Vitamins

Dr Tharanga Thoradeniya, PhD

MSc Nutrition 2019
Hunger…!!!
Hidden hunger…!!!!!!!!!!!
What do you know
about VITAMINS?
A bit of History…
• Casimir Funk, a Polish biochemist, isolated (antiberiberi)
substance from rice polishing
Named it “Vitamine” Vital amine Thiamine
Contains an amine group
Vital for life
•McCollum & Davis extracted a factor from butter
Named fat-soluble A
Each additional discovered …….was given a letter.
Later, what was thought to be one single substance turned
out to be many, so they added numerical subscripts
B-vitamins: B1, B2, B3, B5, B6, B12
Some confusion arose as to which vitamins were really
necessary, resulting in gaps between numerical subscripts.
Eg. B8 (adenylic acid),B13 (orotic acid) were removed from
the list of essential vitamins.
Some other substances, originally designated as different,
were later found to be the same.
Eg. H, M, S, W, and X were all eventually shown to be biotin.
As chemical structures were discovered a chemical name
was given
They were not only amines so “e” was dropped
Today, chemical names are used to help prevent confusion.
 Some facts about vitamins……
• Organic compounds
• Essential to human health
Involved in fundamental functions of the body

• Needed in very small amounts in the diet

Vitamins are measured in I.U.s (International Units) or
on the basis of weight (mg or μg).
For an average adult only 2.5μg of vit. B12 per day
helps prevent pernicious anemia.
(1 g can supply 400,000 people!)
Known as “micronutrients”
Some are not dietary essentials
• Vitamin D
• Niacin containing coenzymes are derived from Tryptophan

• Absence is usually manifested as some deficiency disease

which is corrected only by supplying the vitamin
Keratomalacia caused by Same eye one month
Vitamin A deficiency after treatment
Before treatment
• Most vitamins are chemically altered in some way so
they can function in the body.
•Dietary Reference Intakes (DRI) and
Recommended Dietary Allowances (RDA)
These are suggested levels of essential nutrients considered
adequate to meet nutritional needs of healthy individuals
Learning outcomes
At the end of this teaching learning session
You should be able to…
• Recognize that vitamins can be classified, based on solubility as
well as function.
• Relate their chemical properties to the way in which they are
absorbed, transported and stored in the body.
• Explain the role of vitamin A and vitamin D in modulating
protein synthesis.
• Explain the role of vitamin E, β carotene and vitamin C as
antioxidants.
• Explain the role of vitamin K in γ carboxylation of proteins.

• Briefly explain how the coenzyme forms of B vitamins take part

in dehydrogenation, carboxylation, transamination and one
carbon transfer reactions.
• List the biochemical functions of ascorbic acid.
 Vitamins
Fat soluble vitamins Water soluble vitamins
Vitamin K (phylloquinone)
Vitamin A (retinol) Vitamin B Vitamin C
Vitamin D (calcitriol) complex (ascorbic acid)
Vitamin E (tocopherols)

Functional division

Energy releasing
Thiamin (B1)
Haematopoietic
Riboflavin (B2)
Folate
Niacin (B3)
Vitamin B12 (Cobalamin)
Biotin
Pantothenic acid (B5) Other
Vitamin B6 (pyridoxine)
Fat soluble vitamins and water soluble vitamins differ in
their chemical properties

Therefore, handling by the body during the following

Will be different

• Absorption

• Transport

• Storage
What are the differences
between fat-soluble and
water-soluble vitamins?
 Water Soluble Fat Soluble
Absorption

Transport
Storage
Excretion
Toxicity
Deficiency symptoms

Requirement
 Water Soluble Fat Soluble

Absorption Passive or active diffusion Require bile salts

(some need carriers:B12) Incorporated into micelles,
passive diffusion

Transport Portal vein to liver Lymphatic system to liver

Storage Not stored in appreciable Stored in adipose tissue,

amounts except for B12 except for vit K

Excretion Excess excreted in urine when Minimal, a little lost in bile

renal threshold exceeds

Toxicity At high doses? At relatively low doses,

dangerous/fatal (except for vit K)

Deficiency symptoms Develop rapidly, Slow to develop,

overlapping symptoms except in children

Requirement Required on a daily basis Not required on a daily

Except for vitamin C basis
 Fat Soluble Vitamins

You should be able to…

•Relate chemical properties of water soluble

vitamins to the way in which they are

•absorbed

•transported and

•stored in the body.

