− Process of synthesizing your biomolecules

BIOMOLECULES − Remove water molecule

Biomolecule − Dehydration removes water molecule, forming a bond
− Short polymer: not yet a biomolecule
• Lipids − Ho and H is remove to form H2O
• Proteins − Energy in form ATP stays in the bonds
• Nucleic acid − Longer polymer: stored energy
• Carbohydrates
Hydrolysis
Biomolecule-molecules found in your cell
− Adds water molecule to break the bonds
Macromolecules − Add water molecule to break bonds
− Energy will rise and go away
− known as biomolecules
− breaks a chemical bond between two molecules and
− main compound elements are carbon, hence or organic
involves the use of a water molecule.
molecule
− mainly made by strong covalent bond(except lipids)
Take note:
− all of them have covalent bond
Energy only stays at the bond, when the bond is gone it
− monomer: building blocks of fats will also be gone.
POLYMERS AND MONOMERS
− Water molecules separated
1) Polymers − Enzyme-catalize and fasten up
− this is your macromolecules − Requires enzyme
− are built from your monomers
− building blocks of carbohydrates, protein and DIVERSITY OF BIOMOLECULES
nucleic acid
− are large molecules which are formed by joining • Carbohydrates
many identical or very similar monomers
− Can be found in plants
together.
− Main function: as energy source and structural
− The 3 main polymers are: Carbohydrates -
supports
monomers are joined by glycosidic bonds
− Sugars and starches
Proteins - monomers are joined by peptide
− Minor: structural support
bonds
− Structural: cellulose and Chitin
Lipids - monomers are joined by ester bonds
− Made entirely of carbons, hydrogen and oxygen
2) Monomers − Provides calories or energy and simple sugars
− smaller units from which larger molecules
aremade. Carbon:
− Monosaccharides, amino acids and nucleotides − 18% body by weight
are examples − form four covalent bonds
− small, identical or similar molecules, that can be − can form single or double bonds
joined together to make 2 TYPES OF CARBOHYDRATES:
larger molecules
− Nucleic acids, amino acids, α&β glucose, 1. Simple Sugars
fructose, fatty acids and glycerol are all − Little ring shaped molecules made of carbon,
examples of monomers hydrogen and oxygen
− It is either alone or in pairs
2. Complex Carbohydrates
− Formed when these rings link up together to
Building Blocks: make long chains
• proteins-amino acid Saccharides- this are the sugars
• carbohydrates-monosaccharides
• nucleic acids- nucleotide SUGARS
• lipid- glycerol and fatty acid
− Found naturally in plants like fruits, vegetables and grain
did you know? as as animal products like milk and cheese
− Added Sugars are the sugars that get added to foods like
Polymers except lipid cereals, ketchup, energy bars and salad dressings
built from monomers: − it actually refers to a family of molecules called
SACCHARIDES
• Carbohydrates
You can Write carbohydrates by:
• Proteins
• Nucleic acids • Linear
• Ring form

From not polymers: • Glucose: readily recognized and used as source energy
• Fishcer form: linear form of sugar
• Lipids
2 Kinds of Simple Sugars:
Dehydration reaction
1) Monosaccharides − Found in molasses that can be used as substrate
− Simple sugars to ferment beer
− CH2O DID YOU KNOW?
− Carbonyl group( C=O) and multiple hydroxyl groups (-
OH) ❖ Sugars like fructose for example are most always found in
− Mono means “one” combination with other sugars and combination can be
− One sugar molecule pretty different even in seemingly similar foods.

Classfication of Monosaccharides Synthesis for Maltose

− location of the carbonyl group(C=O) − Made up of glucose and glucose

− Size of carbon skeleton − GH and H are removed then transform into H2O
− They are removed so that they have available area for
Did you know? linking
• 6 carbon-hexose − Process of dehydration then it is now maltose
• 3 carbon-triose − Bonding: alpha- 1,4 glyosidic bond
• No known sugar that has four carbon − alpha because it is linear
1) Location of carbonyl group − clockwise
− Aldoses(aldehyde sugars) Dehydration Reaction for Sucrose
− Carbonyl group at end of carbon skeleton
− Ketoses(ketone sugar) ❖ Glucose
− Trioses: 3-carbon sugars(C3H6O3) -the most important member of the sugar family
• Glyceraldehyde-an initial breakdown product of glucose -one of the main sources of calories for body
• Dihydroxyacetone- an initial breakdown product of -able to cross the blood brain barrier and
glucose nourish the brain
2) Size of carbon skeleton - is a hexose sugar (a monosaccharide) which has six
• Hexoses: 6(carbons yards (C6H12O6) carbon atoms in each molecule.
-The two types of glucose are alpha (α) and beta (β).
❖ Galactose -alpha and beta are isomers, which means
- energy sources of organisms they have the same molecular formula, but the atoms are
-known as milk sugar connected in a different way.
-only found in nature when it links with glucose to form -a monomer
LACTOSE − bonding: alpha- 1,2 glyosidic bond
❖ Fructose − counterclockwise
-an energy source for organisms
TAKE NOTE:
-Commonly found in honey, fruits and root vegetables
• Additional Info/ addition function for − pentose sugar: Counterclockwise
monosaccharides: − heptose sugar: clockwise
− Cellular respiration
− Carbon skeletons serve as raw material for synthesis For Lactose:
of other
− main carbohydrate present in dairy products
Types of small organic molecules: − glucose + galactose
− bonding: beta- 1,4 glyosidic bond
• Glucose, fructose, galactose-components of complex − hydrolysis-broken down into 2 monosaccharides
sugar −
• Ribose and deoxyribose- components of nucleic acid
2) Disaccharides DID YOU KNOW?
− Two monosaccharides joined by a glyosidic linkage or • Simple sugars Whether they’re natural or added are
bond mixtures of monosaccharides or disaccharides
− Di means “two”
− Two sugar molecule linked together THE COMPLEX CARBOHYDRATES INCLUDE:

