.

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• The difference in heredity among the species is determined by the

sequence of the bases in DNA. DNA has four bases: adenine, guanine,
cytosine and thymine.
• RNA also contains four bases. Three-adenine, guanine and cytosine-
are same as those in DNA. But the fourth base in RNA is uracil instead
of thymine.

• A compound with a base bonded to D-ribose or 2’-deoxy-D-ribose is

called nucleoside. Figure 2 shows an example using adenine as base.
Similarly, other bases (guanine, cytosine, uracil and thymine) can also
make bond to the sugar to give the corresponding nuleotides. The
stereochemistry of the linkage between the base and the ribose is most
commonly β.

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• Nucleotide is nucleoside with either the 5’ or the 3’-OH group bonded in

an ester linkage to phosphoric acid. The nucletotide where the sugar is
D-ribose is called ribonuleotide, whereas the nucleotide with 2’-deoxy-D-
ribose is called deoxyribonuleotide (Figure 3).

• Nucleic acids are biopolymers composed of nucleotide subunits linked

by phosphodiester bonds. DNA and RNA are polynucleotides.
Nucleotide triphosphate serves as substrate precursor for the
biosynthesis of nucleic acids. The nucleotides are linked by the
nucleophilic attack of 3’-OH of one nucleotide triphosphate on the -
phosphorus of another nucleotide (Figure 4).

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• Primary Structure: It describes the sequence of bases in the strand. By

convention, the sequence of bases is written in the 5’ to 3’ direction.

• Secondary Structure: DNA consists of two strands of nucleic acids with

the sugarphosphate backbone outside and the base inside. The chains
are held together by H- bonding between the base of one strand with the
base of another strand. Adenine pairs with thymine, while guanine pairs
with cytosine through two and three H-bonds, respectively. This means if
we know the sequences bases in one strand, we will be able to
sequence the bases in the other strand (Figure 5a). If the two strands
run in opposite directions, the strands are not linear. Instead they are
twisted into a helix around common axis, which is known as double helix
(Figure 5b).

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• Figure 6 shows the base pairing in DNA: adenine and thymine form two H-bonds;
cytosine and guanine form three H-bonds

Stability of DNA and RNA

In RNA, the 2’-OH of ribose attacks the adjacent phosphodiester group

that leads to the cleavage of the strand (Figure 7). This reaction does not
take place in DNA, because it does not have the 2’-OH group. Thus,
DNA remain intact throughout the life span of cells .

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Biosynthesis of DNA:
Replication Each strand of DNA acts as a template for the formation of
complementary new strand (Figure 1). The new (daughter) DNA molecules have the
same genetic information as that of the parent DNA. The synthesis of the identical
copies of DNA is known as replication (Figure 1).

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• The synthesis take place in a region where the strands have started to separate,
because a nucleic acid can be synthesized only in the 5’ to 3’ direction.
• The synthesis is catalyzed by enzyme is known as DNA polymerase, and the
fragments are joined together by an enzyme is called DNA ligase. • In each of
daughter DNA molecules, one strand comes from the parent DNA and another
strand is synthesized. This process is called semiconservative replication.
DNA replication is semi-conservative. This means that each of the two strands in
double-stranded DNA acts as a template to produce two new strands.
Replication relies on complementary base pairing, that is the principle explained by
Chargaff's rules: adenine (A) always bonds with thymine (T) and cytosine (C) always
bonds with guanine (G).

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This base pairing provides a means

of duplicating the DNA during cell
division. Each strand of the parent
DNA molecule unwinds, and
different nucleoside triphosphates
(deoxyadenosine triphosphate,
dATP; deoxycytidine triphosphate,
dCTP; etc.) are paired with the
exposed bases on each strand. The
free energy of the triphosphate is
used to connect these paired
nucleotides into a 5`-3` polymer, so
that each of the parent DNA strands
now is paired with a new strand
identical to the one from which it
separated.

This replication process is shown
schematically on the right. The
result is two daughter helices, each
identical with the parent in base
sequence and pairing, and each
containing one of the parent strands
and one newly polymerized strand.
The double helix is not only a
protection, it is the basis for
reproduction.