You should be able to…

•Explain the role of vitamin A and vitamin D in

modulating protein synthesis.

•Explain the role of vitamin A in vision.

•Explain the role of vitamin E and β carotene as

antioxidants.

• Explain the role of vitamin K in γ carboxylation of

proteins.
Vitamin A and -carotene
 Discovery of vitamin A

• Link between nutrient deficiency & night

blindness and drying of the eye
• McCollum (1913) showed that some animal fats
eg. butter, egg yolk or cod liver oil cured
these eye disorders.
• Named it fat-soluble A
• Later it was called Vitamin A
Chemical structures of vitamin A
Retinoids •Poly isoprenoid tail
•Contains cyclohexenyl ring
Retinol
•Polar end group
Retinal
Retinoid acid
pre-formed vitamin A

provitamin A
Chemical structures of biologically active retinoids
Figure 1 Chemical structures of some biologically active retinoids

Biochemical Journal www.biochemj.org Biochem. J. (2000) 348, 481-495

 Vitamin A and -carotene
Β-carotene (in plant tiss.)
provitamin
 -carotene Retinol (in animal tiss.)
Diet Preformed

Retinol esters

Intestine, liver
CH=O
Dioxygenase Retinol dehydrogenase
All trans Retinal
Zn 2+, Zn 2+, NADH, H+
bile
Conversion is
salts
not efficient All trans Retinol
(1/6)
6µg β carotene= 1µg retinol

COO
11-cis Retinal
Retinoic acid
Absorption, transport and storage of vitamin A
RBP: retinol binding protein
 Functions of vitamin A
• Protects against anaemia
- promotes red cell proliferation
- promotes better utilisation of stored iron
• Required for vision in dim light (rod cells of retina)
• and for colour vision (cone cells)

Two types of photoreceptor cells

• Rods
• Cones
Vitamin A and function in vision in dim light
Retina
Retinol all-trans retinol
(Protein bound) Retinol isomerase Retinol dehydrogenase
Zn 2+
all-trans retinal
11-cis retinol Retinol isomerase
Retinol dehydrogenase
Zn 2+
11-cis retinal

Opsin
Rhodopsin (11-cis retinal opsin)
Trigger a
neuronal
signal to
All-trans retinal brain
 normal Night blindness

Can see
objects
 Impaired vision in dim light is
an early sign of vitamin A deficiency
conjunctival xerosis
large Bitot spot

vitamin A deficiency
Explain the role of vitamin A in
vision.
Plasma retinolVitamin A acts as a steroid hormone
(Protein bound)

Retinol
Target cell
Retinoic acid

Retinoic acid

binds to
intra-nuclear
receptors

Activation of
specific genes

Synthesis of specific proteins

Cellular differentiation
Explain the role of vitamin A in
modulating protein synthesis.
• Modulate protein synthesis
gene expression & tissue differentiation

Role of vitamin A in gene expression

• Growth

• Reproduction
• Mucous secretion:
glycoprotein synthesis – vitamin A
carries oligosaccharides across membrane

• Maintains epithelial cell integrity:

retinoic acid - epithelial cell differentiation

• Involved in immune response

Vitamin A in excess can cause toxicity
- Hypervitaminosis A
 Importance of carotenoids
• Some carotenoids have provitamin A activity

• Carotenoids show antioxidant properties

- help to scavenge oxygen free radicals at low oxygen tensions

– Thus protect against many chronic degenerative diseases

esp. cancer, cardiovascular disease

Foods rich in retinol (pre-formed vitamin A)