Glycosidic bonds is a form of covalent bonds 3) Polysaccharides

• Sucrose: Glucose + fructose − complex carbohydrates

− table sugar − architecture and function
− its formed when fructose links up with glucose sugar monomers
− found in various fruits and vegetables with sugar positions of its glyosidic linkages
cane and sugar beets having the HIGHEST − storage:
QUANITITY starch and glucose
• Maltose: Glucose + Glucose − Structural:
− Rice Chitin
− Two glucose molecules linked together Cellulose
− Found in molasses that can be used as substrate − Dehydration process involved 10 or more sugars
to ferment beer molecules are linked together
• Lactose: Glucose + galactose − Larger chain with branches
− Dairy Products − Most abundant type of carbohydrates found in food
− Two glucose molecules linked together • Starch
− Plants
 − Polymer of glucose monomers -sucrase, maltase breakdown lactose, sucrose and
− Joined by alpha 1-4 glyosidic linkage maltose into their monosaccharides
− Within cellular structure known as plastids
Did you know?’
− Simplest form: Amylose
− Polysaccharides with molecular bond between The individual monosaccharides that result from digestion of
sugars molecule that human intestinal enzymes can larger carbohydrates molecules-glucose, fructose and
breakdown galactose goes into bloodstream to be used by body
− Important sources of calories
− Can be found in foods like rice, potatoes, wheat and Summary:
maize • Simple sugars are monosaccharides and disaccharides
− They don’t taste sweet because they don’t activate that body can readily absorbed
taste buds in same way as simple sugars • Starches are polysaccharides take longer to absorb
• Glycogen • Fibers are polysaccharides that body can only partially
− Liver(synthesize) absorbed with help of gut bacteria
− Muscle cells
− Fat cells
− Systemic and cellular energy source
• Cellulose
− A major component of tough walls that enclose plant
cells
− Structural support
− Fiber in foods (fiber is another term for roughage)
− Most abundant organic Compound on earth
• Chitin
− Major constituent in exoskeleton
− Arthropods
− Cell walls of fungi
− Anti-parallel sugar structure
− Twisted plywood or bioligand structure

MONOSACCHARIDES

− Link together through a glycosidic bond

− Glycosidic bond (OH from carbon on 1
monosaccharide bonds with H from carbon of
another monosaccharide and forms H2O)

GLYCOSIDIC BONDING

❖ MALTOSE
− Alpha,1-4, glycosidic bond
An alpha refers to fact that molecules lined up next to
one each other

❖ LACTOSE
− Beta 1-4, glycosidic bond
− 1 carbon of lactose on the other hand has beta 1-4
glycosidic bond, carbon 4 or glucose are bonded)
− This time molecules are stacked with one higher than
the other

❖ SUCROSE
− Alpha, 1-2 glycosidic bond
− Carbon 1 of glucose and carbon 2 of fructose are
bonded)

Did you know?

➢ Enzymes start breaking down disaccharides,

oligosaccharides and polysaccharides into
monosaccharides so they can be absorbed

DIFFERENT ENZYMES HELP TO BREAK DIFFERENT LINKAGES:

• Amylases
-breakdown large polysaccharides like starch into smaller
units
• Lactase
 cysteine lysine Tyrosine
Glutamic acid methionine Valine
glutamine Phenylalanine

DIFFERENT GROUPS OF AMINO ACID:

• Non-Essential Amino Acids

− 5 amino acids: alanine, asparagine, aspartic acid,
glutamic acid, serine
− are we can get from foods and we can get from
ourselves
• Conditionally Essential
− Healthy bodies can make them under normal
circumstances
− Arginine, cysteine. Glutamine, glycine, proline and
tyrosine
− We can’t make them in cases like starvation or certain
inborn errors of metabolism
• Essential Amino Acid
− Can only get from food
− Histidine, isoleucine, leucine, lysine, methionine,
phenylalanine, threonine, tryptophan and valine
− hose necessary for construction of proteins in the
body, although not produced by the body;

Did you know?

Dietary protein provides essential amino acids to make own

• PROTEINS
− Monomers: amino acid
− Long chains (polymers) of subunits called amino
acids(monomers)
− BONDING: Peptide Bonds
− Amino acids are joined by peptide bonds which are
produced by dehydration synthesis reaction
− DNA dictates amino acid
− found in variety of foods like eggs, dairy, seafood,
legumes, nuts and seeds
− gets broken down and reformed into new proteins in
our body
− is a chain of amino acids bound to one another by
peptide bonds
− gets broken down into amino acids peptide bonds
− gets twisted and folded into a protein shape
proteins, hormones and other important molecules
AMINO ACID STRUCTURE:
❖ Amino Group
- because of nitrogen
- one of several nitrogen-containing functional groups
found in organic molecules.
- the nitrogen atom is connected by single bonds to either
hydrogen or carbon
❖ Carboxyl Group
- because of carbon
- made up of one carbon (C) and two oxygen (O) atoms.
-has a negative charge and has lost its hydrogen (H) atom
- weak acids, dissociating partially to release hydrogen
ions.
-has both a carbonyl and a hydroxyl group attached to the
same carbon atom, resulting in new properties.

❖ R GROUP
• Amino Acids
− Building blocks of protein
− Contain nitrogen, carbon, hydrogen, oxygen
− There are naturally 20 of this occurring
− About half of this can be made by our body and about
half need to be consumed(bet.8-10 are essential)
− Have a central carbon atom bounded to one amino or
nitrogen containing group or one carboxylic acid
group
-chemical structure of your amino acid
-determines the characteristics (size, polarity, and pH) for
each type of amino acid.
- specific side chain
- which a carbon or hydrogen atom is attached to the rest
of the molecule.
- Sometimes used more loosely, to include other elements
such as halogens, oxygen, or nitrogen.

Did you know? Facts:

