BIOCHEMISTRY

REVIEW
Mary Grace S. Biagtan, RPh, MS Pharm
Lecturer for Module 2: Biochemistry
Second Semester; AY 2021-2022

BIOCHEMISTRY REVIEW
01. Introduction

02. Amino Acids, Proteins & Enzymes

03. Carbohydrates
04. Lipids

05. Nucleic acids and Central Dogma

01 Proteins Carbohydrates

BIOCHEMISTRY
• the chemistry of life Nucleic Acids Lipids
• focuses on primary metabolites

02
PROTEINS, PEPTIDES &
AMINO ACIDS
 Amino Acids
● building units of proteins (monomers of proteins)
● ampotheric in nature: possesses both basic and acidic group
● zwitter ion: a molecule that has (-) charge on one atom and (+)
charge on another atom, but has no net charge
● peptide bond: the bond that joins each amino acid
 Structure of an Amino Acid

Side Chain Of Some Amino Acids

Alanine
Valine
Alkyl R Group Leucine
Isoleucine
Proline
Aromatic Group Phenylalanine
Tryptophan
S-Containing (Thioester) Methionine
 Side Chain Of Some Amino Acids
R-H Glycine

Serine
Hydroxyl Threonine

Tyrosine

Asparagine
Amide
Glutamine
Sulfhydril Cysteine

01 02

TRYPTOPHAN GLYCINE
Synthesis of 5-
hydroxytryptamine (5-HT) or Heme (hemoglobin)
Serotonin

03 04

TYROSINE HISTIDINE SOME BIOLOGICAL

Synthesis of Catecholamines
(Dopamine, Norepinephrine, Synthesis of Histamine USES OF AMINO ACIDS
Epinephrine
 General Qualitative Tests For Amino Acids

Reactive Group Test Visible Result

𝜶-Amino Group Ninhydrin Test Violet Complex

Amino Grp: Lys Schiff Test Pink-Violet Color

Guanidino Grp: Arg Sakaguchi Test Red-Orange Complex

Aromatic Ring: Tyr

Xanthoproteic Test Yellow-Orange Complex
& Trp

General Qualitative Tests For Amino Acids

Reactive Group Test Visible Result

Sulfhydril Grp Lead Acetate Test Black Lead Sulfide

Phenolic Ring: Tyr Millon’s Test Old-Rose/Red Ppt

Indole Ring: Trp Hopkin’s Cole Violet Complex

Peptide Linkages Biuret Test Blue-Violet Color

 CLASSIFICATION OF AMINO ACIDS
01. pH

Basic, Acidic or Neutral

02. Polarity

Polar or Non-polar

03. Metabolic Classification

Ketogenic, Glucogenic or Mixed/Both

04 Nutritional Classification

Essential, Non-essential or Semi-essential

01. pH
Amino Acids With Charged Polar Groups
Acid Glutamic Acid
Aspartic Acid
Basic Histidine
Arginine
Lysine
02. POLARITY Amino Acids With Non-Polar R-Groups
Alkyl R Group Alanine
Valine
Leucine
Isoleucine
Proline
Aromatic Group Phenylalanine
Tryptophan
S-Containing Methionine

02. POLARITY
Amino Acids With Unchanged Polar Groups
R-H Glycine
Hydroxyl Serine
Threonine
Tyrosine
Amide Asparagine
Glutamine
Sulfhydril Cysteine
 03. METABOLIC CLASSIFICATION
The carbon skeleton of amino acids can serve as a
precursor for the synthesis of glucose (glycogenic) or fat
(ketogenic) or both.
Glucogenic amino acids generate precursors of glucose or glycogen, such as
pyruvate or a citric acid cycle intermediate.

Ketogenic amino acids generate ketone bodies; fats can be synthesized from
amino acids.

