Professional Documents
Culture Documents
THE PRINCIPAL
THE NATURE OF
01 03 COMPOUNDS OF
METABOLISM CATABOLIC PATHWAYS
Catabolism is a Anabolism is a
process of breaking process of
down molecules to synthesizing
(building up)
supply energy.
molecules.
METABOLIC REACTIONS INTO TWO BROAD
GROUPS:
➢ The main outlines of metabolic pathways are
well known and, in some cases, have been
known for decades. Molecular biology is
developing a new layer of understanding of
the topic by seeing how signaling
mechanisms and genetic control play a large
part in determining the physiological state of a
cell. Cancer cell growth, circadian rhythms,
and longevity are affected by the metabolism
of cells.
➢ To focus on cancer, we know that genes which
promote cancer (onco-genes) and mutations in genes
that suppress cancer (tumor suppressor genes) can
shift metabolic patterns to those characteristic of tumor
cells from those found in normal cells.
➢ For example, It has been known for decades that
when cancer cells metabolize sugars, the products do
not enter the normal metabolic pathways. Instead, the
intermediates are used in ways that aid uncontrolled
cell growth, which is a characteristic of cancer cells.
A BIOCHEMICAL PATHWAY
+ H2PO4 + 7.3
kcal
Dihydrogen
phosphate ion
➢ AMP, ADP, and ATP all contain adenosine
connected to phosphate groups. The only
difference between the three molecules is the
number of phosphate groups. On the (Figure
26.5), each phosphate is attached to the next by
an anhydride bond. ATP contains three
phosphates, one phosphoric ester and two
phosphoric anhydride bonds. In all three
molecules, the first phosphate is bonded to the
ribose by a phosphoric ester bond.
➢ A phosphoric anhydride bond contains more chemical
energy (7.3 kcal/mol) than a phosphoric ester bond (3.4
kcal/mol). Thus, when ATP and ADP are hydrolyzed to
yield phosphate ion, they release more energy per
phosphate group than does AMP. When one phosphate
group is hydrolyzed from each, the following energy yields
are obtained: AMP=3.4 kcal/mol; ADP=7.3 kcal/mol;
ATP=7.3 kcal/mol). (The PO43 -- ion is called inorganic
phosphate). Conversely, when inorganic phosphate bonds
to AMP or ADP, greater amounts of energy input are
required than when it bonds to adenosine. ADP and ATP
contain high-energy phosphoric anhydride bonds.
➢ ATP releases the most energy and AMP releases the least energy
when each gives up one phosphate group. This property makes
ATP a very useful compound for energy storage and release. The
energy gained in the oxidation of food is stored in the form of
ATP, albeit only for a short while ATP molecules in the cells
normally do not last longer than about 1 minute. They are
hydrolyzed to ADP and inorganic phosphate to yield energy that
drives other processes, such as muscle contraction, nerve signal
conduction, and biosynthesis. As a consequence, ATP is
constantly being formed and decomposed. Its turnover rate is
very high. Estimates suggest that the human body manufactures
and degrades as much as 40 kg (approximately 88 lb) of ATP
every day. Even with these considerations, the body is able to
extract only 40 to 60% of the total caloric content of food.
B. AGENTS FOR TRANSFER OF ELECTRONS IN
BIOLOGICAL OXIDATION-REDUCTION
REACTIONS
➢ Two other actors in this drama are the
coenzymes NAD+ (nicotinamide adenine
dinucleotide) and FAD (flavin adenine
dinucleotide), both of which contain an ADP
core. The + in NAD+ refers to the positive
charge on the nitrogen. In NAD+, the
operative part is the flavin portion.
For example, when NAD+ is reduced, the
nicotinamide part of the molecule gets reduced:
The reduced form of NAD+ is NADH. The same reduction
happens on the two nitrogens of the flavin portion of FAD:
The Structures of NAD+ and FAD
C. AGENT FOR TRANSFER OF ACETYL GROUPS
➢ The final principal compound in the common catabolic
pathway is coenzyme A, is the acetyl-transporting
molecule. Coenzyme A also contains ADP, but here the
next structural unit is pantothenic acid, an other B
vitamin. Just as ATP can be viewed as an ADP molecule to
which a —PO3^2- group is bonded by a high-energy
bond, so can acetyl coenzyme A be considered a CoA
molecule linked to an acetyl group by a high-energy
thioester bond, for which the energy of hydrolysis is 7.51
kcal/mol. The active part of coenzyme A is the
mercaptoethylamine. The acetyl group of acetyl
coenzyme A is bonded to the SH group.
The Structure of
the Coenzyme A
THE CITRIC ACID CYCLE AND
IN METABOLISM 04
➢ The common catabolism of
carbohydrates and lipids begins when
they have been broke down into
molecules of two carbon atoms each.
08
OTHER FORMS
➢ The storage of chemical
energy in the form of ATP
lasts only a short time.
Usually, within a minute, the
ATP is hydrolyzed (an
exothermic reaction) and
releases its chemical energy.
