HOW?
Steps in urine formation
URINALYSIS
WHAT IS URINE?
 It is the fluid secreted by the kidneys,
transported by the ureters, stored in the
bladder, and voided through the urethra.
 Normal urine is clear, straw-colored, and
slightly acid; has the odor of urea (most
important constituent of urine); and has a
specific gravity between 1.003 and 1.035.
 Its normal constituents include water, urea,
sodium chloride, potassium chloride,
phosphates, uric acid, organic salts, and the
pigment urobilin.
 Abnormal constituent’s indicative of disease
includes ketone bodies, protein, bacteria,
blood, glucose, pus, and certain crystals.
 Normally people produce about 2 liters of urine a
day however the amount varies per day depending
on how much you drink, stress levels, illness etc.
 Typically, yellow-amber the color of urine varies
according to diet and concentration; drinking more
water generally means your wee will be less
concentrated.
WHY DO KIDNEYS PRODUCE URINE?
 To regulate blood composition and volume.
-Disposal of metabolic waste (Urea, creatinine,
ammonium, uric acid)
-Maintenance of water-salt balance
(Sodium, potassium, bicarbonate, etc.)
-Maintenance of acid-base balance
(Blood pH must be approx. 7.4)
 Urine is formed in nephrons
 About 1 million nephrons per kidney Each
DAY:
 Approx. 1000-2000 liters of blood flow though
kidney
 Approx. 180 L of filtrate processed Approx.
1.2 L of urine actually excreted the rest is
reabsorbed
Filtration- water and small molecules removed from
blood (Glomerular Filtration)
Reabsorption- water and essential molecules
returned to blood (Tubular Reabsorption)
Secretion- wastes and excess salts added from body
fluids to filtrate (urine) (Tubular Secretion)
FILTRATION
 It is the first process.
 20% of C.O.P pass to the kidney (filtration
fraction).
 As the blood passes through the glomeruli,
much fluids with useful substances (water,
Na, glucose) and waste products (urea) will
pass in the tubules.
 The GFR is 125 ml/min 180 L/day.
 If 200 liters of filtrate enter the nephrons each
day, but only 1-2 liters of urine result, then
obviously most of the filtrate (99+ %) is
reabsorbed.
REABSORPTION
 It is the passage of fluids from the renal
tubules to the
 peritubular capillaries.
 The useful particles reabsorbed from the
proximal convoluted tubule till the loop of
Henle.
 Water, 99% of the water filtrate is reabsorbed
by passive reabsorption.
 Glucose, actively reabsorbed in the proximal
tubules according to the renal threshold.
 Na, actively reabsorbed according to the diet.
SECRETION
 It is the reverse of reabsorption.
 It is either by active process or by diffusion.
  H +,K+, ammonia. Are the principle particles • Due to the presence of fresh blood
that is excreted by the kidney. (hematuria) or Hb (hemoglobinuria)
 H+ ions play an important role in acid base • Fresh blood will give smoky color while Hb
balance. gives clear reddish
URINE urine, which may be due to: -
 0.05% Ammonia • Urinary tract infection, Calculi,
 0.18% Sulphate Trauma
 0.12% Phospahate • Menstrual contamination.
 0.6% Chloride • Cancer kidney or cancer bladder
 0.01% Magnessium Dark brown:
 0.015% Calcium • Malignant Melanoma:
 0.6% Potassium Melanogen (Colorless) ──light─Melanin
 0.1% sodium (Brown).
 0.1% Creatinine • Nephritic syndrome (cola color of
 0.03% Uric Acid urine)
 2% Urea Black Urine: -
 95% Water • Alkaptonurea (ochronosis), a disease of
COLLECTION OF URINE tyrosine
 Use clean glass or plastic container metabolism.
 A morning (or over night) sample is best !!!
 If not processed within the hour, the specimen CHEMICAL EXAMINATION
should be preserved !! pH:
 Satisfactory methods of preserving urine include:  pH of urine varies in different species and
 Refrigeration individuals!!
 Formalin (few drops)  In man, acidity is found in fever and diabetes.
 Toluene (few drops)  Litmus paper or pH range paper are used to
measure the urine pH.
EXAMINATION OF URINE Characteristics of Normal Urine:
 Physical examination  Quantity:
 Chemical examination  Averages 1500 to 2000 ml in an adult
 Microscopic examination man daily.
 It may vary with the amount of fluid
PHYSICAL EXAMINATION taken.
Color:  In fact it is linked with the protein
Normal; yellow to amber Blood; brown to red color metabolism;
Bile; produce yellow foam Transparency:  Higher is the protein intake higher will
Normal urine; clear and not cloudy! be theurinary output since the urea
Odor: produced from the protein needs to
Ammonia is formed by bacterial urease action. be flushed out from the body.
Prominent in retained urine Acetone odor suggests  Higher is the urea production in the
ketosis body, the higher is the volume of
urine to excrete it.
Yellow – green  Specific gravity: It varies from 1.010 to 1.025.
• Biliverdin (greenish) just in abnormal cases Specific gravity is determined \ with
when there is liver cirrhosis urinometer.
• Which give a yellow foam & (- ve) test for  Odor: The odor is aromatic.
bilirubin  Reaction: The reaction of normal urine is
Blue – Green: slightly acidic with an average pH of 6.0.
• Pseudomonas Infection
Composition of normal urine:
Brownish yellow:  Water: Near about 96%
Hepatitis and obstructive jaundice, with excessive  Solids: Urea 2% and other metabolic
bilirubin in urine products 2%.
Bilirubin on shaking yellow foam will appear
Urobilin on shaking the foam has no color. Organic constituents
 Urea is one of the end products of protein
Pink – Red: metabolism. It is prepared from the
 deaminated amino-acid in the liver and  Yellow color of urine
reach the kidneys through blood circulation  by-product that results from the breakdown
(The normal blood urea level is 20-40 mg/dl). of hemoglobin
About 30 gram urea is excreted by the kidneys  effect of liver disease or obstructive biliary
daily. disease
 Other components include uric acid,  elevated bilirubin in the urine is termed
creatinine, electrolytes or salts such as bilirubinuria