Both: precursors for synthesis of glucose as well as fat

03. METABOLIC CLASSIFICATION

 03. METABOLIC CLASSIFICATION
Ketogenic, Glucogenic Or Both?

Leucine Phenylalanine Arginine

Lysine Isoleucine Alanine

Tyrosine Asparagine

Tryptophan Glutamine

04. NUTRITIONAL CLASSIFICATION

Essential Amino Acids

PVT TIM HALL
Phenylalanine Tryptophan Histidine
Valine Isoleucine Arginine
Threonine Methionine Leucine
Lysine
04. NUTRITIONAL CLASSIFICATION

Non-Essential Amino Acids

Triple A & Triple G Can Prick Some Tires (Tyrs)
Alanine Glutamic acid Cystine
Asparagine Glutamine Proline
Aspartic acid Glycine Serine
Tyrosine

AA AA AA

Peptides
unbranched chain of amino acids, each joined to the next by a peptide bond
that classified by the number of amino acids present in the chain

tripeptide
dipeptide oligopeptide
 BIOLOGICALLY IMPORTANT PEPTIDES
01. Peptide Hormone: Vasopressin/Anti-Diuretic Hormone
substance that decreases urine production; causes the kidneys to return more water to the blood
thus decreasing urine volume

02. Peptide Hormone: Oxytocin

enhances contraction of the smooth muscle cells in the wall of the uterus; stimulates milk ejection;
Synthetic Oxytocin: given to induce labor or to increase uterine tone and control hemorrhage just after
giving birth

03. Peptide Neurotransmitter: Enkephalins

produced by the brain which binds to receptor sites to reduce pain; Met-Enkephalin/Leu-Enkephalin

04 Peptide Antioxidant: Glutathione

regulator of oxidation–reduction reactions ; protect cellular contents from oxidizing agents such
as peroxides and superoxides

01 50-55%
Proteins Carbon

02
• naturally occurring, Oxygen
19-24%
unbranched polymer in
which the monomer units are
03
amino acids Nitrogen

13-19%
• most abundant organic Sulfur Hydrogen
molecules of the living system
05 04
• occur in every part of the cell 0-4% 6-7.3%
 CLASSIFICATION OF PROTEINS
01. Functional Classification
based on biological roles/functions

02. Complexity
• Simple Proteins: made up only of amino acid residues
• Conjugated Proteins: in combination with prosthetic group (non-protein)

03. Shape or Confirmation

• Fibrous: parallel fibers
• Globular: spherical form

01. FUNCTIONAL CLASSIFICATION

FUNCTION EXAMPLES

Structural Collagen, Elastin, Keratin & Glycoproteins ! "

Contractile/
Actin & Myosin #
Motile

Nutrient Ovalbumin & Casein $ %

01. FUNCTIONAL CLASSIFICATION
CLASSIFICATION EXAMPLES

Hormones Insulin &

Defenses Antibodies (IgA, IgG, IgD, IgE, IgM) '

Transport Storage Myoglobin, Hemoglobin & Ferritin (

02. COMPLEXITY
SIMPLE PROTEINS EXAMPLES/OCCURRENCE

ovalbumin in egg $
Albumins
serum albumin in blood (

ovoglobulin in egg white $

Globulins serum globulin in blood (
lactoglobulin in milk %

Glutelins glutelin in wheat )

02. COMPLEXITY
SIMPLE PROTEINS EXAMPLES/OCCURRENCE
Prolamins zein in corn *
(plant storage proteins) gliadin in wheat )

Albuminoids keratin, elastin & collagen + "

Histones histones in chromatin (DNA + histones) ,

Protamines salmin in salmon, sturin in fish sperm &

(basic proteins in
spermatozoa)
scombrine in mackerel - . /

02. COMPLEXITY
CONJUGATED PROSTHETIC
PROTEINS GROUP EXAMPLES/OCCURRENCE
(P +NP) (NP)
Phosphoproteins Phosphoric Acid Casein % & Ovovitellin 0

Nucleoproteins Nucleic Acid Nuclein (cell nucleus)

