GENERA

L
BIOLOG
Y
(REVIEWER)
STEM - 11

BIOLOGICAL MOLECULES
CARBOHYDRATES
Classifications of Monosaccharides
1. Triose – 3-carbon monosaccharide
2. Tetrose – 4-carbon monosaccharide
3. Pentose – 5-carbon monosaccharide
Examples: Ribose, Deoxyribose,
arabinose, ribulose
4. Hexose - 6-carbon monosaccharide
5. Heptose - 7-carbon monosaccharide
6. Octose - 8-carbon monosaccharide
7. Nonose - 9-carbon monosaccharide
What are the Biological Functions of
MONOSACCHARIDES
-serve as a structural unit for various
biological compounds
- through GLYCOSIDIC BONDS –
disaccharides, oligosaccharides, and
polymers (cellulose, starch, and glycogen)
 Monosaccharides are found
in fruits, vegetables, and
many other dietary sources
 Consumed and metabolized
to drive ATP (which fuels
various biological activities)
METABOLISM OF MONOSACCHARIDES
Aerobic respiration
                      - Aerobic respiration is the
process by which organisms use oxygen to
turn fuel, such as fats and sugars, into
chemical energy.
Anaerobic respiration
Anaerobic respiration is the type of
respiration through which cells can break
down sugars to generate energy in the
absence of oxygen. 
DISACCHARIDES
-two monosaccharides
a) Sucrose
- non reducing disaccharide that
forms glucose and fructose when linked
together by an alpha linkage between
carbon 1 of glucose and carbon 2 of
fructose.
CARBOHYDRATE BREAKDOWN
Enzymes  in the mouth, stomach, and small
intestine, breakdown the carbohydrate
molecules.
These large complex carbohydrate
molecules breakdown into simple sugars.
HOW DOES BREAKDOWN OCCUR?
Our bodies use special protein molecules
called enzymes to break the larger
molecules into smaller pieces.
Enzymes Are Catalysts
Catalysts are chemicals that quicken a
chemical reaction without undergoing any
change themselves
They are essential for respiration, digesting
food, muscle and nerve function.
ENZYMES
Lipases: This group of enzymes help digest
fats in the gut.
Amylase: In the saliva, amylase helps
change starches into sugars.
Maltase: This also occurs in the saliva, and
breaks the sugar maltose into glucose.
 Monomer-are the small units for building
blocks 
Polymer-are the large units composed of
multiple monomers

SOURCE OF CARBOHYDRATES 
•pasta,breads,cereals,grain,rice,fruits
•Composed of C,H and O atoms with a
ration of 1:2:1

BIOLOGICAL MACROMOLECULES  •Represented by the stoichiometrics formula

C6H12O6
Carbohydrates-Proteins-Lipids-Nucleic Acid
SUBTYPES OF CARBOHYDRATES 
Macromolecules
 Monosaccharide-Simple Sugar
 A large molecules necessary for life  Disaccharide-Complex Sugar
that are built from different  Oligosaccharides-Complex Sugar
combinations of smaller organic  Polysaccharides-Complex Sugar
compounds.

Monosaccharides
WHY ARE MACROMOLECULES
IMPORTANT?  are simple sugar that constitutes the
building blocks of a more complex
Carbohydrates  forms of sugar.
 Are the body’a main source of
energy COMMON MONOSACCHARIDES 
Lipids 1).Glucose
 Provide stored energy reserves  is a monosaccharides that occurs
naturally and is ubiquitous.
Proteins 
 Molecular Formula:C6H12O5
 Help us to stay srong,by turning new
1).Glucose Disaccharide 
bones and muscles.
 Nucleic Acid  Maltose=glucose+glucose”Malt
 The blueprint for our genetic Sugar”
structure.  Lactose=glucose+galactose”Milk
Sugar”
 Suctose=glucose*fructose”Fruit
“THE BIG FOUR MACROMOLECULES”
Sugar”
Building blocks
2).Galactose
POLYMER/MONOMERS
 it is similar to glucose in terms of
 Carbohydrates/Monosaccharides  chemical structure.
 Proteins/Amino acids
3).Fructose
 Lipids/Fatty Acids and Glycerol
 Nucleic Acid/Nucleotides  is regarded as the sweetest
naturally occurring carbohydrates.
  1. Oxygen Transport