• Liver (fish liver - richest source)

• Egg yolk
• Butter, milk & other milk products
• Fortified foods eg. margarines
• Breast milk for infants
Pre-formed vit. A more effective in improving vit. A
status than carotenoids

RAE = Retinol activity equivalents

1 µg RAE = 1 µg all trans retinol = 3.33 IU
 Foods rich in provitamin A carotenoids

• Yellow fruits eg. papaw, mango

• Carrots, pumpkins, yellow sweet potatoes
• Dark green leafy vegetables

1 µg RAE is equivalent to:

6 µg -carotene in oils (highly absorbable)
12 µg -carotene in foods
24 µg of other provitamin carotenoids
in mixed foods
 Stability of vitamin A

• Destroyed by heat, specially in the presence of light

Should be stored in dark bottles
• Retinyl esters are more stable
• Vitamin E reduces oxidation
 Review/Recall

Vitam Active Major Deficienc Toxicity Dietary

in form functio y sources
ns

Vit A Retinol Functio Night Hypervita Liver, egg

, n in blindness minosis A yolk,
retinal, vision, ,………… butter,
…….. milk, yellow
fruits,
DGLV
 Vitamin D
•Active form:
•1,25-dihydroxycholecalciferol (Calcitriol)

Vitamin D2 – ergocalciferol:
found in plants

Vitamin D3 – cholecalciferol:
found in animals
Vitamin D production requires UV
light (sunlight)
• Vitamin D3 is synthesized in the skin

Skin

25-hydroxylase

Liver 25 -hydroxycholecalciferol
1- hydroxylase

1,25 -dihydroxycholecalciferol
Kidney
(calcitriol) - active form
Functions of vitamin D
Function as a hormone

• Main function- Ca absorption & homeostasis

Maintains adequate plasma levels of calcium

When necessary, calcitriol can:

➢ increase uptake of calcium by the intestine: by increasing
the gene expression of calcium binding proteins

➢ minimize loss of calcium by the kidney

➢ stimulate bone resorption

➢Affects synthesis & secretion of parathyroid & thyroid Hormones

Acts like a steroid hormone - binds to nuclear receptor protein

 1,25 -dihydroxycholecalciferol
(calcitriol) - active form

Calcium homeostasis
Target organs

intestine bone kidney

Ca ++ absorption Essential for bone Ca ++

mineralisation & reabsorption
resorption
 kidney
liver 25-H D3
25-H D3 Increase Ca
++

reabsorption
+ -
Low Ca
Parathyroid H +
1,25-diH D3
Thyroid Calcitonin
+

intestine
+
+
- Increase Ca ++
bone absorption
Ca ++ resorption
Calcium homeostasis
 1,25-diOH D3
Intestinal cell
1,25-diOH D3

1,25-diOH D3

binds to
intra-nuclear
receptors

Activation
of specific
genes

Ca2+ binding protein

+
Ca2+ Ca2+
Explain the role of vitamin D in modulating
protein synthesis.
 Other functions of Vitamin D

• Controls cell differentiation

• Affects the immune system specially CMI

• Other roles of vitamin D

Vitamin D & health in the 21st century: bone & beyond. Am J Clin Nutr
80(6): Dec. 2004
Factors influencing synthesis in the skin

• Season, latitude, time of day & degree of exposure of skin

• Solar radiation responsible for causing wrinkles & skin

cancer (in genetically susceptible people) is the same
radiation for producing vitamin D
- Advise people, specially elderly that exposure to
morning or late afternoon for vitamin D synthesis &
less damaging to skin
 Vitamin D deficiency

• Rickets

• Maternal vitamin D deficiency during pregnancy:

- linked to maternal osteomalacia

- neonatal hypocalcaemia & tetany

• Placental transfer of vitamin D to fetus important because of

low vitamin D content in human milk (vary from 0.3-0.9 ug/L)

• Vit. D & Ca protect against osteoporosis

Vitamin D in excess can cause toxicity- Hypervitaminosis D
 Vitamin E
Two families tocopherols tocotrienoles

Most active form: D-α-tocopherol

Vitamin E does not have a precisely defined function

Role in cell signaling ?