Glycoproteins Carbohydrate Mucin (saliva) 1

Chromoproteins Colored Compound Hemoglobin (

Lipoproteins Lipid LDL & HDL 2 3
Carbonic anhydrase (Zn) &
Metalloproteins Metal
Tyrosinase (Cu)⚡
03. SHAPE/CONFIRMATION
DESCRIpTION SHAPE EXAMPLES/OCCURRENCE

Fibrous
parallel fibers
and sheets in Collagen, Elastin & Keratin
structural
framework

Globular
compact
spherical forms & Antibodies, Hormones &
insoluble in Albumin
water

LEVELS OF STRUCTURAL ORGANIZATION

DESCRIpTION SHAPE EXAMPLES/OCCURRENCE

sequence of amino acids

Primary
resistant to denaturation

twisting and folding

Secondary
Hydrogen bonds
LEVELS OF STRUCTURAL ORGANIZATION
LEVEL SHAPE DESCRIPTION

3D structure with
Tertiary Disulfide , H-bond, Ionic &
Hydrophobic interaction

determines specificity
& arrangement of polypeptide
Quaternary
chains; multiple identical or
distinct polypeptide chains

METABOLISM
the sum total of all chemical reactions needed to maintain life

building up (simple to complex); endergonic (energy consuming)

Anabolism
e.g. Glycogenesis (addition of glucose units to stored glycogen)

breaking down (complex to simple); exergonic (energy producing)

Catabolism
e.g. Glycolysis (breakdown of glucose (C6) to pyruvate (C3)

combination
Amphibolism
e.g. Kreb’s Cycle
 METABOLISM
Enzyme a catalyst, it increases the rate of reaction

Substrate the reacting molecule (reactant) that binds to the enzyme

Co-enzyme required by enzymes to further exert catalytic activity

Product/s intermediate reaction species that is /are formed

Digestion
PROTEIN METABOLISM
Absorption

Transamination

Oxidative Deamination

Urea Cycle
 Digestion PROTEIN METABOLISM
• starts in the stomach
• proteins are denatured in the stomach by
the HCl present in gastric juice
• HCl activates the zymogen pepsinogen to
pepsin
• continues to the small intestines with the
release of enzymes in the pancreatic juice

Digestion PROTEIN METABOLISM

Enzyme
trypsin, chymotrypsin & elastase
carboxypeptidase
peptidases: aminopeptidase
peptidases: dipeptidase
Action
continue to break down proteins into
peptides
splits off the amino acid at the
carboxyl end of a peptide
cleaves off the amino acid at the
amino end of a peptide
splits dipeptides into single AA
 Absorption PROTEIN METABOLISM
• absorbed in the intestinal wall
• through the portal vein and
transported to the liver via
active transport (with
expenditure of energy)
• enter the bloodstream, which
distributes them throughout the
body

Transamination PROTEIN METABOLISM

• interchange of the amino group of an a-amino acid with the keto group of an
α-keto acid
• transfer of amino group from AA to keto acid
• key enzyme: transaminase
• co-enzyme: pyridoxal phosphate
 Oxidative Deamination PROTEIN METABOLISM
• liberation of free ammonia from the amino group
• release of ammonium ion
• key enzyme: glutamate dehydrogenase
• co-enzyme: NAD

Ammonia PROTEIN METABOLISM

• synthesis of non- essential amino
acids, purines, pyrimidines, amino
sugars, asparagine etc.
• maintain acid-base balance of the
body
• ❗ slurring of speech and
blurring of the vision and
causes tremors
• ❗ leads to coma and death
Urea Cycle
• ammonia has to be converted to its
less toxic and easily excreted form
which is urea
• urea so produced is then
transported in the blood from the
liver to the kidneys and eliminated
from the body in urine

• synthesis of non- essential amino acids, purines, pyrimidines, amino sugars,

 Urea Cycle PROTEIN METABOLISM
• carbamoyl phosphate: fuel for
urea cycle
• sites: mitochondria and cytosol
• End Product: Urea