Right: DNA is replicated by

unwinding the two strands and
building a new complementary
strand to each. The daughter
molecules are exact copies of the
parent, each with one of the
parent strands. Based and
adapted from James D.
Watson, Molecular Biology of the
Gene, Second Edition, W. A.
Benjamin, Inc. Copyright © 1970
J. D. Watson.

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The replication process

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DNA replication occurs through the help of several enzymes. These
enzymes "unzip" DNA molecules by breaking the hydrogen bonds that
hold the two strands together.

Each strand then serves as a template for a new complementary

strand to be created. Complementary bases attach to one another (A-T
and C-G).

The primary enzyme involved in this is DNA polymerase which joins

nucleotides to synthesize the new complementary strand. DNA
polymerase also proofreads each new DNA strand to make sure that
there are no errors.

Leading and lagging strands

DNA is made differently on the two strands at a replication fork.

One new strand, the leading strand, runs 5' to 3' towards the fork and is
made continuously.

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The other, the lagging strand, runs 5' to 3' away from the fork and is
made in small pieces called Okazaki fragments.

Example: Determining a complementary strand

DNA is only synthesized in the 5' to 3' direction. You can determine the
sequence of a complementary strand if you are given the sequence of
the template strand.

For instance, if you know that the sequence of one strand is 5’-
AATTGGCC-3’, the complementary strand must have the sequence 3’-
TTAACCGG-5’. This allows each base to match up with its partner:

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Common mistakes and misconceptions

 DNA replication is not the same as cell division. Replication occurs

before cell division, during the S phase of the cell cycle. However,
replication only concerns the production of new DNA strands, not of new
cells.
 Some people think that in the leading strand, DNA is synthesized in
the 5’ to 3’ direction, while in lagging strand, DNA is synthesized in
the 3’ to 5’ direction. This is not the case. DNA polymerase only
synthesizes DNA in the 5’ to 3’ direction only. The difference between
the leading and lagging strands is that the leading strand is formed
towards replication fork, while the lagging strand is formed away from
replication fork.

Biosynthesis of RNA:
Transcription
• The synthesis of RNA from DNA blueprint is known as transcription. It starts by
DNA at a particular region to afford two single strands: (i) sense strand and (ii)
template strand (Figure 2).
• The template strand read in 3’ to 5’ direction, and the RNA is synthesized in 5’ to 3’
direction. • The base in the template strand specifies the base sequence to be
incorporated in RNA.

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RNA
RNA is a single stranded polymer and does not form double helix.
There are three types of RNA:
• Messenger RNA (mRNA), whose base sequence specifies the amino
acid sequence in protein.
• ribosomal RNA (rRNA), that comprises the particles on which the
biosynthesis of protein occurs.
• transfer RNA (tRNA), which carries the amino acid that will be
incorporated into the protein.
 tRNAs are shorter than mRNA and rRNA, and folded into a
characteristic cloverleaf like structure (Figure 3). They have a CCA
sequence at the 3’end, and the three bases at the bottom are
called anticoden.
 Each tRNA carries an amino acid as an ester to its terminal 3’OH.
The amino acid will be inserted into a protein during the protein
synthesis.

Figure 4. Mechanism for amino acyl tRNA synthetase-the enzyme that catalyzes the
attachment of an amino acid to tRNA
 Figure 4 shows the mechanism for the attachment of an amino acid in tRNA.
 In the first step, the CO2 of amino acid attacks the α-phosphorus of ATP. The
carboxylic acid of amino acid is now activated with good leaving group.
 The 3’-OH group of tRNA attacks the carbonyl carbon via nucleophilic addition to
give the amino acid attached tRNA.

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Biosynthesis of Proteins: Translation
During the synthesis, rRNA attaches to one end of the mRNA strand and travels
along the strand (Figure 5). As it travels, the nucleic acid bases of mRNA are read as
triplets. The tRNA that recognizes that triplet is bound and brings the amino acid
coded by that triplet. The protein is constructed on tRNA and transferred from one
tRNA to the next until the synthesis is completed.