• Main function:

as major lipid soluble antioxidant in non-enzymetic oxidation

of cell membranes & plasma lipoproteins

As such is associated with mem. Lipid structures/lipoproteins etc

Premature infants are born with inadequate vitamin E stores.
Erythrocyte membranes become fragile as a result of
Peroxidation-----Lead to haemolysis
Trigger:Vitamin E prevents damage to cell membrane.
 Peroxidation

Metabolic reactions free radicals

Peroxidation (auto oxidation) of lipids ---

form peroxide radicals

Lipid peroxidation; a chain reaction

Dangerous

Vitamin E is a chain-breaking, free radical-trapping

antioxidant
 Free radical
chain reaction

PUFA - OO• PUFA - OOH

R

α-tocopherol-OH α-tocopherol-O• Relatively

O2 R• (reduced) unreactive
(oxidized)
Polyunsaturated FA - H
(in phospholipids)

Enzymetical
ly or non-
Vitamin C (oxidized) Vitamin C (reduced)
enzymetical
GS-SG GS-SG
ly form PUFA – OOH, GSH
non- H2O2
reactive Superoxide
Catalase Glutathione
compounds dismutase Se
peroxidase
O•-2
Superoxide H2O,
PUFA – OH GS-SG
Vitamin E (D-α-tocopherol) as an antioxidant

• First line of defense against membrane

phospholipid peroxidation

• effective at high PO2 : RBC membrane

: respiratory tree

β-Carotene as an antioxidant
• Traps peroxy free radicals formed in tissues
• Functions at low PO2
• Complements vitamin E function in the body
Explain the role of vitamin E and β carotene as
antioxidants.
Dietary sources
• Seed oils - soyabean, gingelly, sunflower, palm & corn
oil, nuts, whole grains
• Breast milk imp. source for infants

Functions
• Nature’s most powerful fat-soluble antioxidant - prevents
lipid peroxidation
• Maintenance of cell membrane integrity
• Anti -inflammatory effects
• Inhibits platelet aggregation
Deficiency

Premature infants born with inadequate stores

- haemolytic anaemia in premature infants
- bronchopulmonary dysplasia,
retinopathy & intraventricular
haemorrhage linked to vit. E deficiency
but causal role not demonstrated
 Vitamin K
Active forms: Phylloquinone (K1)
(in green vegetables)

Menaquinone (K2) (synthesised by intestinal bacteria)

menadione (K3) (synthetic)

• Functions -
cofactor for carboxylation of glutamate in post-
translational modification of calcium binding proteins
• synthesis of blood clotting proteins
• synthesis of bone Ca binding protein- osteocalcin and bone
matrix Gla protein
(osteocalcin also contains hydroxyproline so dependant on vitamin C as well.)
Carboxylation of glutamate to form γ –Carboxy-glutamyl residue
polypeptide
Precursors of
clotting factors Glu
II,VII.IX,X Glutamate residue
COO -

Vitamin K-hydroquinone
(coenzyme)
O2
Vitamin K
epoxidase
γ carboxylase Reductase

Vitamin epoxide
CO2
Mature clotting
factors
II,VII.IX,X Glu
γ –Carboxyglutamate
COO - COO - residue
Chelates Ca2+
 cofactor for carboxylation of glutamate in post-
translational modification of calcium binding
proteins