• synthesis of non- essential amino acids, purines, pyrimidines, amino sugars,

03
ENZYMES & VITAMINS
 ENZYMES
proteins that catalyze nearly all the chemical
reactions taking place in the cells of the body
• Work best at temperatures between 35-40°C (optimal: 37°C)
• Activity is dependent on pH of the medium

ACTIVE SITE SUBSTRATE

part of the enzyme the reacting molecule
that participates in (reactant) that binds
the interaction with to the enzyme
a substrate

TERMS TO REMEMBER

CO-ENZYMES ZYMOGENS APOENZYMES

Vitamin Co-factors inactive form of an enzyme protein part of the
e.g. Pyridoxal phosphate e.g. Pepsinogen enzyme
from Vitamin B6

CO-FACTOR HOLOENZYME

non-protein part catalytically active enzyme (P+NP)

of the enzyme Apoenzyme + Co-Factor
CLASSES OF ENZYMES
DESCRIpTION EXAMPLES/OCCURRENCE
catalyzes an oxidation–reduction reaction;
requires a coenzyme
Oxidoreductase
(Glutamate dehydrogenase & HMG-
CoA reductase)
catalyzes the transfer of a functional group
Transferase from one molecule to another
(Phosphofructokinase & Transaminase)
catalyzes the break down of a substance with
Hydrolase the action of water
(Sucrase & Lactase)

CLASSES OF ENZYMES
DESCRIpTION EXAMPLES/OCCURRENCE
 catalyze the breaking a chemical bond
between 2 parts of a molecule through other
Lyase
means other than hydrolysis & oxidation
(Dehydratase & Decarboxylase)
-rearrangement of atoms of a substrate in a
reaction, converting it into a molecule isomeric
Isomerase
with itself
(Racemase & Phosphoglucoisomerase)
joins two molecules with the action of ATP
Ligase
(DNA Ligase)
 MODELS OF ENZYMATIC ACTION
Lock and Key Hypothesis
best explains the enzyme-substrate
• the active site has a distinctive configuration
• only the specific substrate molecules with the right shape can fit
into the active site to form enzyme-substrate complex

MODELS OF ENZYMATIC ACTION

Induced-Fit Model
adapts to incoming substrate
• the active site of the enzyme may change shape to fit the substrate
• the enzyme is flexible and molds to fit the substrate molecule.
 VITAMINS
Organic substances, not synthesized within the body, that
are essential in small amounts for the maintenance of
normal metabolic functions

FAT-SOLUBLE WATER-SOLUBLE
• A, D, E, K
• B1, B2, B3, B5, B6, B9, B12,
• released, absorbed, & transported
B15, B17, C, H,
with the fat of the diet
• not stored in the body
• not readily excreted in the urine
• excreted in the urine
• significant quantities are stored in
the liver and adipose tissue

TaRa Na PaPy Feeling Close

Vitamin B 1, 2, 3, 5, 6, 9, 12

Other Names

Functions

Deficiencies
 Vitamin Other Name/s & Deficiency
B1 Thiamine ❗ Beriberi, Wernicke-Korsakoff (CAN)

B2 Riboflavin ❗ Cheilosis, Glossitis, Seborrhea and Photophobia

B3 Niacin❗ Pellagra (3D: Dermatitis, Dementia & Diarrhea)

B5 Pantothenic acid ❗ Paresthesias of the extremities/Burning Foot
syndrome

B6 Pyridoxine ❗ Peripheral neuropathy, RBC fragility,

Hypochromatic microcytic anemia

B9 Folic Acid ❗ Megaloblastic anemia, Macrocytic anemia

B12 Cobalamin ❗ Pernicious Anemia (impaired intrinsic factor)

Vitamin Other Name/s & Deficiency

Vitamin A Retinol, Retinal, Retinoic acid & β-Carotene ❗ Nyctalopia
xerophthalmia & hyperkeratosis