Lipid basics
Lipids are fatty substances that are required for maintenance of normal bodily
function. Cholesterol and triglycerides are the major lipids that circulate in blood
plasma and are transported in globules known as lipoproteins. Cholesterol is an
important component of cell membranes and is required for the synthesis of steroid
hormones and bile acids. As the daily requirement for cholesterol cannot be met
from dietary intake, the majority (80%) is derived from biosynthesis in the liver.
Triglycerides are the storage form of long chain fatty acids, derived from the diet or
synthesised in the liver, which are an important source of energy and structural fatty
acids required for formation of phospholipids, an essential component of cell
membranes. Both the liver and the gut package cholesterol, triglycerides and fat-
soluble vitamins into lipoproteins for delivery to other tissues.
LIPID SYNTHESIS
Lipids are organic compounds found in plant and animal tissue, and are oily/greasy
substances. They are soluble in organic solvents such as benzene, ether or
chloroform, but only sparingly soluble in water. In routine feed analysis, all kinds of
lipids are determined together as the ether extract. Thus, the lipids include fats, oils,
steroids, waxes, and other related compounds. Lipids are important dietary
constituents not only because of their high energy value but also because of fat-
soluble vitamins and the essential fatty acids contained in the fat of natural foods.
Lipids are organic compounds that are found in living organisms. They have variety
of structures and functions, and soluble in organic solvents due to their hydrocarbon
component. Scheme 1 illustrates some examples:

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All lipoproteins have a common basic structure (figure 1) but they vary greatly in their
size, density and composition (figure 2 and table 1).

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Lipid fractions are mixtures of lipoproteins of similar size and density which can be
separated by the ultracentrifuge and are named accordingly as:
 high density lipoproteins (HDL)
 low density lipoproteins (LDL)
 very low density lipoproteins (VLDL).

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As VLDL are metabolised into LDL (see below), short-lived intermediate density
lipoproteins are also seen (IDL).
Chylomicrons, which appear after meals, are the largest and lowest density
lipoproteins and rapidly float to the top of stored plasma without ultracentrifugation.
Chylomicrons are rapidly metabolised into smaller VLDL sized particles (chylomicron
remnants).
Apolipoproteins
In addition to their lipid components, lipoproteins contain specific protein components
known as apolipoproteins which provide a structural framework and have a number
of other important functions, including binding to receptors and activation of lipid
transporters and metabolising enzymes. More detail on specific apolipoproteins can
be found in the drop down box.
Specific apolipoproteins
Hide details
Apolipoprotein B100 is the bulk carrier of endogenously produced lipids and is
secreted by the liver as the major apolipoprotein component of VLDL and LDL, one
molecule per lipoprotein, which stays with the particle until it is removed from the
circulation by the LDL receptor. A shorter form of this apolipoprotein, apolipoprotein
B48, is secreted by the intestine as the major structural component of chylomicrons
which carry dietary (exogenous) lipids.
The large, triglyceride rich VLDL and chylomicrons also contain multiple copies of
small exchangeable apolipoproteins (apolipoproteins AI AII AIV, CI CII CIII and E)
which enter the HDL fraction as triglyceride is removed by triglyceride metabolising
enzymes lipoprotein lipase (LPL) and hepatic lipase (HL). Apolipoprotein A1 is
secreted by both the gut and the liver and is the major apolipoprotein component of
HDL which has an important role in the reverse transport of cholesterol back to the
liver from peripheral tissues.
Plasma lipid pathways
The three major pathways are co-ordinated by the liver to ensure that balance
(homeostasis) of the major lipid classes is maintained, avoiding the twin perils of
deficiency and overload:
 endogenous
 exogenous
 reverse.

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Intestinal (exogenous) pathway

Figure 3 shows the intestinal (exogenous) pathway. Cholesterol and triglycerides

derived from dietary lipids are absorbed in the gut and incorporated into
chlyomicrons, regulated by the Niemann-Pick C1-Like 1 (NPC1L1) transporter and
microsomal triglyceride transfer protein (MTP). These very large, triglyceride-rich
lipoproteins are secreted into the lymph and bypass the liver, entering the plasma
post-prandially via the thoracic duct. Chylomicrons deliver the fat to adipose tissue
via lipoprotein lipase (LPL) which allows it to be taken up rapidly in the form of fatty
acids. Once small enough the resulting chylomicron remnant is removed from
plasma by the liver via apoE (see drop down box) binding to the remnant receptor
(LRP) or to the LDL receptor (LDLR). Left over surface material and exchangeable
apolipoproteins (AI AII AIV, CI CII CIII and E) may enter the HDL pool as ‘nascent
HDL’. Between meals (post-absorptive phase), as insulin levels fall, fatty acids are
released from adipose tissue by lipolysis (hormone sensitive lipase and adipose
tissue triglyceride lipase) and enter the circulation where they are rapidly bound to
albumin.