Carbon has one hydrogen atom and sidechain which is unique There are 20 amino acids, 20 r groups.
to each amino acid
Proteins are…
Humans only use 20 amino acids to make basically every type
of protein they include: − Made by ribosomes
− Joined together by peptide bonds following a sequence
alanine Glycine Proline dictated by DNA
arginine histidine Serine − The sequence of amino acid is dictated by DNA
asparagine isoleucine Threonine − 20 diff amino acids are encoded by DNA
Aspartic acid leucine Tryptophan
Did you know:
This is how your body uses amino acids as building blocks:
Amino acids-→reptide→polypeptide→protein
polypeptide chain folds to become a biologically active protein
in its native 3D structure
Folding of Polypeptide to form proteins:
• Shape of proteins are important because:
✓ This determines how they interact with other
molecules
✓ This determines their particular function
• C, H, O, N and S some have( a few might acs have P due to
addition of P in modification process, but P is nota
component of amino acids
• Insulin: C254H317N65O76S6
• Phosphorus will attach to your amino acids but later will
detach
Summary:
− Peptide bond
− Forms bet. Carboxyl end of one amino acid and
amino end of next amino acid
− two or more amino acids joined together by
peptide bonds
− Polypeptide
− A polymer of 3-100 amino acids
− a chain of many amino acids
− Protein
− A polypeptide longer than 100 amino acids that
has a complex structure and function peptide
bond linkage:
(always carboxyl-amino)
− H310 pertains to unlink amino acid
− TERMINICS: they will no longer accept amino
acid
− contains one or more polypeptides.
− are long chains of amino acids held together by
peptide bonds.
4 LEVELS STRUCTURE OF PROTEIN
− Primary Structure
− Amino acid sequence
− Stabilized by peptide bonds
− simply the sequence of amino acids in a
polypeptide chain
− the hormone insulin has two polypeptide chains,
A and B, shown in diagram below.
− Each chain has its own set of amino acids,
assembled in a particular order.
− the sequence of the A chain starts with glycine at
the N-terminus and ends with asparagine at the
C-terminus, and is different from the sequence of
the B chain
Did you know?
• The sequence of a protein is determined by the DNA of the
gene that encodes the protein A change in the gene's DNA
sequence may lead to a change in the amino acid sequence
of the protein. Even changing just one amino acid in a
protein’s sequence can affect the protein’s overall
structure and function.
− Secondary Structure
− Alpha helix(twisting)
− Beta pleated sheets(turning)
− refers to local folded structures that form within
a polypeptide due to interactions between atoms
of the backbone.
− most common types of secondary structures are
the α helix and the β pleated sheet.
− Both structures are held in shape by hydrogen
bonds, which form between the carbonyl O of
one amino acid and the amino H of another.
− in an α helix, the carbonyl (C=O) of one amino
acid is hydrogen bonded to the amino H (N-H) of
an amino acid that is four down the chain. (E.g.,
the carbonyl of amino acid 1 would form a
hydrogen bond to the N-H of amino acid 5.)
− This pattern of bonding pulls the polypeptide
chain into a helical structure that resembles a
curled ribbon, with each turn of the helix
containing 3.6 amino acids.
− he R groups of the amino acids stick outward
from the α helix, where they are free to interact
− In a β pleated sheet, two or more segments of a
polypeptide chain line up next to each other,
forming a sheet-like structure held together by
hydrogen bonds.
− he hydrogen bonds form between carbonyl and
amino groups of backbone, while the R groups
extend above and below the plane of the sheet
− Certain amino acids are more or less likely to be
found in α-helices or β pleated sheets.
Did you know?
Proline is typically found in bends, unstructured regions
between secondary structures
− Tertiary Structure
− Three-dimensional shape
− Creates polar and non-polar areas in molecule
− Stabilized by disulfide and hydrogen bonds
− Side chain(R-group) interaction
− Folding polypeptide
− R Group: disulfide and hydrogen
− Disulfide may be present or not depends on
amino acids
− It’s a functional structure
 − primarily due to interactions between the R
groups of the amino acids that make up the
protein.
− R group interactions that contribute to this
include hydrogen bonding, ionic bonding, dipole-
dipole interactions, and London dispersion forces
– basically, the whole gamut of non-covalent
bonds.
− Ex:, R groups with like charges repel one another,
while those with opposite charges can form an
ionic bond.
− Also important this are hydrophobic
interactions, in which amino acids with nonpolar,
hydrophobic R groups cluster together on the
inside of the protein, leaving hydrophilic amino
acids on the outside to interact with surrounding
water molecules. DENATURATION
− Permanent disruption of protein structure
− Can be damaged by temperature or changes in ph
− Leads to loss of biological function
− 41 o above
− At normal human body temperature
− Loss of biological activity
− involves the disruption and possible destruction of
both the secondary and tertiary structures.
− Since denaturation reactions are not strong enough
to break the peptide bonds, the primary structure
(sequence of amino acids) remains the same after a
denaturation process.
− the alteration of a protein shape through some form
− Quaternary Structure of external stress (for example, by applying heat,
− Two or more polypeptide chains are associated. acid or alkali), in such a way that it will no longer be
− some proteins are made up of multiple able to carry out its cellular function.
polypeptide chains, also known as subunits.
When these subunits come together, they give
the this
− hemoglobin is an example
− DNA polymerase, is also an example where an
enzyme that synthesizes new strands of DNA and
is composed of ten subunits

ROLES OF PROTEIN/ FUNTION

1) CATALYST (enzymes)
− Lipose is an example
− Breakdown of fats
− Enzymes work for metabolism
− Fatty acids and glycerol
− Metabolism
− Enzymes are the proteins that regulate biochemical
processes.
− they function to lower the activation energy of the
reaction and thereby increases the rate of the
reaction
− that increase the rate of virtually all the chemical
reactions within cells
− most biological reactions are catalyzed by proteins