Inorganic Constituents BILIRUBINURIA

 PHOSPHATES
 SULFATES
 CHLORIDES
 MAGNESIUM
 CALCIUM
 POTASSIUM
 SODIUM

ABNORMAL CONSTITUENTS OF URINE

ALBUMIN
 protein in the urine
 effect of damage or destroy in nephrons
 elevated albumin in the urine is termed
albuminuria
 microalbumin urine test GLUCOSE
Protein  the presence of glucose or blood sugar in
 Normally no protein can be demonstrated in urine is called glucosuria
urine by the usual tests  effect of diabetes
 Plasma protein can be detected in urine
during kidney disorders! GLUCOSURIA
 Presence of whole blood in urine would also
give a positive test for protein
 Protein can also be derived from pus and
mucus

Proteins found in urine in various pathological

conditions
*Plasma: Albumin, globulin and fibrinogen
*Red blood cells: haemoglobin & methaemoglobin
*Bence jone’s protein
*Protein from pus and mucus from UT or vagina in KETONE BODIES
female  the presence of ketone bodies in urine called
ketonuria
ALBUMINURIA  effect of diabetes or anorexia(eating
disorder)
 it may also be elevated during fasting and
starvation

MICROBES
BILIRUBIN
  the presence of microorganisms, such as
bacteria or fungus
 effect of urinary tract infection (UTI)

BLOOD
 the presence of red blood cells in urine called
hematuria
 gross or microscopic
 effect of renal or kidney disease and cancer

HEMATURIA
 gross hematuria means blood can be seen in
the urine
 microscopic hematuria means blood can be
seen only with a microscope