➢ A. Conversion to Other Forms of Chemical Energy
The activity of many enzymes is controlled and regulated
by phosphorylation. For example, the enzyme
phosphofructokinase (PFK-2), which catalyzes the formation
of fructose-2,6-bisphosphate, (chemical connections 22E), a
key allosteric effector in the glycolytic pathway that
catabolizes glucose is activated by phosphorylation. When
ATP transfers a phosphate group to a serine residue, the
enzyme becomes active. Thus, the chemical energy of ATP is
used in the form of chemical energy to activate PFK-2 so that
glucose can be metabolized.
B. Electrical Energy
The body maintains a high concentrations of K+ ions inside its
cells despite the fact that the K+ concentration is low outside the
cells. The reverse is true for Na+. So that K+ does not diffuse out of
the cells and Na+ does not enter them, special transport proteins
in the cell membranes constantly pump K+ into and Na+ out of the
cells. This pumping requires energy, which is supplied by the
hydrolysis of ATP to ADP. Because of this pumping, the charges
inside and outside the cell are unequal, which generates an
electric potential. Thus, the chemical energy of ATP is
transformed into electrical energy, which operates in
neurotransmission.
C. Mechanical Energy
ATP is the immediate source of energy in muscle contraction.
In essence, muscle contraction takes place when thick and thin
filaments slide past each other. The thick filament is myosin, an
ATPase enzyme (that is, one that hydrolyzes ATP). The thin
filament, actin, binds strongly to myosin in the contracted state.
However, when ATP binds to myosin, the actin-myosin complex
dissociates, and the muscle relaxes. When myosin hydrolyzes ATP,
it interacts with actin once more, and a new contraction occurs. In
this way, the hydrolysis of ATP drives the alternating association
and dissociation of actin and myosin and consequently, the
contraction and relaxation of the muscle.
D. Heat Energy
One molecule of ATP upon hydrolysis to ADP yields 7.3
kcal/mol. Some of this energy is released as heat and used to
maintain body temperature. For example, if we estimate that
the specific heat of the body is about the same as that of
water, a person weighing 60 kg would need to hydrolyze
approximately 99 moles (approximately 50 kg) of ATP to raise
the temperature of the body from room temperature, 25°C to
37°C. Not all body heat is derived from ATP hydrolysis; some
other exothermic reactions in the body also make heat
contributions.
➢ In the thin filament of skeletal muscle fiber, a small globular protein that masks
the active sites on the actin, is “troponin”. The thin filament of skeletal muscle fiber
is composed of three distinct proteins, i.e. actin, tropomyosin, and troponin.
Troponin inhibits the actin-myosin interaction. The binding of calcium to the
troponin unmasks the myosin binding active sites on actin. Tropomyosin is a
fibrous molecule that attaches to actin in the groove between its filaments. G-actin
is the monomer of the actin filament.
ATP in Cell Signaling
➢ In recent years, research has made it clear that
ATP and its derivatives act in cell signaling.
Receptors for ATP, ADP, AMP, and adenosine
bind all these molecules and set off the type of
cascade. Vesicles in the ATP-releasing cell fuse
with the cell membrane, releasing ATP into the
intercellular medium. Enzymatic reactions
catalyze the hydrolysis of ATP to ADP, then to
AMP, and finally to adenosine. In the target cell,
ATP binds to the P2X receptor. Both ATP and
ADP bind to the P2Y receptor. AMP and
adenosine bind to the P1 receptor.
ATP in Cell Signaling
➢ The effect in the cell is frequently the release of
calcium ion from intracellular reservoirs, leading
to the activation of key enzymes that trigger a
number of responses, including effects on the
nervous system and blood vessel dilation.
Research is in progress to find other
health-related applications of cell signaling.
One example already in existence is the drug
clopidogrel, which blocks ATP receptors on
platelets to prevent clot formation in blood
vessels. Other drugs that can be used for pain
management by their effects on ATP receptors
are in various stages of development.
SALAMAT!
REFERENCES
Bettelheim, F.A., Brown, W.H., Campbell, M.K., Farrell, S.O., & Torres, O. (2019). Introduction to General, Organic,
and Biochemistry (12th ed.). Cengage Learning.
Adobe Stock. (n.d.). Flavin adenine dinucleotide (FAD) redox enzyme molecule. Skeletal System. Retrieved from
https://stock.adobe.com/images/flavin-adenine-dinucleotide-fad-redox-coenzyme-molecule-skeletal-formula/1
71660456
Omote, H. & Moriyama, Y. (2013). Vesicular neurotransmitter transporters: an approach for studying transporters
with purified proteins. Semantic Scholar.
https://www.semanticscholar.org/paper/Vesicular-neurotransmitter-transporters%3A-an-for-Omote-Moriyama
/36ed5ddfe0e29db6ed73e71df2b21383d7bab6fd
REFERENCES
Slide Serve. (2013). What is Bioenergetics?. Retrieved from
https://www.slideserve.com/talitha/what-is-bioenergetics
Eldridge, L. (2023). Cancer Cells vs. Normal Cells: How Are They Different?. Verywell health.
https://www.verywellhealth.com/cancer-cells-vs-normal-cells-2248794
Madhu. (2018). Difference Between Acetyl Coa and Acyl CoA. Difference Between.
REFERENCES
Franca-Neto, J.D.B. & Krzyzanowski, F.C. (2019). Tetrazolium: an important test for physiological seed quality
evaluation. Journal of Seed Science.
The Editors of Encyclopedia Britannica. (2023). Sir Hans Adolf Krebs. Article History.