2 types of metabolism:\
1) Anabolism
− refers to a state in skeletal muscle tissue
where synthesis exceeds degradation, and
thus lean tissue is being built.
 − builds complex molecules from simpler 3.2 STRUCUTRAL ( Histone)
ones
− the process by which the body utilizes the − major structural proteins of chromosomes
energy released by catabolism to synthesize − the DNA molecule is wrapped twice around a Histone
complex molecules. Octamer to make a Nucleosome.
− These complex molecules are then utilized − Six Nucleosomes are assembled into a Solenoid in
to form cellular structures that are formed association with H1 histones.
from small and simple precursors that act − The solenoids are in turn coiled onto a Scaffold, which is
as building blocks futher coiled to make the chromosomal matrix.
− Histone is positively charged while DNA is negatively
charged that’s why they attract
− PROCESS:
2) Catabolism
1) DNA will wrap to histone proteins
− refers to a state in skeletal muscle tissue
2) Histone wrap around DNA so that it will be compact
where degradation exceeds synthesis, and
and be in nucleus
thus lean tissue is being broken down
3) If histone isn’t compacted, it can’t change the DNA
− breaks large molecules into smaller ones.
− include breaking down and oxidizing food
molecules.
− to provide the energy and components 4.1 TRANSPORT ( Haemoglobin)
needed by anabolic reactions.
− Transports oxygen and found in red blood cells
− Iron is the element we can find in Hemoglobin
2) REGULATION ( Hormones)
− The iron is where oxygen binds
− An example is insulin
− Lack of iron leads to anemia and iron deficiency
− Insulin: C254H377N65O76S6
− It is composed of four protein chains, two alpha
− Insulin converts sugar to energy that issue by body
chains and two beta chains, each with a ring-like
− Negative feedback heme group containing an iron atom.
− hormones are released, either directly by an − Oxygen binds reversibly to these atoms and is
endocrine gland or indirectly through the action of transported through blood.
the hypothalamus of the brain, which stimulates
− The structure of the this molecule is essential to its
other endocrine glands to release hormones in order
function, which is carrying oxygen around the body.
to maintain homeostasis.
− Other hormones that can work:
 Primary Structure
o Calcitonin
− At its simplest level, hemoglobin is made up
− Calcium
of amino acids stuck together in chains.
− involved in helping to regulate levels of
− These chains are polypeptides that are also
calcium and phosphate in the blood,
stuck to a heme molecule, which is where
opposing the action of parathyroid
the oxygen will eventually stick.
hormone
− Hemoglobin is different than other proteins
− reduces calcium levels in the blood by two
because its individual polypeptides, of
main mechanisms: It inhibits the activity of
which there are four, are called globins
osteoclasts, which are the cells responsible
instead of simply protein subunits.
for breaking down bone.
o Secretin
 Secondary Structure
− PH in digestive system
− The most common secondary protein
− is a hormone that controls parts of the
structures are the alpha helix and the beta-
digestive system and maintains water
pleated sheet,
balance in the body.
− and each globin contains eight alpha
− It's released by the duodenum, the upper
helices.
part of the small intestine.
− The alpha helices are a result of each globin
− Ph refers to concentration of acid
interacting with itself to form stable
− (1) inhibiting the secretion of gastric acid structures.
from the parietal cells of the stomach and
− (2) stimulating the production of
 Tertiary Structure
bicarbonate from the ductal cells of the
− Tertiary structure describes how each
pancreas.
globin bends in space.
− The heme molecule is important for the
3.1 STRUCTURAL ( Keratin)
tertiary bending structure of hemoglobin, as
− Can be find in hair and nails − it helps twist the globins into shape by
− the protein that protects epithelial cells from damage or connecting to histidine residues on them.
stress.
− Those who have more curly hair have lots of keratin
 Quaternary Structure
− Has a presence of disulfide bonds
− Of the four globins that make up
− Disulfide bonds make the hair curlier
hemoglobin, two are identical and called
− re also a cytoskeletal component of desmosome cellular
alpha chains,
junctions.
− and the other two are called beta chains
− highly cross-linked proteins typically containing α-helix
and are also identical.
and β-sheet motifs and are high in glycine and alanine
− They can also be called alpha-globins and
content.
beta-globins.
 − The quaternary structure of hemoglobin is
these units fitting together.
4.2 TRANSPORT ( Protein channels or carrier proteins)
− Protein channels and carrier proteins allow
transport of specific substance across cell
membrane
− channel proteins are exactly what they sound
like – proteins that open channels in the cell
membrane, allowing molecules to flow in and
out along their concentration gradient
− carrier proteins are only open to one side of the
membrane in question at a time.
− Carrier proteins are glycoproteins,
− whereas channel proteins are lipoproteins.
− Carrier proteins have solute-bound
conformations
5. IMMUNITY ( Antibodies)
− Antibodies=immunoglobin (lg)
− Antibodies are involved in adaptive immunity
− also called immunoglobulin,
− a protective protein produced by the immune
system in response to the presence of a foreign
substance, called an antigen.
− recognize and latch onto antigens in order to remove
them from the body.
− Antibodies are proteins produced by the body to
neutralize or destroy toxins or disease-carrying
organisms.
− Antibodies are disease-specific.
6. CONTRACTILE ( Actin and Myosin)
− Involve in muscle contraction and relaxation
− If muscle contracts-it slides(the actin and myosin)
− Actin participates in many important cellular
processes, including muscle contraction, cell motility,
cell division and cytokinesis, vesicle and organelle
movement, cell signaling, and the establishment and
maintenance of cell junctions and cell shape.
− Myosins are a large super-family of motor proteins
that move along actin filaments, while hydrolyzing
ATP to forms of mechanical energy that can be used
for a variety of functions such as muscle movement
and contraction.
− Myosin is the most abundant contractile protein and
consists of two heavy and four light chains.
− Muscle contraction thus results from an interaction
between the actin and myosin filaments that
generates their movement relative to one another.
The molecular basis for this interaction is the binding
of myosin to actin filaments, allowing myosin to
function as a motor that drives filament sliding.
7. SURFACE RECEPTORS
− All receptors are attached to your cell membrane
− Receives molecule/stimuli from outside
− Send signal inside cells
− Receptors are also called cell-cell communication
➢ ENZYMES
− Are very specific for what they will catalyze;
− Will only work for specific substrate
− Usually end in -ase, ligase, sucrase
− Used only temporarily; can be used again for
biochemical reaction with other
molecules/reusable
− Very little enzyme needed to help in many
reactions
− biological molecules (typically proteins) that
significantly speed up the rate of virtually all of
the chemical reactions that take place within
cells.
− Substrate complex
− The substrate an enzyme acts on is called
substance reactant
− Substrate binds to enzyme that is the active site
− They are vital for life and serve a wide range of
important functions in the body, such as aiding
in digestion and metabolism.
− specialized class of proteins responsible for
catalyzing chemical reactions within the cell and
thus are ideal drug targets.
WHAT ARE ENZYMES?
• The substance an enzymes acts on is called SUBSTRATE
(reactant)
• Without enzymes, many biochemicals reactions would
not proceed quickly enough to sustain life
• Maintenance of homeostasis is critical, in order to
maintain the shape and biologic activity of enzymes
HOW DO ENZYMES WORK?
• Enzymes work by weakening bonds which lowers
activation energy
ACTIVE SITE
− A restricted region of an enzyme molecule in which a
substrate will bind
− Induced fit in the presence of substrate
− A change in shape and configuration of an enzyme’s
active site ( H+ and ionic bonds are involved)
− Hydrogen and ionic bonds are weak bonds
What affect enzyme activity:
1) Environmental conditions
2) Cofactors and coenzymes
3) Enzyme inhibitors
1) ENVIRONMENTAL CONDITIONS
I. Extreme temperature are the most dangerous
− High temperatures may denature(unfold)
the enzyme
II. pH (most like 6-8 pH near neutral)
III. Ionic concentration
▪ TEMPERATURE
*affects the rate of enzyme activity
a) Optimum temperature
− Greatest number of collisions between
enzyme and substrate
− Human enzyme
− 35o- 40o C (body temp. 37o)
 b) Raise Temperature
− Denature protein=unfold and loose its
shape
c) Lower temperature 1o
− Molecules move slower
− Fewer collisions between enzyme and
substrate
2) COFACTORS AND CONENZYMES
− Inorganic substances (zinc, ion and vitamins
respectively) are sometimes need for proper
enzymatic activity
• Ex. Iron must be present in quaternary structure-
hemoglobin for pick up oxygen
• Ex. Vitamin A, B1(conenzymes)
Steps:
1. Without cofactors attached, the protein is not active
2. Cofactor bonding activates protein
• Apoenzymes
− inactive form of enzymes, are still able to
bind substrate with an affinity comparable
to holoenzyme, but they are not able to
transform substrate into product
− The binding of substrate to this may result
in a conformational change that can be
easily detected by fluorescence
measurements.
• Cofactor
− serve the same purpose as coenzymes, as
they regulate, control, and adjust how fast
these chemical reactions would respond
and take effect in our body.
− Inorganic substance
• Coenzyme
− serve the same purpose as cofactor, as they
regulate, control, and adjust how fast these
chemical reactions would respond and take
effect in our body.
− are organic substances
3) ENZYME INHIBITORS
2 TYPES:
 Competitive Inhibitors
− Chemicals that resembles an enzyme normal
substrate and compete with it for active site
− Inhibits activity of your enzymes
− inhibitor that occupies the active site of an
enzyme or the binding Site of a receptor and
prevents the normal substrate or ligand from
binding.
− the inhibitor binds directly to the active site
of the enzyme. This therefore prevents the
substrate from binding to the enzyme and
forming the enzyme-substrate complex.
− It is directly competing with the substrate.
• Examples:
♣ Cyanide-cytochrome (oxidase)
-used for atp production
♣ antineoplastic drug methotrexate
Methotrexate has a structure similar to that
of the vitamin folic acid
 Non-competitive Inhibitors
− Inhibitors that do not enters the active site
but bind to another part of the enzyme
causing the enzyme to change its shape which
in turn alters the active site
− to change the shape of the enzyme and thus
the active site, so that the substrate can no
longer interact with the enzyme to give a
reaction.
− involves reversible binding of the inhibitor to
an allosteric site, but it is possible for the
inhibitor to operate via other means including
direct binding to the active site.
• Nucleic Acid
2 types of nucleic acid
▪ DNA: Deoxyribonucleic Acid
▪ RNA: Ribonucleic Acid
❖ NUCLEOTIDES
− Building blocks(monomers) of nucleic acid\
− Composed of phosphate sugar, sugar and
nitrogenous base
• 5 Carbon Sugar
− Deoxyribose (In DNA)
− Ribose (In RNA)
− the sugars found in nucleic acids are
pentose sugars; a pentose sugar has five
carbon atoms. A combination of a base and
a sugar is called a nucleoside.
DID YOU KNOW?
− Phosphodiester bond links the nucleotide to another
− the phosphodiester bond is the linkage between the
3' carbon atom of one sugar molecule and the 5'
carbon atom of another, deoxyribose in DNA and
ribose in RNA.
• DNA (Deoxyribonucleic acid)
− Double stranded helix
− Contains:
Phosphate group
Deoxyribose sugar
Nitrogenous Base
− Nitrogenous base contains: Adenine, Guanine,
Cytosine and Thymine
DID YOU KNOW?
The complementary base pairing in your DNA is
Adenine=Thymine and Guanine=Cytosine
• RNA (Ribonucleic Acid)
− Single stranded
− Nucleotides contain:
Phosphate group
Ribose sugar
Nitrogenous Base
DID YOU KNOW?
ATP is always nucleotide and never nucleic acids
➢ ADENOSINE TRIPHOSPHATE (ATP)
*The structure and function of adenosine
triphosphate
− Nucleotide adenosine triphosphate not
nucleic acid
− Universal source of energy
 − Bonds between phosphate groups contain
potential energy
− Breaking bonds releases energy