 Hemoglobin – protein found in red blood

cells
2. Proteins as Enzymes

 - Catalyze specific biochemical

reactions

 - Lipase, Amylase, and Maltase

3. Antibodies are Proteins

 -Antibodies are defensive proteins that

have binding sites which allows them to
identify and bind to very specific foreign
BIOLOGICAL MOLECUES molecules.
Carbohydrates – proteins – lipids – nucleic  4. Structural Proteins
acids 
 - frequently long and fibrous
PROTEINS
 - keratin and collagen
-are nutrients which
contain materials the body  5. Contract Proteins
uses for growth and repair.
 - actin and myosin
     -made of Carbon, Hydrogen, Oxygen and
Nitrogen.  PROTEIN BREAKDOWN

    -Proteins are large molecules made up of  -In order for the body to use protein,
combinations of amino acids enzymes in the stomach and small
intestine break the polypeptides down
  into individual amino acids.


 LIPIDS

 -Lipids function as stored energy,

insulation for the body, and assist
absorption of certain vitamins.

 -composed of triglycerides. 

 -These molecules are made up of

 Amino acids are the building blocks of carbon, hydrogen, and oxygen atoms. 
proteins.

  These building blocks bond together to

form chains that are called peptides.

  Proteins (polypeptides) are formed

through formation of peptide bonds
between amino acids.

FUNCTION OF PROTEINS
  - Maintains constant temperature.
- Fatty acids are also required for proper
reproductive health.
3.Insulating and Protecting
Visceral fat – surrounds vital organs such as
the heart, kidneys, and liver.
Subcutaneous fat - insulates the body from
extreme temperatures.
- It can pad our hands and buttocks to prevent
friction.

FATS VS OILS
LIPID BREAKDOWN
A triglyceride that is a fat 

  Is solid at room temperature.

  Is prevalent in meats, whole milk,

butter, and cheese.
A triglyceride that is an oil

  Is liquid at room temperature.

  Is prevalent in plants such as olive and Bil

sunflower. e and enzymes in the small intestine break lipids
down into small molecules of fatty acids and
FUNCTION OF LIPIDS glycerol. 

1.Energy Storage NUCLEIC ACIDS

-The excess energy from the food we eat is -Stores and carries genetic information
digested and incorporated into adipose tissue, or
fat tissue.  -Composed of nucleotides

-While glycogen provides a ready source of -NOT obtained from food

energy, lipids primarily function as an energy -Occur in two forms:
reserve.
2.Regulating and Signaling
- Lipids are part of the cell membrane structure = FUNCTION OF DNA AND RNA
fluidity and flexibility. 
DNA
   DNA replicates and stores genetic
information
- Serves as a “blueprint”

RNA

  Converts the genetic information

contained in DNA to a format used to
build proteins.

Nucleotides
-the basic building block of nucleic acids (RNA
and DNA).
consists of a sugar molecule (either ribose in
RNA or deoxyribose in DNA) attached to a
phosphate group and a nitrogen-containing
base. 

 Base pairs in DNA

 Adenine (A) & Thymine

(T)
 Nitrogenous bases in DNA
 Guanine (G) & Cytosine
Adenine (A) (C)

Thymine (T)  Base Pairs in RNA

Guanine (G)  Adenine (A) & Uracil (U)

Cytosine (C)  Guanine (G) & Cytosine

(C)