WHITE BLOOD CELLS

 the presence of white blood cells in urine
ABNORMAL EFFECT TEST
CONSTITUENTS
(CAUSE)
ALBUMIN Damaged nephrons Microalbumin
urine test
BILIRUBIN Liver disease or obstructive Blood test,
biliary disease urine test etc
GLUCOSE Diabetes Urine glucose
test
KETONE BODIES Diabetes or anorexia Spot test
MICROBES Urinary tract infection (uti) Urine culture
BLOOD Renal or kidney disease Blood test,
urine test etc
WBC Infections in the kidney or Blood test,
other organs of the urinary urine test etc
tract

 effect of infections in the kidney or other

organs of the urinary tract
 BLOOD HEMOPOEISIS
 A specialized connective tissue in which cells The process of blood cell formation
are suspended in fluid extracellular material Site of Hemopoeisis
called plasma.  yolk sac mesoderm
Propelled mainly by rhythmic contraction of the heart.  liver and spleen
Functions of the Blood:  bone marrow
• transport O2 and CO2 *at birth: liver and spleen undergoes hemopoeisis
metabolites *in adults: hemopoeisis occurs only at bone marrow
hormones
• regulate body temperature ERYTHROCYTES
• acid-base maintenance
• osmotic balance  a.k.a red blood cells
1. Plasma- 55% total volume of blood  contain O2 carrying haemoglobin
 Mostly liquid water (91%)  lack nuclei
 Soluble blood proteins (7%)  shape: biconcave disk
 Hormones (2%)  lifespan: 120 days
 Electrolytes (2%)  size: 7 um in dm
 Nutrients (2%) anisocytosis: RBC’s with great variation in size
2. Cellular Component-m 45% total volume of blood macrocytes- greater than 9um in dm microcytes- less
 White blood cells than 6um in dm
 Platelets approximate number of RBC
 Red blood cells women: 3.9- 5.5 million per microliter
men: 4.1 - 6 million per microliter
PLASMA
• the liquid part of the blood  ANEMIA
• an aqueous solution, pH 7.4 o Deficiency in normal hemoglobin
• carries nutrients, metabolites, antibodies , o Lack energy and excessively tired
hormones and protein
PLASMA PROTEINS: LEUKOCYTES
Albumin-58%  a.k.a white blood cells
Globulin-37%  the body’s defense against infections
Fibrinogen- 4%  have nucleus
 Albumin-58%  Lack hemoglobin
 most abundant plasma protein Divide into two groups:
 made in liver • granulocytes – possesses granules
 for the maintenance of osmotic pressure of • agranulocytes – don’t have spec. granules
the blood • approximate number of WBC
 Globulin-38% 5,000 -10,000 cu/ml
 made in liver more than 10,000 cu/ml - infection
 transferring and transport factor
 coagulation factor GRANULOCYTE
 are immunoglobulin (antibodies)  Neutrophils
 Fibrinogen- 4% • phagocytize bacteria
• largest plasma protein • 60-70% of WBC
• transport protein • leave the bloodstream via amoeboid
• block blood loss movement
• made in the liver. • does not undergo mitosis
Serum • size: 10-12 micra in dm
• A plasma without the clotting factor. • with 2-5 lobes of nucleus
• NEUTROPENIA
THE FORMED ELEMENTS  Eosinophil
• response and kills parasitic infection
• increased during allergic rxn.
• modulate local inflammation
• 1-4% WBC
• leave the bloodstream via diapedesis
• size: 11-14um in dm with 2 lobes
 • EOSINOPHILIC FOLLICULITIS BLOOD GROUPING
 Basophil an ANTIGEN
• containing heparin and histamine  is the substance that binds specifically to the
• usually found at the site of inflammation respective antibody.
• 0-1% WBC An ANTIBODY
• size: 10-12 micra  (also known as an immunoglobin (Ig), is a
• with 3 nuclear lobes forming S-shape large Y-shaped protein produced by B cells
• POLYCYTHEMIA VERA that is used by the immune system to identify
AGRANULOCYTES and neutralize foreign objects such as
 Lymphocytes bacteria and viruses.
• For adaptive immunity  Each antibody combine only with certain
• found outside of the blood vessels grouped antigen
in lymphatic organs
• undergo mitosis
• assist only in inactivation of foreign substance
• size: 6-14 um in dm
• with spherical nucleus
With 2 major functional group
a. B-cells – humoral immunity
b. T-cells – cellular immunity
 LEUKEMIA