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Hepatic (endogenous) pathway

Fatty acids, arriving at the liver bound to albumin or newly-synthesised

(de novo lipogenesis), are re-esterified to form triglyceride and together
with cholesterol are loaded onto apoB to form VLDL. These large
triglyceride rich lipoproteins enter the plasma between meals and deliver
the fat to adipose tissue and muscle via lipoprotein lipase (LPL) which
allows it to be taken up in the form of fatty acids (see figure 4). Once
small enough, the resulting IDL is either taken up directly by the liver
(cf. Chylomicron remnant) or converted to LDL by hepatic lipase (HL).
The resulting LDL may then be taken up by peripheral tissues via the
LDLR to meet local cholesterol needs. Any surplus LDL particles are
finally removed by the liver via the LDLR.

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Reverse cholesterol pathway

HDL inhibits the development of atheroma and coronary artery disease by

transporting excess tissue cholesterol to the liver, where it is converted into bile
acids and excreted (figure 5). Lower levels of HDL have been correlated with an
increased risk of atherosclerosis, the primary cause of cardiovascular disease. The
principal HDL pathway, termed reverse cholesterol transport (RCT) is a major
contributor to lipid homeostasis. Cholesteryl ester transfer protein (CETP) is
responsible for the exchange of cholesteryl esters from HDL for triglyceride in more
atherogenic cholesterol fractions including LDL and VLDL. Some individuals with
loss of function in the gene encoding CETP appeared to be at lower cardiovascular
risk and CETP therefore became an attractive target for pharmaceutical inhibition.
Nascent HDL, in the form of flattened discs, is generated from LPL- mediated
lipolysis of triglyceride rich lipoproteins (TRLs,) including (VLDL and cChylomicrons),
or triglyceride rich lipoproteins (TRLs) or secreted directly from the gut or liver, and
enters plasma and where it picks up additional exchangeable apolipoproteins.
Free cholesterol is removed from peripheral tissues (including cholesterol laden
macrophages in the arterial wall) via ATP-binding cassette A1 (ABCA1) activated by
apoA1, rapidly esterified by the action of lecithin cholesterol acyl transferase (LCAT)
and funnelled into the core of the new HDL particle converting it to the mature

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spherical form. Core lipid exchanges between HDL and TRLs occur in the
circulation, catalysed by CETP. This allows cholesterol to be offloaded from HDL into
VLDL and LDL which are destined for hepatic uptake, permitting further cholesterol
uptake from tissues. Finally the cholesterol-enriched HDL particle returns cholesterol
to the liver via the scavenger receptor B1 (SCARB1) for biliary excretion. The
cholesterol-depleted HDL particles can then return to the circulation to undertake
more reverse cholesterol transport.
Cholesterol homeostasis
The rate of cholesterol formation by the liver and absorption by the small intestine
is highly responsive to the cellular level of cholesterol. This feed back regulation is
controlled primarily by changes in the amount and activity of 3-hydroxy-3
methylglutaryl CoA reductase (HMGCoA reductase). This enzyme catalyses
formation of mevalonate, the committed step in cholesterol biosynthesis. (For more
detail on this process of cholesterol homeostasis, see dropdown box).