 Nitrogenous bases in RNA

ENZYMES 
Adenine (A) WHAT IS ENZYMES? 
Uracil (U) -are important proteins that speed up the rate of
chemical reactions such as photosynthesis,
Guanine (G) respiration, and protein synthesis. 
* also known as the most effective catalyst. 
Cytosine (C)
GENERAL CHARACTERISTICS
OF ENZYMES 
•lower activation energy. 
•human body has 1000s of enzymes. 
•most are globular proteins. 
•are unchanged at the end of the reaction and can be
reused. 
ENZYMES CAN…. 
1.Help breakdown large molecules into small
molecules. 
2.Build up large molecules from smaller ones 
HOW ENZYMES WORK? 
ACTIVE SITE  q A cofactor : Nonprotein part of a conjugated
-the region on enzyme where the substrate binds and enzyme. 
where the reaction is catalyzed.  q A holoenzyme is the biochemically active
SUBSTRATE  conjugated enzyme 
-A reactant in a chemical reaction is called substrate Apoenzyme + cofactor = holoenzyme (conjugated
when acted upon on enzyme  enzyme) 
•Enzyme-substrate complex is a temporary formed Conjugated enzyme 
when an enzyme comes into perfect contact with it’s Apoenzyme + Cofactor = Holoenzyme 
substrate.   
TWO MODELS OF ENZYME-  
SUBSTRATE INTERACTION  
-LOCK AND KEY MODEL   
-INDUCED FIT MODEL   
ACTIVE SITE AND SUBSTRATE SPECIFICITY   
1.LOCK-AND-KEY MODEL 
 Proposed by Emil Fischer in 1894  COFACTORS 
 This model proposed that the active site and Cofactors 
substrate are exactly complementary  • Cofactors are important for the chemically reactive
 The enzymes active site and substrate should fit like enzymes 
lock and key to initiate reaction  • Cofactors are small organic molecules or inorganic
 Only substrate of specific shape can bind with active ions 
site  – Organic molecule cofactors: also called as co-
  enzymes which are derived from dietary vitamins 
2. INDUCED FIT MODEL   Inorganic ion cofactors 
 Proposed by Daniel Koshland in 1958  – Typical metal ion cofactors - Zn2+, Mg2+, Mn2+,
 The active site of the enzyme DOES NOT have a and Fe2+  
rigid conformation  – Nonmetallic ion cofactor - Cl-  
 Active site of the enzyme modifies its shape upon – Inorganic ion cofactors derived from dietary
the binding of the substrate  minerals 
 (e.g., how a hand fits into a glove)   
  NOMENCLATURE OF ENZYMES 
  How are enzymes named? 
  • Nomenclature: Most commonly named with
  reference to their function 
– Type of reaction catalyzed  
– Identity of the substrate 
1.Suffix -ase identifies it as an enzyme 
– E.g., urease, sucrase, and lipase are all enzyme
designations 
– Exception: The suffix -in is still found in the names
of some digestive enzymes, E.g., trypsin,
chymotrypsin, and pepsin 
2.Type of reaction catalyzed by an enzyme is often
used as a prefix 
– E.g., Oxidase - catalyzes an oxidation reaction,  
– E.g., Hydrolase - catalyzes a hydrolysis reaction 
Enzyme Structure  3. Identity of substrate is often used in addition to the
Enzymes are of two types: simple enzymes and type of reaction 
conjugated enzymes   – E.g. Glucose oxidase, pyruvate carboxylase, and
• Simple enzyme: composed only of protein (amino succinate dehydrogenase 
acid chains)   
• Conjugated enzyme: Has a nonprotein part in SIX MAJOR CLASSES OF ENZYMES 
addition to a protein part.   
Conjugated enzyme 
q Apoenzyme: Protein part of a conjugated enzyme. 
 •Optimum temperature: Temperature at which the
rate of enzyme catalyzed reaction is maximum 
•Optimum temperature for human enzymes is 37ºC
Oxidoreductases  (body temperature) 
•An oxidoreductase enzyme catalyzes an oxidation– •Increased temperature (high fever) leads to
reduction reaction:   decreased enzyme activity 
–Oxidation and reduction reactions are always linked •Enzymes of thermophilic bacteria that live in hot
to one another   springs will have very high temperatures 
–E.g., Lactate dehydrogenase is an oxidoreductase  • At low temperature, enzymes are inactive. 
• As temp rises = rate of enzyme activity rises 
Transferases 
• Max at optimum temp 
•A transferase is an enzyme that catalyzes the
transfer of a functional   PH 
group from one molecule to another  pH changes affect enzyme activity 
Hydrolases  • Drastic changes in pH can result in denaturation of
A hydrolase is an enzyme that catalyzes a hydrolysis proteins 
reaction  • Optimum pH: pH at which enzyme has maximum
• The reaction involves addition of a water molecule activity  
to a bond to cause bond breakage  • Most enzymes have optimal activity in the pH range
• Hydrolysis reactions are central to the process of of 7.0 - 7.5  
digestion:   • Exception: Digestive enzymes 
– Carbohydrases hydrolyze glycosidic bonds in oligo- • Pepsin: Optimum pH = 2.0 
and polysaccharides  • Trypsin: Optimum pH = 8.0 
– Proteases effect the breaking of peptide linkages in •Enzymes in ACIDIC conditions 
proteins,   Ø Renin and pepsin – found in stomach 
– Lipases effect the breaking of ester linkages in • Enzymes in ALKALINE conditions 
triacylglycerols  Ø Intestinal enzymes like maltase, sucrase, lipase 
• Enzymes in NEUTRAL conditions 
Lyases 
Ø Amylase 
 A lyase is an enzyme that catalyzes the
addition of a group to a double  Substrate Concentration 
 bond or the removal of a group to form a double Substrate Concentration: At a constant enzyme
bond in a manner that  concentration, the enzyme activity increases with
 does not involve hydrolysis or oxidation  increased substrate concentration. 
 Lyases breakdown the substrate without •Substrate saturation: the concentration at which it
addition of water.  reaches its maximum rate and all of the active sites
are full 
Isomerase and Ligase 
An isomerase is an enzyme that catalyzes the Enzymes Concentration 
isomerization (rearrangement of atoms) reactions.  Enzymes are not consumed in the reactions they
L isomer -> D isomer  catalyze 
•A ligase is an enzyme that catalyzes the formation of •At a constant substrate concentration, enzyme
a bond between two molecules   activity increases with increase in enzyme
involving ATP hydrolysis  concentration  
Ex: Acethyl COA Synthetase  –The greater the enzyme concentration, the
greater the reaction rate. 
 