Vitamin C Ascorbic acid ❗ Scurvy

Vitamin D Cholecalciferol, Ergocalciferol ❗ Rickets & osteomalacia

Vitamin E α-Tocopherol ❗ Neurologic dysfunctions (rare)

Vitamin H D-Biotin & Vit. B7 ❗ Impaired fat and CHO metabolism &
dermatitis
Vitamin K Menadione, Menaquinone, Phylloquinone ❗ Hemorrhage &
capillary fragility
 04
CARBOHYDRATES &
RELATED COMPOUNDS

CARBOHYDRATE
a polyhydroxy aldehyde, a polyhydroxy ketone, or a compound
that yields polyhydroxy aldehydes or polyhydroxy ketones upon
hydrolysis

Epimers: isomers that differ Epimers of Glucose

only in 1 carbon C2 – mannose & C4 – galactose
 01 02

SUGAR UNITS NUMBER OF CARBONS

• mono/di/oligosaccharide • pentose
• polysaccharide • hexose

03 04

FUNCTION FUNCTIONAL GROUP CLASSIFICATION OF

• storage • aldose CARBOHYDRATES
• structural framework • ketose

POINTS TO REMEMBER
MONOSACCHARIDES

GLUCOSE FRUCTOSE GALACTOSE

dextrose, blood sugar, fruit sugar, levulose, brain sugar, synthesized in
aldohexose, most biologically
ketohexose, sweetest the mammary glands, present
important in the chemical markers that
monosaccharide
60-90mg/dL distinguish blood type
 POINTS TO REMEMBER
DISACCHARIDES
SUCROSE LACTOSE MALTOSE
Glucose + Fructose Glucose + Galactose Glucose + Glucose
Table sugar Beer/Malt sugar
Milk sugar
produced from starch digestion
Non-reducing sugar

POINTS TO REMEMBER
PENTOSES

ARABINOSE RIBOSE DEOXYRIBOSE

Gum arabic/acacia found in RNA found in DNA

OLIGOSACCHARIDE
DEXTRIN
product of starch
degradation
 POINTS TO REMEMBER ABOUT POLYSACCHARIDES
HOMOPOLYSSACCHARIDES (same)

STARCH CELLULOSE
storage polysaccharide structural polysaccharide
in plants in plants
⍺ 1-4/⍺ 1-6 β-1,4

GLYCOGEN CHITIN
storage polysaccharide structural polysaccharide in
in humans insects & crustaceans
⍺ 1-4/⍺ 1-6 N-acetylglucosamine subunits

POINTS TO REMEMBER ABOUT POLYSACCHARIDES

HETEROPOLYSSACCHARIDES/GLYCOSAMINOGLYCANS (different)

HEPARIN CHONDROITIN KERATAN

anticoagulant used in combination found in nails
with glucosamine for
osteoarthritis

DERMATAN HYALURONIC ACID PEPTIDOGLYCAN

found in skin synovial fluid of bacterial cell wall
joints & vitreous
humor
 Chemical Tests For Carbohydrates

Name of the Test Objective Positive Result

Molisch Test Violet junction

General Tests
Anthrone Test Blue-green complex

For Starch and Deep blue for starch & Brown for
Iodine Test
Glycogen Glycogen

Seliwanoff’s Test For Ketohexose Red product in two minutes

Tollen’s Test Identifies Aldose Silver-mirror precipitate

Aniline Acetate For Pentose Bright Red color on the filter paper
Test

Chemical Tests For Carbohydrates

Name of the Test Objective Positive Result
Bial’s Test For Pentose Green, Red or Brown coloration