Cholesterol homeostasis
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The concentration of free cholesterol determines the fluidity and function of cell
membranes and regulates overall cholesterol homeostasis (see figure 6). The
concentration of free cholesterol is ‘sensed’ by membrane bound transcription
factors, known as sterol regulatory element binding proteins (SREBPs). When
TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS
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Instructor: SUSANA N. PE
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hepatic cholesterol content is reduced by export in lipoproteins or conversion to bile
acids, membrane cholesterol concentration falls and SREBP-2 activates the
enzymes of cholesterol synthesis, including HMG-Co-A reductase which is the rate
limiting step in the pathway. SREBP-2 also activates the synthesis of LDL-receptors,
accelerating the uptake of cholesterol in LDL to help restore membrane cholesterol
concentration. In addition, SREBP-2 activates synthesis and secretion of proprotein
convertase subtilisin/kexin type-9 (PCSK9), a counterbalancing factor which ‘applies
the brakes’ by binding LDL-receptors and directing them to destruction in the
lysosome, thereby preventing their recycling to the cell membrane.
Conversely, when hepatic cholesterol is increased by receptor mediated uptake of
cholesterol in lipoproteins or return of cholesterol to the liver by HDL particles,
membrane cholesterol increases, preventing activation of SREBP-2 and leading to
LDL-receptor downregulation and inactivation of cholesterol synthesis.
Lipoproteins and atherogenesis
The majority of circulating
cholesterol is carried in
LDL which is the
lipoprotein most closely
associated with the
development of
atherosclerosis.
Table 2. Steps in
atherogenesis

The steps in atherogenesis

are summarised in table 2.
Under normal circumstances, LDL may pass from the plasma into the subendothelial
space and return to the liver to be removed from the circulation. At this point it has
performed its transport functions without being taken up by macrophages and indeed
is unable to stimulate foam cell formation in vitro. However, if retention of the LDL in
the endothelial space is increased, due to endothelial injury (e.g. with smoking,
hyperglycaemia, hypertension) or if removal of LDL from the circulation is delayed, it
can become damaged by oxidation or modified in other ways.
Oxidised or otherwise modified LDL are retained in the subendothelial space and are
taken up by monocyte-derived macrophages via the scavenger receptor leading to
the formation of foam cells, and the development of arterial sub-endothelial fatty
streaks, the precursor of atheroma. Small dense LDL particles, typically found in
found in association with prolonged postprandial hypertrigylceridaemia and low HDL

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cholesterol, appear more susceptible to oxidation which may make them more
atherogenic. Retention of oxidised lipoproteins in the subendothelial space
generates an inflammatory reaction – the ‘response to retention’ hypothesis of
atherosclerosis
Partially metabolised remnants of triglyceride-rich lipoproteins (remnant lipoproteins)
that appear post-prandially are able to induce foam cell formation without
modification. These are considered the most highly atherogenic of all. Other
atherogenic lipoproteins readily retained in the subendothelial space include glycated
LDL and lipoprotein(a). HDL are, however, able to penetrate deep into the
subendothelial space and are able to remove oxidised lipid from macrophages and
prevent foam cell formation, in addition to having a protective effect on the
endothelium. Reduction of HDL particle numbers or functional activity is therefore
pro-atherogenic.
Figure 7 shows the progression of atherosclerosis.

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LIPOLYSIS
Lipolysis is the metabolic process through which triacylglycerols (TAGs) break
down via hydrolysis into their constituent molecules: glycerol and free fatty
acids (FFAs). Fat storage in the body is through adipose TAGs and is utilized
for heat, energy, and insulation. The body uses fat stores as its main source of
energy during starvation, conserving protein. Overall, fats are quantitatively
the most important fuel in the body, and the length of time that a person can
survive without food depends mainly on the amount of fat stored in the
adipose tissue. Thus, lipolysis is especially important in the fasting state of
metabolism when blood glucose levels have decreased. However, it also
occurs under non-stimulated (basal conditions).
The glycerol produced by lipolysis is a source of carbon for gluconeogenesis
in the liver. FFAs are transported in the blood bound to albumin and are either
oxidized in tissues by a process called beta-oxidation or converted to ketone
bodies. The byproducts of beta-oxidation, ATP, and NADH, promote
gluconeogenesis. FFAs convert to ketone bodies in the liver, which serves as
an energy source for the brain, thus decreasing further consumption of
already depleted blood glucose. FFAs are utilized throughout the body for
energy production or biosynthetic pathways except in white adipose tissue
(WAT) where they are stored. In a metabolic "fasting" state, when the body is
deprived of nutrients, WAT releases FFAs and glycerol to supply non-adipose
tissues. The major enzymes participating in lipolysis constitute adipose
triglyceride lipase (ATGL), hormone-sensitive lipase (HSL), and
monoglyceride lipase (MGL).
Lipolysis is the process by which fats are broken down in our bodies through
enzymes and water, or hydrolysis. Lipolysis occurs in our adipose
tissue stores, which are the fatty tissues that cushion and line our bodies and
organs. In fact, fats can be thought of simply as stored energy. Fats are ready
and available for when our glucose stores run low between meals, and it
makes sense for lipolysis to occur as it will facilitate the movement of these
stored fats through our bloodstream. Breaking down this “potential energy”
into free moving fatty acids can then allow them to be repurposed or
expended as fuel!
Lipolysis actually has links to various processes within our bodies. Free fatty
acids are vital cell-to-cell communicators, are a staple ingredient
of gluconeogenesis and cellular respiration, and can upregulate
the transcription of proteins like the uncoupling proton channels that line our