• synthesis of bone Ca binding protein- osteocalcin

and bone matrix Gla protein (and several other bone
proteins)

vitamin K is necessary for bone health

Explain the role of vitamin K in γ- carboxylation
of proteins.
Functions
Required as a coenzyme for -carboxylation of:
- clotting factors
- bone Ca binding proteins
Important for: haemostasis, early skeletal development &
maintenance of healthy bone
Deficiency
- prolonged prothrombin time
- decreased plasma  -carboxylated proteins
Primary deficiency is rare in adults
May occur as a consequence of GI disorders leading to
malabsorption, Use of vitamin K antagonists
New born
May arise due to: limited placental transfer, low content in BM,
low liver reserves, low gut bacterial flora
Dietary sources

Vitamin K1 - phylloquinone
plants: green leafy vegetables
some vegetable oils & legumes

Vitamin K2 -menaquinone (bact. Origin)

liver
fermented foods -cheese, yoghurt
gut bacterial synthesis
True or false?

A. Intestinal absorption of β carotene is greater than

the absorption of preformed vitamin A
B. Intestinal absorption of retinol is enhanced when
taken with oil
C. Vitamin D increases calcium absorption by inducing
calcium binding proteins
D. Vitamin K is a coenzyme in γ carboxylation of blood
clotting factors
E. Vitamin K is needed for the synthesis of calcium
binding protein in the bone.
 Summary

Fat Soluble Vitamins

Structurally related compounds with different biological

activity
• Vitamin A – All trans retinol, retinal, RA
hormone like activity
• Vitamin D – Cholecalciferol (Vit. D3)
precursor of a hormone
• Vitamin E – tocopherols
membrane bound antioxidant
• Vitamin K – phylloquinone: K1,
precursor of a coenzyme
 Review/Recall

Micro Active Major Deficiency Toxicity Dietary

nutrient form functions sources

Vit A Retinol, Function Night Hypervitamin Liver, egg yolk,

retinal, in blindness,… osis A butter, milk,
vision,……. ……… yellow fruits,
. DGLV
 Water Soluble Vitamins

Most vitamins are precursors of coenzymes

 Learning outcomes

At the end of this teaching learning session

You should be able to…

• Briefly explain how the coenzyme forms of

B vitamins take part in;
dehydrogenation,
carboxylation,
transamination and
one carbon transfer reactions.

• List the biochemical functions of ascorbic acid.

 Water soluble vitamins

• Not stored in appreciable amounts except for B12

• Readily excreted in urine when renal threshold is
exceeded
• Toxicity rare
• Most converted to coenzymes & used in energy
generation or haematopoiesis
• Overlapping symptoms/signs, rapidly growing
tissues most affected eg. nerve tissue
• Deficiency of single B vitamin is rare – present
with multiple deficiency states
 Vitamin B1 (Thiamin)

+
ATP

TPP synthase
AMP

Active form: Thiamin pyrophosphate (TPP)

TPP has a key role in CHO metabolism
TPP acts as a coenzyme
1. Oxidative decarboxylation reactions
Eg: In CHO metabolism
TPP provides a reactive carbon,
which helps in decarboxylating the substrate
Deficiency of
Pyruvate dehydrogenase B1
Pyruvate Acetyl-CoAIncreases
TPP
CO2
plasma
lactate &
pyruvate
α-ketoglutarate dehydrogenase
α-ketoglutarate Succinyl-CoA
TPP
CO2

(citric acid cycle & amino acid metabolism)

2. Transketolase reactions
(Pentose Phosphate Pathway - PPP)

Ribose 5-phosphate
Xylulose 5-phosphate
Transketolase TPP

Sedoheptulose 5-phosphate

Glyceraldehyde 3-phosphate
 Vitamin B2 (Riboflavin)
Riboflavin B2
Active forms
Flavin mononucleotide (FMN)

Flavin adenine dinucleotide (FAD)

Riboflavin has a central role in energy yielding metabolism

Flavin coenzymes are electron carriers: in oxidoreduction reactions
Tightly bound to flavoenzymes
Required in dehydrogenases
Enzyme catalyses
electron transfer
reduced substrate oxidized substrate