− ATP to ADP+P+Energy
Did you know?
• ATP is nucleotide because it is composed of phosphate
group, ribose sugar and nitrogenous base
• You need to breakdown energy to breakdown ATP
• Extraction of ATP by hydrolysis(breaking bond in
phosphate group
• Mitochondria contains DNA
 Lipids
− Insoluble in water or hydrophobic
− Insoluble in H2O
− Soluble in Benzene
− Lipid Dents:
Chloroform
Ether
Acetone
3 CLASSIFICATIONS OF LIPIDS:
1. Triglycerides
− Energy storage molecule
− When you eat, your body converts any calories
it doesn't need to use right away into
triglycerides.
− the most common type of fat in your body.
− They come from foods, especially butter, oils,
and other fats you eat.
− These are the calories that you eat, but your
body does not need right away.
− Your body changes these extra calories into
triglycerides, and stores them in fat cells.
− When your body needs energy, it releases the
triglycerides.
− Having a high level of triglycerides can raise your
risk of heart diseases, such as coronary artery
disease.
2. Phospholipids
− Cell membrane structure
− Are derivatives of triglycerides. They're very
similar to them but slightly different on a
molecular level.
− Half of each molecule is water-soluble and the
other is not, which causes them to react
differently than triglycerides.
− Located on cell membranes, they form double-
layered membranes with the water-soluble
molecules on the outside of the cell membrane
and the water-insoluble molecules in the inside.
− These lipids are responsible for protecting and
insulating cells.
3. STEROIDS
− Carbon based ring structure
− Steroids are a type of lipid that includes
hormones and cholesterol.
− It falls under lipids level because they share
common charcateristics, being hydrophobic
THE EXAMPLES ARE:
1. Cholesterol
−
− is produced by the body and consumed
through food, and it plays a role in the
production of hormones.
− Cholesterol, the most abundant steroid lipid
in the body, is required in every cell in the
body. It plays a role in cell repair and the
formation of new cells.
− However, too much cholesterol is a bad
thing. When it combines with other
compounds in your blood, it can build up as
plaque in your arteries, blocking blood flow
to and from the heart.
− Having a high cholesterol level increases
your risk of cardiovascular disease.
−
It derives hormones, vit D and bile salts
2. Hormones
− include the sex hormones estrogen and
testosterone, as well as your other
hormones like adrenaline, cortisol and
progesterone.
− Derive from cholesterol
− Your estrogen and testosterone
3. Vitamin D
− Cholecalciferol
− For bone and teeth structure
− is important for the absorption of calcium
from the stomach and for the functioning of
calcium in the body.
− Cholecalciferol is used to treat or prevent
many conditions caused by a lack of vitamin
D, especially conditions of the skin or bones.
4. Bile Salts
− are made of bile acids that are conjugated
with glycine or taurine.
− They are produced in the liver, directly from
cholesterol.
− are important in solubilizing dietary fats in
the watery environment of the small
intestine
− for digestion and fats
OTHER LIPID DERIVED SUBSTANCES
1. Soaps and Detergent
− Has an Alkyl chains longer than eight carbons
2. Waxes
− Esters of fatty acid with ion chains monohydric
carbon
DIFFERENT WAXES
• Bees Wax- lip gloss, lip balm, hand creams, moisturizer
• Spermaceti- pomades, ointments, wax candle(from
sperm whales)
• Carnauba Wax- automobile wax, shoe and floor polishes,
and from wax levels of Copernican prunitein
CELL RESPIRATION
 Aerobic and anaerobic, fermentation are under
catabolic pathways.
CATABOLIC PATHWAYS
-Released stored energy by breaking down complex molecule
-are those that generate energy by breaking down larger
molecules - involve
the degradation of complex molecules into simpler ones,
releasing the chemical energy stored in the bonds of those
molecules. -Some catabolic pathways can capture
that energy to produce ATP, the molecule used to power all
cellular processes
• AEROBIC RESPIRATION
-Oxygen is consumed as reactant
-most efficient
-utilize food
energy with the us of oxygen.
process of producing cellular energy involving oxygen.
-Cells break down food in the mitochondria in a long,
multistep process that produces roughly 36 ATP.
-Its first step in is glycolysis, the second is the citric acid cycle
and the third is the electron transport system.
-During aerobic respiration, oxygen is present and helps the
process to crank out energy very efficiently.
Organic compound + oxygen CO2 + H2O + Energy
3 PROCESSES:
1) Glycolysis
2) Citric Acid Cycle
3) Oxidative Phosphorylation
(PIC)
• FERMENTATION
-Partial degradation of sugars/other organic fuel
-no oxygen
-partial breakdown
ex. Yoghurt, wine
-fermentation complements glycolysis and makes it
possible for ATP to be continually produced in the
absence of oxygen.
- By oxidizing the NADH produced in glycolysis,
fermentation regenerates NAD+, which can take part in
glycolysis once again to produce more ATP.
-In fermentation, the only energy extraction pathway is
glycolysis, with one or two extra reactions tacked on at
the end.
-
Lactic acid fermentation can happened in our body.
• ANAEROBIC RESPIRATION
-Use substances other than oxygen
-Some examples of anaerobic respiration include alcohol
fermentation, lactic acid fermentation and in
decomposition of organic matter.
-The equation is: glucose + enzymes = carbon dioxide +
ethanol / lactic acid. -ex. Sprinting
-similar to aerobic cellular respiration in that electrons
extracted from a fuel molecule are passed through an
electron transport chain, driving ATP synthesis
REDOX REACTIONS
-Transfer of one or more electrons from one reactant to
another
-known as oxidation reduction
-type of chemical reaction that involves a transfer of
electrons between two species.
-An oxidation-reduction reaction is any chemical reaction
in which the oxidation number of a molecule, atom, or
ion changes by gaining or losing an electron.
-REDUCTION: Addition of electrons
-OXIDATION: Removal of electrons
RESPIRATION
- the biochemical process in which the cells of an
organism obtain energy by combining oxygen and
glucose, resulting in the release of carbon dioxide, water,
and ATP (the currency of energy in cells).
-Food molecules or glucose are turned into ATP
-Occurs in cytoplasm and mitochondria
- PHOTOSYNTHESIS
- -Plants use sunlight and carbon dioxide to build food
molecules
-release oxygen as a waste product
-occurs in chloroplast
AEROBIC RESPIRATION
1) GLYCOLYSIS
-Breaks glucose into two molecules called PYRUVATE
-“GLY” means SUGAR; “LYSIS” means BREAKDOWN
-is the process of breaking down glucose into two
molecules of pyruvate.
-It produces ATP and is the first stage of cellular
respiration.
-Glycolysis can occur with or without oxygen.
-In the presence of oxygen, glycolysis is the first stage of
cellular respiration.
-LOCATION: Cytosol
-PRODUCED: 4 ATP
-USED: 2 ATP
- -NET YIELD: 2 ATP
TAKE NOTE:
GGP AND FGP are isomers
• ENERGY INVESTMENT PHASE
-Steps 1-4 in glycolysis
- the cell actually "spends" ATP by phosphorylating
glucose.
-Glucose is then split into two three-carbon molecules.
• ENERGY PAYOFF PHASE
-Energy yield
-steps 6-10 in glycolysis
-consists of five additional steps and results in the
formation of four ATP, two NADH + H+, and two pyruvate
molecules.
-Substrate level phosphorylation is the process by
which ATP is produced from the transfer of a phosphate
group from a substrate molecule in a metabolic pathway.
- is the last five steps of glycolysis, which produce the
final two pyruvate molecules product.
TAKE NOTE:
ISOMERS have Similar structures but different orientation.
STEPS IN GLYCOLYSIS:
1) INVESTMENT STAGE
ENZYME: Hexokinase
PROCESS: Phosphorylates glucose in cell’s cytoplasm
PRODUCT: Glucose 6-phospate
MORE DETAILED EXPLANATION IN STEPS:
o Glucose will phosphorylate HEXOKINASE that will
capture in Phospate Group (ATP an ADP) and
transfer to glucose to make it G6P
ANOTHER VERSION:
The first step in glycolysis is the conversion of D-
glucose into glucose-6-phosphate. The enzyme that
catalyzes this reaction is hexokinase.
Details:
Here, the glucose ring is phosphorylated.
Phosphorylation is the process of adding a
phosphate group to a molecule derived from ATP. As
a result, at this point in glycolysis, 1 molecule of ATP
has been consumed.
The reaction occurs with the help of the enzyme
hexokinase, an enzyme that catalyzes the
phosphorylation of many six-membered glucose-like
ring structures. Atomic magnesium (Mg) is also
involved to help shield the negative charges from the
phosphate groups on the ATP molecule. The result of
this phosphorylation is a molecule called glucose-6-
phosphate (G6P), thusly called because the 6′
carbon of the glucose acquires the phosphate group.
GLUCOSE -----→ GLUCOSE 6 PHOSPHATE
(pic)
2) INVESTMENT STAGE
ENZYME: Phosphoglucoisomerase
PROCESS: converts glucose 6-phospate into its isomer
PRODUCT: fructose 6-phospate
GLUCOSE 6- ---------→ FRUCTOSE 6-
PHOSPHATE PHOSPHATE
More detailed process:
• G6P converted to fructose 6-phospate, convert G6P to
F6P (This 2 are isomers)
ANOTHER VERSION:
The second reaction of glycolysis is the rearrangement of
glucose 6-phosphate (G6P) into fructose 6-phosphate
(F6P) by glucose phosphate isomerase (Phosphoglucose
Isomerase).
Details:
The second step of glycolysis involves the conversion of
glucose-6-phosphate to fructose-6-phosphate (F6P). This
reaction occurs with the help of the enzyme
phosphoglucose isomerase (PI). As the name of the
enzyme suggests, this reaction involves an isomerization
reaction.
The reaction involves the rearrangement of the carbon-
oxygen bond to transform the six-membered ring into a
five-membered ring. To rearrangement takes place when
the six-membered ring opens and then closes in such a
way that the first carbon becomes now external to the
ring.
3) INVESTMENT PHASE
ENZYME: Phosphofructokinase
PROCESS: uses another ATP to transfer another
phosphate molecule on C1
PRODUCT: Fructose 1,6-bisphosphate
More detailed process:
• F6P phosphorylated by PFK will capture ATP and transfer
to F6P----F1,6BP4
ANOTHER VERSION:
Phosphofructokinase, with magnesium as a
cofactor, changes fructose 6-phosphate into
fructose 1,6-bisphosphate.
Details:
In the third step of glycolysis, fructose-6-phosphate
is converted to fructose- 1,6-bisphosphate (FBP).
Similar to the reaction that occurs in step 1 of
glycolysis, a second molecule of ATP provides the
phosphate group that is added on to the F6P
molecule.
The enzyme that catalyzes this reaction is
phosphofructokinase (PFK). As in step 1, a
magnesium atom is involved to help shield
negative charges.
F6P------→ F1,6BP
4) INVESTMENT PHASE
ENZYME: aldolase, triose phosphate isomerase (TPI)
PROCESS: Aldolase splits fructose 1,6-biphosphate (c6)
into two (c3 sugar); TPI Converts dihydroxyacetone
phosphate (DHAP) to Glyceraldehade 3-phosphate (G3P)
PRODUCT: DHAP and G3P
FINAL PRODUCT: (2) G3P
FRUCTOSE 1,6 DHAP----→ G3P
-BIPHOSPHATE-----→
G3P
More detailed process:
• F1,6BP split bby aldolase (results molecule and converted
DHAP by TPI
ANOTHER VERSION:
The enzyme Aldolase splits fructose 1, 6-bisphosphate
into two sugars that are isomers of each other. These
two sugars are dihydroxyacetone phosphate (DHAP) and
glyceraldehyde 3-phosphate (GAP).
Details:
This step utilizes the enzyme aldolase, which catalyzes
the cleavage of FBP to yield two 3-carbon molecules. One
of these molecules is called glyceraldehyde-3-phosphate
(GAP) and the other is called dihydroxyacetone
phosphate (DHAP).
Triosephosphate:
 The enzyme triosephosphate isomerase rapidly inter- converting the NAD to NADH. The phosphate group then
converts the molecules dihydroxyacetone phosphate attacks the GAP molecule and releases it from the
(DHAP) and glyceraldehyde 3-phosphate (GAP). enzyme to yield 1,3 bisphoglycerate, NADH, and a
Glyceraldehyde phosphate is removed / used in next step hydrogen atom.
of Glycolysis. 6) ENERGY PAY OFF
Details:
ENZYME: Phosphoglycerokinase
GAP is the only molecule that continues in the glycolytic PROCESS: phosphoglycerokinase transfers a P from (2)
pathway. As a result, all of the DHAP molecules produced 1,3-biphosphoglycerate to (2) ADP to produce (2) ATP
are further acted on by the enzyme Triosephosphate and (2) 3-phosphoglycerate
isomerase (TIM), which reorganizes the DHAP into GAP PRODUCT 1:2 ATP
so it can continue in glycolysis. At this point in the PRODUCT 2: (2) 3-Phosphoglycerate
glycolytic pathway, we have two 3-carbon molecules, but
have not yet fully converted glucose into pyruvate.
(2) 1,3- BISPHOSPHO -→ (2) 3-
Take note: GLYCERATE BIPHOSPHOGLYCERATE