Insoluble precipitate or white crystals

Mucic Acid Test Identifies Galactose
in water

Black solution and/or precipitate

Nylander’s Test

Barfoed’s Test Reddish precipitate

For Reducing Sugars
“No BBF” Red, green, yellow precipitate
Benedict’s Test

Orange to brick-red precipitate

Fehling’s Test
 STAGES OF
METABOLISM

Digestion CARBOHYDRATE METABOLISM

• starts in the mouth by salivary alpha

amylase/ptyaline
• continues in the small intestines by
pancreatic ⍺-amylase
• sucrase, maltase, lactase act on the
disaccharides
 Fate of Glucose CARBOHYDRATE METABOLISM
AA Synthesis

glucose to AA to be incorporated to proteins

to AA ➡ Proteins
Glycogen Synthesis
“ Glycogenesis”
to Glycogen (Glycogenesis) glucose monomers to glycogen
Triglyceride Synthesis
“Lipogenesis”
to TGs (Lipogenesis)
glucose to glycerol and fatty acids
 Fate of Glucose CARBOHYDRATE METABOLISM

GLUCOSE CATABOLISM
oxidation of glucose to produce ATP is also known as cellular respiration, and it involves four
sets of reactions: glycolysis, the formation of acetyl coenzyme A, the Krebs cycle, and the
electron transport chain

Glycolysis AKA
Electron
Embden- Formation of
Krebs Cycle Transport
Meyerhof Acetyl CoA
Reaction
pathway

anaerobic
aerobic cellular aerobic cellular aerobic cellular
cellular
respiration respiration respiration
respiration
 GLUCOSE CATABOLISM
Glycolysis AKA Embden-Meyerhof
pathway
glucose ➡ 2 pyruvate + 2 NADH+H
1 mole of glucose ➡ 6-8 ATPs
anaerobic cellular respiration
(cytoplasm)
Three distinct phases:
A. Energy investment phase or priming stage
B. Splitting phase
C. Energy generation phase.

REACTION ENZYME PRODUCT/S

1.Phosphorylation of Glucose Hexokinase G6PO4 + ADP

2. Isomerization Phosphoglucoisomerase F6PO4

3. Phosphorylation Phosphofructokinase F1,6, biPO4 + ADP

4. Cleavage Aldolase 2 triosePO4: Dihydroxyacetone

phosphate (DHAP) & glyceraldehyde 3-
phosphate (G3P)

5. Isomerization Triosephosphate isomerase 2 glyceraldehyde3PO4

6. Oxidation & Glyceraldehyde phosphate-3 (2) 1,3-Bisphosphoglycerate

Phosphorylation dehydrogenase

7. Phosphorylation of ADP Phosphoglycerokinase (2) 3-Phosphoglycerate + ATP

8. Isomerization Phosphoglyceromutase (2) 2-Phosphoglycerate

9. Dehydration Enolase (2) Phosphoenolpyruvate

10. Phosphorylation of ADP Pyruvate kinase (2) pyruvate + ATP

 FATE OF PYRUVATE
Fate of Pyruvate depending on Oxygen
scarce (anaerobic conditions) plenty (aerobic conditions)
➡ Lactic Acid ➡ Acetyl CoA

• 2 pyruvate + 2 NADH +H ➡ • 2 pyruvic acid ➡ Acetyl CoA

Lactic acid + 2 NAD NADH+ H & CO2
• key enzyme: lactate • key enzyme: pyruvate
dehydrogenase dehydrogenase
• co-enzyme: NAD • co-enzyme: CoA
 GLUCOSE CATABOLISM
Krebs Cycle
Acetyl CoA ➡ CO2, ATP, NADH+H
& FADH2
Redox: NAD and FAD
Decarboxylation: release of CO2

final common oxidative pathway

in the mitochondria for
carbohydrates, fats and AA
 Reaction Enzyme Product/s

1. Condensation Citrate synthase Citrate (Can)

2. Isomerization Aconitase Isocitrate (I)

3. Oxidation and
Isocitrate dehydrogenase ⍺-Ketoglutarate (Keep)
Decarboxylation
4. Oxidation and ⍺-Ketoglutarate
Succinyl CoA (Selling)
Decarboxylation dehydrogenase
5. Phosphorylation Succinyl CoA synthetase Succinate (Shoes)