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mitochondrial membrane – which will inhibit ATP synthesis without disrupting
the respiratory chain. In sum, lipolysis is a key life-sustaining biological
process; although, as of late, it’s taken on new meaning at cosmetic clinics
around the world for its promise to zap unwanted fat! While for their
namesake, both processes technically “lyse” or break fats, the way in which

they accomplish this is obviously different – the latter utilizing cool lasers or
heat to reduce fat cells.
Lipolysis Mechanism

Triglycerides are undoubtedly the main energy molecule in eukaryotic cells.

Triglyceride is a glycerol derivative that is stored as lipid droplets within our fatty
tissues, and herein lipolysis takes place. Let’s begin by describing lipolysis in big
picture scope. These lipid droplets are first targeted by lipolytic enzymes that are
highly regulated and will access these droplets in the event of phosphorylation.
These lipases will ensue to sequentially hydrolyze our triglycerides into their glycerol
and fatty acid components until we are left with sole glycerols, and this takes place
with three enzyme reactions. The breakdown of fats is termed beta-oxidation, or
“fatty acid” oxidation because the triglycerides are being oxidized into their most
basic functional parts. We are thus left with free fatty acids and glycerol that can
enter other metabolic pathways or find new purpose. Let’s dive into specifics.

The image depicts the Lipolysis mechanism, breakdown of triglycerides into fatty
acids and glycerol.

The first and rate-limiting step of lipolysis involves the enzyme, adipose triglyceride

lipase (or ATGL), which is sensitive to hormones. The ATGL will hydrolyze our
triacylglycerol into a diacylglycerol, losing a free fatty acid that will be free to mobilize
in our bloodstream. The resultant diacylglycerol will then be acted upon by hormone-
sensitive lipase (HSL), which will remove another fatty acid to give a
monoacylglycerol molecule. Finally, monoacylglycerol lipase (MGL) will break the
monacylglycerol further down to a single glycerol molecule.

The figure below illustrates the main “destinies,” if you will, of the resulting fatty acids
and glycerol. Fatty acids can undergo beta-oxidation and repurpose to create Acetyl-
CoA. Of course, Acetyl-CoA is best known as a vital starting molecule that initiates
the Krebs’s cycle in cellular respiration. This repurposing is vital when glucose stores
are low in times of starvation, or even between meals, as cellular respiration can
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Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE
 ILOCOS SUR POLYTECHNIC STATE COLLEGE
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MODULE 8
continue to run and sustain life. Similarly, the free glycerol can enter glycolysis.
Normally glucose is converted to G6P at the first step of glycolysis. In the event that
glucose levels are low, glycerol will be converted to dihydroxyacetone phosphate
and will enter glycolysis at the second control point to keep glycolysis running. Thus,
fats make the best energy store as they will ensure that cellular respiration continues
to run and ATP is produced.

The figure illustrates Lipolysis and the pathways the

fatty acids and glycerol components take.

Lipolysis Regulation

Like every vital biological process, lipolysis is regulated to meet our needs. At any
given time, it would be extremely harmful to have tons of free fatty acids flowing
through our bloodstream. Anyone with high cholesterol or arterial plaques will attest
to that. Thus, lipolysis – and its inverse process, lipogenesis – need to be counter-
regulated and highly sensitive to the levels of specific hormones and proteins. For

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 ILOCOS SUR POLYTECHNIC STATE COLLEGE
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example, stimulatory hormones like, epinephrine, norepinephrine, cortisol, glucagon,
and growth hormone induce lipolysis. Key hormones glucagon and epinephrine will
use the same pathways to induce lipolysis with minor differences.