 Monocyte *The antibodies of the DONOR will react to the

• become phagocytic and do not recirculate antigen
• precursors of macrophage, which of the RECIPIENT.
phagocytizes bacteria, dead cell, dead cell
and other debris in the body
• 3-8% of WBC
• size: 12-20 um in dm
• shape: kidney or horseshoe shape
• lifespan: 1 week

THROMBOCYTES Rh +
• a.k.a platelets  Have certain Rh antigens on the
• smallest formed element in the blood surface of their RBC.
• Produced in the red bone marrow from
megakaryocytes Rh –
• for blood clotting  Doesn’t possesses Rh antigens.
• It forms platelet plugs: seal up break in blood
vessel *Rarest combination is AB -
• lack nuclei
• shape: disc-like cell fragments
• size: 2-4 micra in dm
• lifespan: 8 days

Each platelets has :

• Hyalomere- maintains platelet’s discoid shape
• Granulomere- contains few mitochondria and
glycogen
• Approximate number of platelets
• 150,000 to 400,000 per cu. mm
• HEMOPHILIA
METABOLISM
1 MOLE MALTOSE = 2 MOLES OF GLUCOSE

1 MOLE OF GLUCOSE = 36ATP

-CATABOLISM OF GLUCOSE – GLYCOLYSIS – THEREFORE, 2 MOLES GLUCOSE X 36 ATP = 72 ATP

COMPUTATION OF ATP

HOW MANY NADH IS PRODUCED FROM 5 MOLES OF

GLUCOSE?
CARBOHYDRATES
1 MOLE OF GLUCOSE = 10 NADH
CATABOLISM OF GLUCOSE - GLYCOLYSIS -
COMPUTATION OF ATP 5 MOLES OF GLUCOSE X 10 NADH = 50 NADH

IN GLYCOLYSIS (1 CYCLE)

GLUCOSE + 2 NAD + 2ADP + 2 Pi →’ HOW MANY PYRUVIC ACID WILL BE PRODUCED FROM
20 MOLES OF GLUCOSE?
2 PYRUVATE + 2 NADH + 2H + 2 ATP + 2 H20
1 MOLE OF GLUCOSE = 4 PYRUVIC ACID

4 PYRUVICACID X 20 MOLES OF GLUCOSE = 80

PYRUVICACID

HOW MANY FADH2 IS PRODUCED FROM 15 MOLES

6 ATP 2 ATP OF GLUCOSE?

 2 NADH = 3ATP 1 MOLE OF GLUCOSE = 2 MOLES OF FADH2

 2 X 3 ATP = 6 ATP 15 MOLES OF GLUCOSE X 2 MOLES OF FADH2 = 30
 2 ATP MOLES OF FADH2
2ATP + 6 ATP = 8 ATP (GLYCOLYSIS) X 2 CYCLE =
16 ATP
LIPIDS
In KREB’S CYCLE: (1 CYCLE) CATABOLISM OF LIPIDS - COMPUTATION OF ATP

1 GTP = 1 ATP LIPIDS CATABOLISM

1 FADH2 = 2 ATP • BETA- OXIDATION - Oxidation of two (2) carbon

atoms in a lipid molecule forming ACETYL CoA
3 NADH = 9 ATP
• ACETYL Co-A - formation of two (2) carbon atoms
TOTAL = 12 ATP (KREB’S CYCLE) X 2 CYCLES = 24 ATP