Energy
2H+ + 2e-
FAD FADH2
FMN FMNH2

Temporarily hold electrons

Free energy trapped
 reduced substrate oxidized substrate

FAD 2H+ FADH2

FMN FMNH2
oxidized reduced
Temporarily hold electrons
Free energy trapped

Reactions in: mitochondrial respiratory chain, fatty acid and

amino acid oxidation, citric acid cycle
 Vitamin B3 (Niacin)
Niacin B3
Nicotinamide
Nicotinic acid
Active forms:
Nicotinamide adinine dinucleotide (NAD+)

Nicotinamide adinine dinucleotide phosphate (NADP+)

NAD+; accepts a hydride ion (:H-)
in oxidation-reduction reactions

reduced substrate oxidized substrate

:H-
NAD+ NADH + H+
NADP+ NADPH + H+
oxidized reduced
 Coenzyme for dehydrogenases
Eg: Lactate dehydrogenase & malate dehydrogenase

NAD+ linked NADP+ linked

Oxidation-reduction reactions Reductive
in oxidative pathways biosynthetic pathways

Both NAD+ and NADP+ move form one enzyme to another

Source of ADP-ribose:
ADP-ribosylation of proteins
DNA repair mechanisms
 Vitamin BPantothenic
5 (Pantothenic
acid B5 acid)

Active form: Coenzyme A

Coenzyme A
HS - pantothenate

Thiol group carries the acyl group

Pantothenic acid is metabolised to two main cofactors

- Coenzyme A (CoA) and
- Acyl Carrier Protein (ACP)
CoA in reactions in:
Citric acid cycle,
Acetylations,
Cholesterol synthesis
Fatty acid oxidation

Fatty acid synthesis

CoA and ACP both are essential for the synthesis of FA

Pyruvate dehydrogenase complex -

TPP
Coenzyme A
FAD
NAD+
& lipoic acid
 Vitamin B6
Pyridoxine
Pyridoxal
Pyridoxamine

Active form: pyridoxal phosphate

Pyridoxamine phosphate
Carries amino groups

• Transaminase: OAA + glutamate Asp +alpha KG

• Deamination: serine pyruvate + NH3
• Decarboxylation: histidine histamine + CO2
• Glycogen metabolism (glycogen phosphorylase)
• important in steroid hormaone action
 Biotin

Active form: Biotin

 Carboxylation reactions

Substrate product
carboxylase - biotin – coo-

Pyruvate carboxylate
Eg. Pyruvate oxaloacetate

•Acetyl-coenzyme A (CoA) carboxylase (ACC)

•Methylcrotonyl-CoA carboxylase
•Propionyl-CoA carboxylase
 Folate
Folic acid (Pteroyl glutamate)
Active form: Tetrahydrofolate (THF)

Reductase
Dietary folate THF

2NADPH +2H+ 2NADP+

 STRUCTURE OF FOLIC ACID

There are
multiple
forms of
folate in
the diet
May have
upto 7
additional
glutamate
residues
Function: Carrier of one carbon units
Methyl
Methylene interconvertible
Formyl

Amino acid
synthesis
THF Methylene-THF
TMP
formate Methenyl-THF
DNA

Formyl-THF Purine synthesis

CO2
 Vitamin B12 (Cobalamine)

Active form: Central cobalt atom

One substituent varies:

1. CH3 – methyl cobalamine

2. deoxyadenosyl cobalamine

• Absorbed bound to ‘intrinsic factor

• Intrinsic factor only binds free
active vitamin B12
Methylation:
Homocysteine Methionine
1.Methionine synthase

Methyl-THF Methylcobalamin
Vitamin B12 THF

• Regeneration of THF
• Synthesis of methionine

Isomerisation:
2.Methylmalonyl-CoA isomerase
Methyl malonyl-CoA Succinyl CoA
Vitamin B12

3.Leucine aminomutase
Lets try to answer a question … a thinking question !

High doses of folic acid alone given as treatment for

megaloblastic anaemia can mask vitamin B12
deficiency in elderly.