Both glucagon and epinephrine will serve as ligands that will bind to G-
protein coupled receptors on the surface of fat cells. The G proteins will
then activate adenylate cyclase and upregulate their conversion of ATP
to cAMP. We might recognize cAMP as the famously ubiquitous
secondary messenger of so many other biological pathways. Likewise,
here the cAMP will activate protein kinase A (PKA), which will expend an
ATP molecule in phosphorylating and upregulating the hydrolysis activity
of our HSL enzyme – otherwise known as our second enzyme in the
lipolysis pathway. As a result, we are left with free fatty acids and
glycerol that can then enter metabolic pathways to counter the low
sugars in our blood, for instance. Understandably, HSL was thought to
be the rate-determining enzyme of lipolysis for some time before TAG
lipase (or ATG, our first enzyme) was uncovered to be the key initiative
lipolytic step. Let’s quickly take a look at why it makes sense for
glucagon and epinephrine to trigger lipolysis.

Glucagon-induced Lipolysis
Glucagon is a peptide hormone that is synthesized by pancreatic cells in
the event that glucose and thus insulin levels drop. Glucagon will then
trigger our liver to break down its glycogen stores and release much
needed glucose into our blood. Conversely, when our glucose and
insulin levels are high, insulin in healthy individuals will allow glucose to
exit the bloodstream and be taken up by insulin-dependent tissues. Of
course, in diabetics, the tissues will no longer respond well to insulin and
this sugar will not reach the tissues and instead cause havoc in the
bloodstream.

Shifting back our focus to lipolysis, glucagon stores are small and will be
expended quickly. Fat stores, on the other hand, are vast and ready to
use. Here, glucagon serves its key role. Glucagon will bind to Glucagon
G-protein coupled receptors on fat cell membranes, and trigger the HSL-
activating pathway described earlier. The glycerol that is released can
then travel to the liver or kidney where it will be eventually converted to

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GA3P and enter glycolysis and our gluconeogenesis pathway to
synthesis badly needed glucose (refer to figure 2).

Epinephrine-induced Lipolysis

The diagram specifically illustrates epinephrine-induced Lipolysis through a G-

protein mediated pathway.

Epinephrine will also bind G-protein receptors on fat cell membranes,

however they will specifically bind beta-adrenergic receptors. This
binding will likewise lead to the cAMP/PKA-led phosphorylation of
hormone sensitive lipase, that will ultimately drive the release of free
fatty acids and glycerol. Epinephrine is known for its connection to our
instinctual “fight or flight” response. This hyperarousal occurs when we
perceive an attack or threat to our survival. Thus, it makes sense that
epinephrine would trigger lipolysis and its resulting up-drive of metabolic
processes. If we are ever starving, our body will certainly react to this
threat and use our fatty energy stores to respond and sustain life at all
costs.

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

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MODULE 8

Lipolysis in Popular Culture

As briefly mentioned above, a fun fact is that lipolysis has become a

popular term in the cosmetic world. Not to be confused with the adipose
lipolysis pathways detailed in this article, laser lipolysis and even
injection lipolysis are clinically proven methods of reducing the number
of fat cells without liposuction surgery. Noninvasive fat reduction has
become a new cosmetic staple, and promises to target fat cells through
the use of heat, cooling (via lasers or radiofrequencies), or less
commonly deoxycholic acid injections without disrupting surrounding
tissues.
Assessment :

1. Which of the following enzymes is the rate determining enzyme in lipolysis?

A. HSL
B. ATGL
C. MGL
D. None of the above

2. Which of the following will induce lipolysis?

A. High insulin/Low epinephrine
B. High insulin/High epinephrine
C. Low insulin/High epinephrine
D. Low insulin/Low epinephrine

3. discuss the process involve in lipid synthesis

4. compare and Contrast Lipid synthesis from lipolysis

TOPIC: LIPID CHEMISTRY AND METABOLIC PATHWAYS

Descriptive Title: BIOCHEMISTRY

Instructor: SUSANA N. PE