16 ATP + 24 ATP = 40 ATP – 2 ATP = 38 ATP from

EXAMPLE: PALMITIC ACID = 16 CARBONS
liver
• 16 carbons / 2 = ? Acetyl CoA

• 8 Acetyl CoA
GLUCOSE COMES FROM MUSCLES
• (16 carbons / 2) - 1 = Number of Beta-oxidation
GLUCOSE COMES FROM MUSCLES = 36 ATP
• 8 - 1 =7 Beta-Oxidation  NADH = 3ATP
FOR EVERY ONE MOLE OF GLUCOSE
 FADH2 = 2 ATP

(7 X 3) + (7 X 2) + (8 X 12) = 131 ATP - 2 = 129 ATP

PRACTICE QUESTIONS:
NADH FADH2 KREB S CYCLE
HOW MANY ATP IS USED UP FOR THE DIGESTION OF
MALTOSE?
EXAMPLE: STEARIC ACID = 18 CARBONS • Digestion of Nucleic Acid - convert to basic
constituents (sugar, phosphate and nitrogenous bases
• 18 / 2 = 9 ACETYL COA
• Catabolism of N-bases/Nucleotides
• 18 / 2 - 1 = 9 - 1 = 8 BETA OXIDATION
• PURINES URIC ACID
• (8 X 3) + (8 X 2) + (9 X 12)
• PYRIMIDIENS MALONIC ACID
24 + 16 + 108 = 148 ATP
• XANTHINE - POINT OF CONVERGENCE FOR THE
148 atp - 2 atp (investment) = 146 ATP total to
METABOLISM OF PURINE BASES
hydrolyze stearic acid
• XANTHINE IS CONVERTED TO URIC ACID BY THE
ACTION OF XANTHINE OXIDASE
EXAMPLE: 13 MOLES OF LAURIC ACID = 12 CARBONS

• 12 / 2 = 6 Acetyl CoA
DEFECTS ASSOCIATED TO NUCLEIC ACID
• 12 / 2 - 1 = 6 - 1 = 5 beta oxidation METABOLISM:

• [5 beta- oxidation x 3 ATP (NADH)] + [5 beta- • ADENOSINE DEAMINASE (ADA) DEFICIENCY -

oxidation x 2 ATP (FADH2)] + [6 ACoA x 12 ATP SEVERE COMBINED IMUNODEFICIENCY
(KREB’S)]
• GOUT - CHARACTERIZED BY HYPERURICEMIA WITH
15 + 10 + 72 RECURRENT ATTACKS OF ACUTE ARTHRITIC JOINT

97 ATP - 2 ATP (INVESTMENT) = 95 ATP (1 MOLE OF • LESCH-NYHAN SYNDROME - X-LINKED RECESSIVE

LAURIC ACID) 95 ATP X 13 MOLES = 1 235 ATP INHERITED DISORDER ASSOCIATED WITH A VIRTUALLY
COMPLETE DEFICIENCY OF HYPOXANTHINE-GUANINE
PHOSPHORIBOSYL TRANSFERASE AND THEREFORE AN
INABILITY TO SALVAGE HYPOXANTHINE OR GUANINE
PROTEINS
 Gout: accumulation of uric acid salts in joints
CATABOLISM OF PROTEINS - COMPUTATION OF ATP
 Gout: accumulation of uric acid salts in joints
TWO PROCESSES:
 Gout:
• TRANSAMINATION - transfer of an amino group to
form a keto acid molecule  tophuses -accumulation of uric acid salts in
cartilages, under skin.
• DEAMINATION - removal of the amine group into
the keto acid molecule  Lesch-Nyhan Syndrom: is a inherited disorder
caused by a deficiency of the enzyme
• PRODUCE : NADH = 3 ATP hypoxanthine-guanine phosphoribosyltransferase.
LNS is present at birth in baby boys.