Briefly Explain the biochemical basis.

Folate deficiency and megaloblastic macrocytic anaemia
 “Folate trap” – functional folate deficiency

Homocysteine Methionine
Methionine synthase

5 Methyl-THF Methylcobalamin
Vitamin B12
THF

MTHFR

5-10-methylene THF

only reaction regenerating THF from N5-methyl-THF.

If blocked all THF will eventually end up trapped as N5-methyl-tetrahydrofolate.
Lets look at the question again

High doses of folic acid alone given as treatment for

megaloblastic anaemia can mask vitamin B12
deficiency in elderly.

Briefly Explain the biochemical basis.

 Vitamin C

Active form: Ascorbic acid

A reversible biologic reductant

Transfers hydroxyl group
Ascorbic acid acts as a reducing agent
oxidised to dehydroascorbic acid
 Functions
• As a cofactor for reactions requiring a reduced metal iron
(Fe2+, Cu2+)

• Copper-containing hydroxylases
Ascobic acid
Cu2+ Cu+
reduced

• Iron-containing hydroxylases
Hydroxylases - modification of proteins
Eg: Hydroxylation of proline in collagen synthesis
Cofactor for proline and lysine hydroxylases

- stabilizes the structure & enhance H bonding

Super twisted coil is right-handed,

made of 3 left-handed α-chains
 • Non-enzymetic reducing agent
can readily donate electrons to
-reactive free radicals and oxygen species
to reduce - molecular oxygen
nitrate
cytochrome a, c
-Other biological antioxidents to regenerate active reduced form

• Reduces lipid peroxidation by

- scavenging peroxyl radicals before they initiate lipid peroxidation

- regenerating active form of vitamin E (antioxident)

 Free radical
chain reaction

PUFA - OO• PUFA - OOH

R

α-tocopherol-OH
O2 R• α-tocopherol-O•
Polyunsaturated FA - H
(in phospholipids)

Vitamin C (oxidized) Vitamin C (reduced)

GS-SG GS-SG
PUFA – OOH, GSH
H2O2
Superoxide
Catalase Glutathione
dismutase Se
peroxidase
O•-2
Superoxide H2O,
PUFA – OH GS-SG
• In iron metabolism:
Reduction of Fe3+ to Fe2+ by ascorbic acid:
required in iron transfer and storage pathways
Enhance iron absorption in the gut

Other functions
• Carnitine biosynthesis

• Degradation of tyrosine
Tyrosine epinephrine synthesis
• Bile acid formation

• Inhibit nitrosamine formation during digestion

A. Vitamin A is required for vision in dim light.
B. Folate and vitamin B12 are coenzymes in amino acid metabolism.
C. Deficiency of folate leads to elevated plasma homocysteine
concentrations.
D. Vitamin D regulates protein synthesis.
E. Retinoic acid has a role in the regulation of gene expression and
tissue differentiation.
F. Vitamin K deficiency leads to defected blood coagulation.
G. Vitamin E is the major lipid-soluble antioxidant in cell membranes
and plasma lipoproteins.
H. Vitamin K is important in synthesis of bone calcium binding protein.
I. Vitamin C deficiency leads to deficient collagen synthesis.
 Summary
• Vitamins can be classified, based on solubility as well as
function.
• Absorption, transportation and storage in the body-
related to their chemical properties.
• Explain the role of vitamin A and vitamin D in
modulating protein synthesis.
• Explain the role of vitamin E, β carotene and vitamin C
as antioxidants.
• Explain the role of vitamin K in
γ carboxylation of proteins.
• Briefly explain how the coenzyme forms of
B vitamins take part in dehydrogenation, carboxylation,
transamination and
one carbon transfer reactions.
• List the biochemical functions of ascorbic acid.
• Further reading:
- Harper’s Illustrated Biochemistry
- Lippincott’s Illustrated Reviews - Biochemistry

Vitamins like compounds

Choline
Inositol
Carnitine
Lipoic acid