More detailed process:

• 1 3BPG-PGK (an enzyme) capture phosphate group,
1,3BPGB translate ADP then becomes 3PPC
-reversible arrow
ANOTHER VERSION
-one direction arrow Phosphoglycerate kinase transfers a phosphate group
from 1,3-bisphosphoglycerate to ADP to form ATP and 3-
phosphoglycerate.
5) ENERGY PAYOFF
ENZYME: Triose phosphate dehydrogenase/ G3P
dehydrogenase
Details:
PROCESS 1: TPD transfers H- to NAD+
PRODUCT 1: 2 NADH (Nicotinamide Adenine In this step, 1,3 bisphoglycerate is converted to 3-
Dinucleotide) phosphoglycerate by the enzyme phosphoglycerate kinase
(PGK). This reaction involves the loss of a phosphate group
PROCESS 2: TPD phosphorylates G3P from the starting material. The phosphate is transferred to a
molecule of ADP that yields our first molecule of ATP. Since
PRODUCT 2: (2) 1,3- Bisphoglycerate we actually have two molecules of 1,3 bisphoglycerate
(because there were two 3-carbon products from stage 1 of
(2) NAD+------→ (2) NADH- glycolysis), we actually synthesize two molecules of ATP at
oxidation
this step. With this synthesis of ATP, we have cancelled the
(2) Glyceraldehade 3- --→ (2) 1,3- Bi- first two molecules of ATP that we used, leaving us with a net
Phosphate Phosphoglycerate of 0 ATP molecules up to this stage of glycolysis.