KREB’S CYCLE  NH3 (URINE)  Hypoxanthine and guanine are not used in the
salvage pathway of purine nucleotides synthesis.
PROTEIN CATABOLISM
 Hypoxanthine and guanine are not utilizied
• NADH = 3 ATP repeatedly but converted into uric acid.
• KREB'S CYCLE = 12 ATP o Symptoms:
• TOTAL = 15 ATP = 1 MOLECULE OF PROTEIN -severe gout

-severe mental and physical problems

NUCLEIC ACID DEGRADATION OF PYRIMIDINES

CATABOLISM OF NUCLEIC ACID • DEPHOSPHORYLATION

TWO PROCESSES: • DEAMINATION

• GLYCOSIDIC BOND CLEAVAGE

PYRIMIDINE NUCLEOTIDE CAN BE CATABOLIZED IN

THREE PATHWAYS:

• REDUCTIVE PATHWAY

• OXIDATIVE PATHWAY

• RUT PATHWAY

IMPORTANT NOTES ON THE PATHWAY

• CYTOSINE IS DEAMINATED TO URACIL

• URACIL IN LIVER FORMS B-ALANINE (fed to

panthothenic acid and co-enzyme A biosynthesis

• Converted to Malonyl Co-A

• THYMINE IS DEGRADED TO B-AMINO

ISOBUTYRATE which is converted to methyl malonyl
Co-A
METABOLISM
Metabolic pathways refer to the fate of individual
molecules after digestion and absorption. These pathways
are classified as follows:
1. Anabolic pathways, those involved in the
synthesis of macromolecules
2. Catabolic pathways, those which involve oxidative
processes that release free energy usually in the
form of high-energy phosphate.
3. Amphibolic pathways, those which act as links
between the anabolic and catabolic pathways.
The interrelations between these three pathways
os shown below:
Amphibolic
Anabolic <------------------→ Catabolic
ANABOLIC PATHWAYS
ž The products of digestion upon reaching the cells
are used by the cells in the biosynthesis of
macromolecules, nucleic acid, proteins,
carbohydrates, and lipids.
ž These biosynthetic mechanisms require energy
(ATP, GTP,CTP, TTP) and specific enzymes.
ž Biosynthesis takes place in the cell during the
growth of the organism where new cellular
materials are formed and in non-growing mature
organism, where the macromolecules are
constantly synthesized and degrade, thus the rate
of formation of new molecules is balanced by the
rate of degradation of existing molecules.
BIOSYNTHESIS OF DNA
Steps:
1. Initiation of replication
 accomplished by an endonuclease which cuts one
of the sugar-phosphate backbone strands at
specific points, followed by the breaking of the
purine-
pyrimidine bonds, resulting in the “unzipping” of the
double-stranded DNA
 formation of a “replication bubble” which extends
as a Y-shaped replication fork
2. Unwinding of template DNA
 accomplished by unwinding proteins which bind
to the single strand of DNA near the replication
fork, destabilizing the double helical portion of the
molecule
3. Priming
 formation of short segments of primer RNA
(catalyzed by RNA polymerase) attached to the
3’end of the template strand
 discontinuous synthesis of primer RNA in a 5’ to 3’
direction producing okazaki fragments
4. Polymerization
 closure of gaps on the double-stranded DNA by
the action of polymerases (I-fills gap; II – closes
gap)
5. Linking of the DNA strands to each other by forming H-
bonds; catalyzed by DNA ligase
BIOSYNTHESIS OF RNA
 all synthesized on a DNA template by the action of
polymerases
 requires a bivalent cation
INHIBITORS OF NUCLEIC ACID SYNTHESIS
1. Structural analog of intermediates and cofactors
involved in purine and pyrimidine biosynthesis
a. 5-fluoro deoxyuridine – inhibits thymidylate
reaction
b. aminopterin and amethopterin – inhibits
production of coenzymes
c. 6-mecaptopurine – inhibits conversion of AMP
and GMP
2. Antibiotics
a. d-actinomycin – inhibits transcription of
DNA
b. rifamycin – inhibits RNA polymerase
BIOSYNTHESIS OF PROTEIN
Steps:
1. Transcription – formation of mRNA which contains
the codon (triplet nucleotides) coding for the
sequence of amino acids
2. Translation – formation of polypeptide chain
which is coded for by mRNA
a. amino acid activation
b. transfer of activated amino acid to tRNA
c. assembly of polypeptides
 30S subunit of the first ribosome attaches to
mRNA at an initiator site, coded for by a specific
group of three nucleotides
 tRNA met (formylmethionine) with the first amino
acid binds to the 30S subunit at the p- site (3
protein initiation factors “IF” plus GTP are
required)
 larger 50S subunit attaches to 30S subunit and
completes assembly of the first ribosome
 second charged tRNA binds to the first ribosome
at the letters A-site, so that both sites are
occupied; the P-site with the first tRNA and the A-
site with the second
 peptide bond is formed enzymatically (peptidyl
synthetase in 50S) between the amino group of
the second amino acid and the carboxyl group of
the first
 transfer of the second amino acid residue to the
A-site (elongation factor needed “EF”)
 ejection of tRNA
 translocation of movement of tRNA dipeptide
from the A to the P site and movement of the
mRNA and ribosome relative to each other which
brings the previous A site (with its amino acid)
into location at the P site
 third charged tRNA moves to position at the new
A site
  repetition of these steps until a termination codon FROM FATS
(UGA, UAG, UAA) is reached