6. Oxidation Succinic dehydrogenase Fumarate (For)

7. Hydration Fumarate Malate (Money)

8. Oxidation Malate dehydrogenase Oxaloacetate (Officer?)

GLUCOSE CATABOLISM
Electron Transport Chain
NADH+H & FADH2 ➡ ATP + H20
the reduction of oxygen from the coenzymes NAD and FAD to water and
the series of exergonic reactions release small amounts of energy to
form ATP
chemiosmosis: passage of electrons along the transport chain) with the
pumping of H+
 GLUCOSE RELEASE & ANABOLISM

Glycogenesis Glucose ➡ Glycogen

Gluconeogenesis Fats/Proteins ➡ Glucose

Glycogenolysis Glycogen releases glucose

 GLUCOSE RELEASE & ANABOLISM
Glycogenesis
Glucose storage
⏰Too much glucose
glycogen synthase
Glucose ➡ Glycogen in skeletal muscles
and hepatocytes

(-) glucagon and epinephrine

(+) insulin

GLUCOSE RELEASE & ANABOLISM

Gluconeogenesis
Formation of Glucose from Proteins and Fats
⏰Depleting source of energy
glycerol ➡ glyceraldehyde ➡ glucose
AA or lactic acid ➡ pyruvic acid ➡ glucose or ➡
Krebs cycle
(+) cortisol, glucagon, thyroxine and triiodothyronine
 OTHER PRECURSORS OF GLUCOSE

glycerol of TGs ➡ glyceraldehyde ➡ glucose

AA or lactic acid
➡ pyruvic acid ➡ glucose
➡ Krebs cycle

GLUCOSE RELEASE & ANABOLISM

Glycogenolysis

Glucose release

⏰ Body requires energy

glycogen phosphorylase
Glycogen (n) ➡ Glycogen (n-1)

(+) glucagon and epinephrine

 Carbohydrate Metabolism
Digestion → Glucose Glycolysis → 2 Pyruvic acid

Pyruvic acid → Lactic Acid Pyruvic acid →Acetyl CoA

Acetyl CoA → Krebs Cycle

Electron Transport Reaction

Glycogenesis Gluconeogenesis
Glycogenolysis
store glucose glucose from fats and
release glucose
AA

PENTOSE PHOSPHATE PATHWAY

glucose is used to produce NADPH, ribose 5-phosphate
(a pentose phosphate), and numerous other sugar
phosphates

☝ Significance:
produce lipids: fatty tissue, the liver, mammary glands, and the
adrenal cortex (an active producer of steroid lipids)
☝ Site:
Cytosol
 PENTOSE PHOSPHATE PATHWAY
• synthesis of the coenzyme NADPH
needed in lipid biosynthesis
• production of ribose 5-phosphate, a
pentose derivative needed for the
synthesis of nucleic acids and
many coenzymes
• maintaining reduced Glutathione
inside RBCs

PENTOSE PHOSPHATE PATHWAY

Stages

Oxidative Non-Oxidative
• glucose 6-phosphate ➡ ribulose • ribulose 5-phosphate ➡ ribose 5-

5-phosphate + CO2 phosphate ➡ glyceraldehyde 3-

• Key enzyme: glucose-6- phosphate and fructose 6-

phosphate dehydrogenate phosphate
• Key enzyme: phosphopentose
isomerase
 PENTOSE PHOSPHATE PATHWAY
☝Net Reaction for the Oxidative Stage
Glucose 6-phosphate + 2NADP + H2O ➡
ribulose 5-phosphate +CO2 + 2NADPH + 2H

☝Net Reaction for Pentose Phosphate

3 Glucose 6-phosphate + 6NADP + 3H2O ➡ 2 fructose 6-
phosphate + 3CO2 + glyceraldehyde 3-phosphate + 6NADPH
+ 6H

That’s it for the first half!

Thank you very much for
your time and participation!