MORE DETAILED PROCESS: Again, we see that an atom of magnesium is involved to

shield the negative charges on the phosphate groups of the
• PROCESS 1: 2 molecules of G3P, NAD+--TPD (Starting) will ATP molecule.
oxidize NAD+ and converts NADH, Now, NADH can
synthesize to ATP 7) ENERGY PAYOFF
ENZYME: Phosphoglyceromutase
PROCESS 2: G3P not phosphorylated by G3PD now
becomes 1, 3BPG PROCESS: relocates the P from 3C to 2C
PRODUCT: (2) 2-phosphoglycerate
Another process:
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) MORE DETAILED PROCESS:
dehydrogenates and adds an inorganic phosphate to • 3PPG transfer carbon no. 2 to become 2 PPG done by
glyceraldehyde 3-phosphate, producing 1,3- PGM
bisphosphoglycerate.
ANOTHER VERSION:
Details:
The enzyme phosphoglycero mutase relocates the P from 3-
In this step, two main events take place: 1)
phosphoglycerate from the 3rd carbon to the 2nd carbon to
glyceraldehyde-3-phosphate is oxidized by the coenzyme
form 2-phosphoglycerate.
nicotinamide adenine dinucleotide (NAD); 2) the
molecule is phosphorylated by the addition of a free
phosphate group. The enzyme that catalyzes this
reaction is glyceraldehyde-3-phosphate dehydrogenase Details:
(GAPDH).
This step involves a simple rearrangement of the position of
the phosphate group on the 3 phosphoglycerate molecule,
The enzyme GAPDH contains appropriate structures and
making it 2 phosphoglycerate. The molecule responsible for
holds the molecule in a conformation such that it allows
catalyzing this reaction is called phosphoglycerate mutase
the NAD molecule to pull a hydrogen off the GAP,
(PGM). A mutase is an enzyme that catalyzes the transfer of a
functional group from one position on a molecule to another.
The reaction mechanism proceeds by first adding an
additional phosphate group to the 2′ position of the 3
phosphoglycerate. The enzyme then removes the phosphate
from the 3′ position leaving just the 2′ phosphate, and thus
yielding 2 phsophoglycerate. In this way, the enzyme is also
restored to its original, phosphorylated state.
(2) 3-PHOSPO- ------→ (2) 2-
Immediately upon finishing glycolysis, the cell must continue
respiration in either an aerobic or anaerobic direction; this
choice is made based on the circumstances of the particular
cell. A cell that can perform aerobic respiration and which
finds itself in the presence of oxygen will continue on to the
aerobic citric acid cycle in the mitochondria. If a cell able to
perform aerobic respiration is in a situation where there is no
oxygen (such as muscles under extreme exertion), it will
move into a type of anaerobic respiration called homolactic
fermentation. Some cells such as yeast are unable to carry
out aerobic respiration and will automatically move into a
type of anaerobic respiration called alcoholic fermentation.

GLYCERATE PHOSPHOGLYCERATE

8) ENERGY PAYOFF
ENZYME: Enolase; pyruvate kinase
PROCESS: removes H2O from 2-phosphoglycerate;
transfers P from PEP to ADP
PRODUCT: (2) phophoenolpyruvate (PEP)
FINAL PRODUCT: (2) pyruvate, 2 ATP

MORE DETAILED PROCESS:

• 2 PPG enolase enzyme permit dehydration found 2 PPG
becomes PEP (Phosphate) transfer ADP To synthesize
ATP to become pyruvate

ANOTHER VERSION:
The enzyme enolase removes a molecule of water from 2-
phosphoglycerate to form phosphoenolpyruvic acid (PEP).

Details:

This step involves the conversion of 2 phosphoglycerate to

phosphoenolpyruvate (PEP). The reaction is catalyzed by the
enzyme enolase. Enolase works by removing a water group,
or dehydrating the 2 phosphoglycerate. The specificity of the
enzyme pocket allows for the reaction to occur through a
series of steps too complicated to cover here.