d. chain termination and release

BIOSYNTHESIS OF CARBOHYDRATES
 involves energy-rich systems
a. UDP glucose for synthesis of glucose,
starch, cellulose, glycogen
b. ADP glucose for starch
c. GDP glucose for cellulose
d. UDP galacturonic acid for pectin
e. GDP mannose for mannans
f. UDP-N-acetylglucosamine for
glycoproteins
g. GMP-acetyl neuraminic acid for
glycoproteins
h. UDP galactose for glycoproteins

 The conversion of absorbed glucose to glycogen

(glycogenesis) and its breakdown (glycogenolysis)
occurs mainly in the liver. It involves a compound,
uridine diphosphoglucose (UDPG), where glucose
is added to the nonreducing end of the glycogen
chain in an alpha-1-4 linkage.
 Steps in Glycogen Biosynthesis
Glucose ATP→ Glucose-6-phosphate
Glucose-6-phosphate→Glucose-1-phosphate Glucose-1-
phosphate UTP→ UDP-glucose UDP-glucose glycogen→
glycogen
BIOSYNTHESIS OF LIPIDS
Steps in biosynthesis of fatty acids
1. formation of a 3-carbon intermediate, malonyl-
CoA which is formed in three ways:
a. malonic acid + CoA → malonyl-CoA
b. malonic acid + succinyl-CoA transferase→
malonyl-CoA + succinate
a. CO2 + acetyl-CoA + biotin-E → malonyl-
CoA
b. malonyl-CoA + acetyl CoA NADPH→ 4-
carbon chain
3. repetition of above steps would result in elongation,
yielding successively 6, 8, 10, 12, 14, and finally a 16-
carbon fatty acid like palmitic acid

Steps in the biosynthesis of triglycerides

2. conversion of fatty acids to triglycerides or
phospholipids by combination with glycerol
a. formation of glycerophosphate either by:
FROM PROTEIN 1. glycerol + ATP or
2. dihydroacetone phosphate + NADH
→glycerophosphate + NAD
1. Glycerophosphate + 2 molecules of
activated fatty acids→phosphatidic acid
Biosynthesis of cholesterol and other steroids

 derived from acetate with acetyl CoA, ATP,

NADPH, Mg, glutathione, and a variety of enzymes
 steroids are derived from cholesterol by various
modifications of the basic 4-ring compound,
cyclopentanopherhydrophenanthrene skeleton
CHOLESTEROL SYNTHESIS
 Lipid, hydrophobic
 Required precursor
o Vitamin D
o Steroids
o Membrane stability
o Bile salts
 Structure
o 4 non-aromatic rings
o 1 carbon double bond
o 1 side chain
o 1 hydroxyl group
 Approximately 65% of plasma cholesterol stored
as cholesterol ester
 Most active production occur in:
o Liver
o Adrenal glands
o Intestines
o gonads