FACTORS THAT AFFECT ENZYME  
ACTIVITY 
1.Temperature 
2.pH 
3.Substrate Concentration 
4.Enzyme Concentration 
 
Temperature 
Higher temperature results in higher kinetic
energy which causes an increase in number of ATP-ADP CYCLE
reactant collisions, therefore there is higher activity.  
 How does ATP gives us energy? 
ORGANISM ARE CLASSIFIED ACCORDING
ATP-ADP Cycle
TO THEIR ENERGY SOURCES
AUTOTROPHS 
•Make their OWN food
•Plants are photoautotrophs (light energy ➜ glucose)
HETEROTROPHS
•DO NOT make their own food
•Eats plants or other animals who eats plants to
acquire indirectly the energy from the sun
•ATP → ADP+P + energy

What is the energy currency of the cells of •ADP+P + energy → ATP 

autotrophs and heterotrophs? 
ATP VS ADP
ATP (ADENOSINE TRIPHOSPHATE)
•ENERGY CURRENCY of the cell
•ATP consists of an adenine base attached to a ribose
sugar, which is attached to three 
Phosphate groups.
•ATP IS A NUCLEIC ACID

•ATP contains MORE energy than ADP because it

has more bonds.
Where does the ATP come from?
•When the PHOSPHATE is REMOVED, energy is
•ATP comes indirectly from the food that we eat. RELEASED
•Molecules of carbohydrates (glucose) and lipids are •When a PHOSPHATE is ADDED, energy is
broken down through the process of cellular NEEDED
respiration to produce ATP.
ENERGY COUPLING
To Types of Reactions:
1. Exergonic Reactions – energy-releasing
reactions
2. Endergonic Reactions – energy-demanding
reactions
Energy Coupling

 Coupling two biological reactions SITE OF PHOTOSYNTHESIS

 Coupling occurs when the energy
released by an exergonic reaction is A chloroplast contains: 
linked to an endergonic reaction.
▪stroma – a fluid 
Energy coupling in ATP
▪grana – stacks of thylakoids 
 Hydrolysis in ATP is exergonic 
 Phosphorylation in ATP is endergonic ▪The thylakoids contain chlorophyll
 Energy released after hydrolysis used in
endergonic reactions Why are plants GREEN?
ATP FROM CARBOHYDRATES • CHLOROPHYLL

 Energy: up to 36 ATP molecules (I glucose ▪ Chlorophyll pigments harvest light energy called
unit) photons by absorbing certain wavelengths (blue-420
 Most commonly broken down to make ATP nm and red-660 nm are most important).
 Not stored in large amounts
▪Plants are green because the green
ATP FROM LIPIDS
Wavelength is reflected, not absorbed.
 Energy: about 146 ATP molecules
(triglycerides)
WHAT DO PLANTS NEED FOR
 Lipids store the most energy
PHOTOSYNTHESIS?
 80% of the energy in the body
▪Water
ATP FROM PROTEINS
▪Carbon Dioxide
 Energy: about 36 ATP molecules
 Proteins are LEAST LIKELY to be broken ▪Light energy
down to make ATP
 Amino acids not usually needed for energy From sun

PHOTOSYNTHESIS   ▪Chlorophyll
CARBON DIOXIDE AND WATER
▪ It is the process by which autotrophic organisms use
light energy to make sugar and oxygen gas from ▪Carbon dioxide from the
carbon dioxide and water.
Atmosphere will enter into the leaves of the plants
▪Converts light energy to chemical energy. through the stomata.