PYRUVATE KINASE:
The enzyme pyruvate kinase transfers a P from
phosphoenolpyruvate (PEP) to ADP to form pyruvic acid and
ATP Result in step 10.

Details:

The final step of glycolysis converts phosphoenolpyruvate

into pyruvate with the help of the enzyme pyruvate kinase. As
the enzyme’s name suggests, this reaction involves the
transfer of a phosphate group. The phosphate group attached
to the 2′ carbon of the PEP is transferred to a molecule of
ADP, yielding ATP. Again, since there are two molecules of
PEP, here we actually generate 2 ATP molecules.

Steps 1 and 3 = – 2ATP PYRUVATE OXIDATIVE:

Steps 7 and 10 = + 4 ATP -Follows glycolysis -
pyruvate is carried from cytosol via active transport
Net “visible” ATP produced = 2.
MORE DETAILED PROCESS:
Pyruvate enter mitochondria, carbonyl group will detach in There are times that GTP can’t synthesize GDP
carbon dioxide. Acetyl group will undergo redox reaction and because your body might be undergoing
2 thing will happen: 1NAD+ Undergoes reduction NADH and 2 transcription.
oxidation of acetyl group and coenzyme A to become acetyl
CoA ENZYME: succinyl CoA synthase
REACTION: substrate level phoporylation
PRODUCT: GTP/ATP
CITRIC ACID CYCLE
6. Succinate (substrate) will go under redox (FAD-FADH2)
-Known as krebs cycle and tricarboxylic acid and CTCA Cycle reduction) and oxidation of succinate to fumerate
-goal: act as metabolic furnace that oxidizes fuel derived from ENZYME: succinate dehydrogenase
pyruvate REACTION: RedOx
-use up product of Glycolysis(PYRUVATE) PRODUCT: FADH2 Fumerase
LOCATION: mitochondrial matrix
NET YIELD: (X2) 3 7. Fumarate (starting enzyme) goes under hydration
NADH ENZYME: Fumarase
FADH2 REACTION: Hydration
ATP and/or GTP PRODUCT: Malate

*ACETYL COA AND OXALOACETATE (starting molecule) 8. Oxaloacetate undergoes redox, NADH-NAD+ undergoes
reduction
STEPS: ENZYME: Malate dehydrogenase
REACTION: Redox
1. Acetyl group (2 carbon) add oxaloacetate to form citrate,
PRODUCT: NADH, Oxaloacetate
CoA aalis temporarily
ENZYME: Citrate Synthrase
REACTION: Aldol Condensation PRODUCED:
PRODUCT: CITRATE NADH-3x2
FADH2-1x2
2. ISOMERIZATION-citrate converted to Isocitrate (an ATP-1x2
isomer), a water molecule is remove from citrate then
added again to your isocitrate

ENZYME: Aconitase
REACTION: Dehydration, hydration (isomerization)
PRODUCT: Isocitrate

3. Isocitrate will undergo redox reaction and produce

NADH, isocitrate will loose 1 carbon molecule, it will now
form a-ketoglutarate
ENZYME: Isocitrate Dehydrogenase
REACTION: Oxidative Decarboxylation (RedOx)
PRODUCT: NADH, a-ketoglutarate
TAKE NOTE:
NADH is produce whenever there is redox reaction!

4. CO2 removal then redox, addition of CoEnzyme A(babalik

lang)
*the bond for Coenzyme A is UNSTABLE
*COA-SH is COA with bond of Sulfur
ENZYME: a-ketoglutarate dehydrogenase
REACTION: oxidative decarboxylation (RedOx)
PRODUCT: NADH, Succinyl CoA

5. A phosphate group will remove CoA because it is

unstable, phosphate group can be used to synthesize GTP
Phosphate will bind to GDP

OR
OXIDATIVE PHOSPORYLATION
Acetyl CoA, phosphate group will unbound this Phospate GOAL: ATP generation
Group and bind to GTP to synthesize GDP. GDP can LOCATION: inner membrane of mitochondria
synthesize from ATP to synthesize ADP PHASE 1: Electron Transport Chain
PHASE 2: Chemiosmosis
GTP-for transcription of DNA
ATP-energy for all NADH
Oxidation NADH → NAD+ + H+ +2E-

THERE IS NO ATP GENERATION YET

10 NADH
 2FADH2 3. H+ ions will release back to mitochondria
*ATP production is in catalytic knob
4. Rod will rotate as well but keep in mind that your
catalytic knob shouldn’t rotate.

NUMBERS IN PIC IS CALLED COMPLEX I, II, III, IV

THE ENZYMES:
I. -NADH Dehydrogenase
II. -Succinate Dehydrogenase
III. -Cytochrome- Oxidoreductase
IV. -cytochrome oxidase

Q-ubiquinone Cyt C-
Cytochrome C

Q is not a protein, nor an enzyme but a COENZYME that

activate enzyme

ANAEROBIC RESPIRATION
Oxidative Phosporylation=ATP
2 mechanisms wherein cells can generate ATP w/o
oxygen

ANAEROBIC RESPIRATION
-Prokaryotes in environment w/o oxygen
-other electro negative act as electron acceptor
-sulfate ions-H2s
Overall produced:

10 NADH FERMENTATION
2 FADH2 -No oxygen
-no ETC
-ATP gen: by substrate level phosphorylation
( starting molecule {glucose} synthesize ATP
glycolysis)

TAKE NOTE:
ANAEROBIC RESPIRATION CAN REACH OXIDATIVE
PHOSPORYLATION

i. LACTIC ACID FERMENTATION

CHEMIOSMOSIS
1. H+ Ions will enter stator (enzymes)
2. Nproceed then rotate and make 1 whole rotation

PROCESS:
-Pyruvate is reduced to lactate and NADH is oxidate to NAD+ .
NAD+ Will be used again as glycolysis
PROCESS:
-after glycolysis, pyruvate C must have initial release of
carboxyl group. Decarboxylation of pyruvate results to
acetaldehyde. Acetaldehyde will have redox w/ ethanol.

MORE DETAILED PROCESS:

MORE DETAILED PROCESS:

Lactic acid fermentation converts the 3-carbon pyruvate to

the 3-carbon lactic acid (C3H6O3) (see figure below) and
regenerates NAD+ in the process, allowing glycolysis to
continue to make ATP in low-oxygen conditions. Since there is
a limited supply of NAD+ available in any given cell, this
electron acceptor must be regenerated to allow ATP
production to continue. To achieve this, NADH donates its
extra electrons to the pyruvate molecules, regenerating
NAD+. Lactic acid is formed by the reduction of pyruvate.

C3H3O3(pyruvate)+NADH→C3H6O3(lactic acid)+NAD+(15.3.1)

lactic acid fermentation converts pyruvate to lactic acid, and

regenerates NAD+ from NADH.

APPLICATION:
• Lacto-milk/lactose
• Bacillus- rod shaped bacteria
Ex. Dairy, Cheese, Yogurt, Pickled foods

ii. ALCOHOL FERMENTATION