CHLOROPHYLL AND SUNLIGHT

IMPORTANCE OF PHOTOSYNTHESIS ▪When the white light from

The sun passes through a
PHOTOSYNTHESIS is considered as the most Prism it produces rainbow
important biological process. Why?
Colors.
▪Makes organic molecules out of inorganic materials
▪Two colors are used for photosynthesis, the blue and
▪It begins all food chains/webs. Thus all life is red that are trapped in chlorophyll a and b.
supported by this process.
▪It makes oxygen gas PHOTOSYNTHESIS REACTION
6 CO2 + 6 H2O → Photosynthesis C6H12O6 + 6 O2

TWO MAIN STAGES OF PHOTOSYNTHESIS

•Light-dependent reactions
-happens in thylakoid membrane
-requires sunlight 
-during the day time
•Calvin Cycle “ Light Independent reaction “
-happens in stroma
- do not requires sunlight 
-can occur day or night 

•Oxidation
-Loss of electrons 
-Addition of oxygen
-Removal of hydrogen
PHOTOSYNTHESIS
 A process by which autotrophic
organism use light to make glucose
and oxygen gas from carbon dioxide
•Reduction and water.
-gain of electrons  Converts light energy to chemical
-removal of oxygen energy
 Endergonic process
-addition of hydrogen 
WHY PHOTOSYNTHESIS CONSIDERED AS
NADPH-reduced form of NADP THE MOST IMPORTANT BIOLOGICAL
NADP-electron carrier molecule, coenzyme involved PROCESS ?
in
Oxidation-reduction reactions of photosynthesis
- it makes organic molecules out of
inorganic materials.
(NADP)
- Begins all food chains/webs.
•Nicotinamide adenine dinucleotide phosphate - All life is supported by this process
also it makes oxygen gas.
Where does photosynthesis take place? In
what organelle of the plant ?

CHLOROPLAST CONTAINS: STROMA – a fluid /

GRANA – stacks of thylakoids
The thylakoids contain chlorophyll WHY ARE PLANT ARE GREEN ?

CHLOROPLAST– Green pigment captures light
for photosynthesis
CHLOROPHYLL PIGMENTS harvest light energy
called PHOTONS by ABSORBING certain wave
lengths Blue420 nm and red 660 nm. Plants are
green because the green wavelength is
REFLECTED , not absorbed.

WHAT DO PLANTS NEED FOR

PHOTOSYNTHESIS ?
 WATER
 CARBON DIOXIDE
 LIGHT ENERGY FROM SUN
 CHLOROPHYLL

HOW DOES CARBON DIOXIDE ENTER TE

PLANT ?
CHLOROPHYLL – Two color are used for
- CO2 enter into leaves of the plant photosynthesis ,RED and BLUE that are
through the stomata trapped in chlorophyll

HOW DOES THE WATER ENTER THE STAGE LOCATION EVENTS REQUIRES
SUNLIGHT?
PLANT ?
Light Thylakoid Captured YES
- Enter through the hair rootsof the dependent membrane by
reactions CHLOROPL
plant travel to the stem of the leaves ASTS and
stored as
SUNLIGHT – Passes through a prism it ATP
produce rainbows Light stroma ATP is used NO
independen to create
t reaction sugar, that
(Calvin the plant
Cycle) will use to
grow and
live
TWO MAIN STAGES OF

Light Reactions
PHOTOSYNTHESIS

 Light dependent reaction

 The Calvin cycle

•Light reaction
- happens in the thylakoid membranes.
- primary function is to produce ATP and NADPH.
- uses photons as source of energy.
- photons used to excite electrons and create and
electron transport chain.
• Light Independent Reaction
- Also known as the Calvin Cycle or Dark Reaction.
- Happens in the stroma of the chloroplasts.
- uses ATP, NADPH and CO2 to create glucose.
- Net products: C6H12O6 (glucose) NADP, ADP +P
• Photophosphorylation
- use light energy and electron transport chain to
make ATP.
• Electron transport chain
- embedded in the thylakoid membranes of
chloroplasts.
•(The chlorophyll a molecules from reaction centers).
•P680
- is the reaction-center of photosystem II in a
chlorophyll.
•P700
- reaction center of photosystem I.
(All the other pigments within the membrane form an
antenna complex).
•Antenna complex
- that absorbs light energy and transfers it into these
reaction centers.
 TWO TYPES OF
PHOTOPHOSPHORYLATION:
1.) Noncyclic photophosphorylation
- also called the Z-scheme
- Electrons from chlorophyll travel through an
electron transport chain the reduce NADP+ to
NADPH.
2.) Cyclic photophosphorylation
- Only ATP is produced.
- happens only in Photosystem 1.
• Electron carrier molecules in the electron transport
chain:
*PQ - plastoquinone
*Cyt - cytochrome b6f complex
*PC - plastocyanin
*FD - ferredoxin
• Noncyclic photophosphorylation;
1.) LIGHT ABSORPTION N PSII
- when light is absorbed by one of the many pigments
in Photosystem II, energy is passed inward from
pigment to pigment.
- energy is transferred to P680, boosting an electron
to a high energy level.
- this splitting of water releases the O2 we breathe.
2.) ATP SYNTHESIS
- the high energy electron travels down an electron
transport chain, losing energy as it goes.
- they pass through ATP synthase, driving ATP
production in a process known as chemiosmosis.
3.) LIGHT ABSORPTION IN PS1
- the electron arrives at Photosystem 1 and joins the
P700 special pair of chloropylls in the reaction
center.
- the special pair's missing electron is replaced by a
new electron from PSII (arriving via the electron
transport chain).
4.) NADPH FORMATION
- high energy electron travels down a short second
leg of the electron transport chain.
- at the end of the chain, electron is passed to NADP+
to make NADPH.
 LIGHT INDEPENDENT REACTION
 Also known as Calvin Cycle or Dark Reactions
 Happens in the Stroma of the chloroplast.
 Uses the ATP, NADPH, and CO2 to create
glucose.
 Net Products: C6 H12 O6 (glucose), NADP,
ADP+P
CALVIN CYCLE
 NADPH - important source carrier NADPH
 The Light Reactions of Photosynthesis transfer
light energy to chemical energy, producing the
energy molecule and the electrons.
 ATP - provides usable energy to cells for the
cellular work that is necessary for survival.
 source of electrons for reactions that build
molecules for the cell.
 Humans, like all organisms on earth are carbon
based life form
Calvin Cycle transforms inorganic carbon in the
form of carbon dioxide (CO2) into organic
carbons in the form of carbohydrates.
Carbon 3CO2 combine with 3 RUBP acceptors,
making 6 molecules of glyceraldehyde-3-
phospate(G3P)
1 G3P molecule exists the cycle and goes towards
making glucose.
5 G3P molecules are recycled, regenerating 3 RUBP
acceptor molecules.
ATP - 9 ATP are converted to 9 ADP ( 6 during the
fixation, 3 during regeneration step.)
NADPH 6 NADPH are converted to 6 NADP+
( during the reduction procedure)
Steps of the Calvin Cycle
1. The enzyme Rubisco attaches carbon dioxide
molecules to a 5-carbon sugar called ribulose
bisphosphate (RUBP).
Rubisco à ribulose-1,5-bisphosphate
carboxylase/oxygenase.
This critical first step captures the carbon dioxide
from the environment and is called carbon fixation.
The 6-carbon molecules that are formed by this step
immediately split into two copies of a 3-carbon
molecule.
These 3-carbon molecules are called 3-
phosphoglycerate
2. 3-phosphoglycerate (PGA) is phosphorylated
when it’s given a phosphate group from ATP, which
transfers energy from ATP to the 3-phosphoglycerate.
Next, electrons from NADPH are transferred to the
molecule reducing it to the sugar glyceraldedehyde-
3-phosphate (G3P).
The energy and electrons for this phase, called the
reduction phase, came from the light reactions.
3. One G3P is used to make glucose and other sugars.
This process is called biosynthesis, or just synthesis,
because the plant is making sugars.
4. Five G3P and ATP are used to regenerate RuBP,
the 5-carbon sugar the plant started with
The plant needs to move carbons around to reproduce
the starting molecule so that it can start over again.
This step is called the regeneration phase.
Cellular respiration is a metabolic pathway that
breaks down glucose and produces ATP.
Cells break down food molecules —
carbohydrates, proteins, and fats — through
cellular respiration. Cellular respiration is a
metabolic pathway that, through a series of small
steps, rearranges the atoms in the food
molecules, making their stored energy available
to the cell.
C6H12O6 + 6 O2 → 6 CO2 + 6 H2O + energy