Vitamin B is a group of eight water-soluble vitamins that play a crucial role in

various bodily functions. These vitamins include thiamine (B1), riboflavin (B2),
niacin (B3), pantothenic acid (B5), pyridoxine (B6), biotin (B7), folate (B9), and
cobalamin (B12).

Cobalamin (vitamin B12)

Structure of cobalamin: It contains 63 carbon, 14 nitrogen, and one cobalt atoms.
Four pyrrole rings coordinated with a cobalt atom is called a corrin ring. The 5th
valiancy of the cobalt is covalently linked to a substituted benzimidazole ring.
This is called cobalamin.

Source of vitamin B12

Not present in vegetables. Liver is the richest source. Meat, fish, and egg are
good sources. Curd is a good source, because lactobacillus can synthesize B12.

Dietary sources and availability

Most microorganisms, including bacteria and algae, synthesize vitamin B12, and
they constitute the only source of the vitamin. The vitamin B12 synthesized in
microorganisms enters the human food chain through incorporation into food of
animal origin. In many animals gastrointestinal fermentation supports the growth
of these vitamin B12- synthesizing microorganisms, and subsequently the vitamin
is absorbed and incorporated into the animal tissues. This is particularly true for
the liver, where vitamin B12 is stored in large concentrations. Products from these
herbivorous animals, such as milk, meat, and eggs. constitute important dietary
sources of the vitamin unless the animal is subsisting in one of the many regions
known to be geochemical deficient in cobalt. Milk from cows and humans
contains binders with very high affinity for vitamin B12, whether they hinder or
promote intestinal absorption is not entirely clear. Omnivores and carnivores.
including humans, derive dietary vitamin B12 from animal tissues or products (ie..
milk. butter, cheese, eggs, meat, poultry. etc.). It appears that no significant
amount of the
required vitamin B12 by humans is derived from micro flora, although vegetable
fermentation preparations have also been reported as being possible sources
of vitamin B12.
Requirement of vitamin B12
Normal daily requirement is 1-2 µg\day. During pregnancy and lactation, this is
increased to 2µg\day. Those who take folic acid should also take vitamin B12.

Functional role of B12

Vitamin B12 is required in humans for two essential enzymatic reactions: the
synthesis of methionine and the isomerization of methylmalonyl CoA that is
produced during the degradation of some amino acids, and fatty acids with odd
numbers of carbon atoms. When the vitamin is deficient, abnormal fatty acids
accumulate and become incorporated into cell membranes, including those of
the nervous system. This may account for some of the neurologic manifestations
of vitamin B12 deficiency.

Deficiency of vitamin B12

1. Deficiency of vitamin B12 causes simultaneous folate deficiency due to the

folate trap. Therefore, all the manifestations of folate deficiency are also seen. In
the peripheral blood, megaloblasts and immature RBCs are observed.

2. Damage to nervous system, the subacute combined degeneration, is unique

to B12 deficiency and associated with folate deficiency.
3. Mild deficiency may cause depression, confusion, and less alertness.
4. Pernicious anemia
5. Atrophic gastritis

Pyridoxine (vitamin B6)

Vitamin B6 is a collective term for pyridoxine, pyridoxal, and pyridoxamine, all
derivatives of pyridine. They differ only in the nature of the functional group
attached to the ring. Pyridoxine occurs primarily in plants, whereas pyridoxal and
pyridoxamine are found in foods obtained from animals. All three compounds
can serve as precursors of the biologically active coenzyme. Pyridoxal
phosphate functions as a coenzyme for many enzymes, particularly those that
catalyze reactions involving amino acids.
Toxicity of pyridoxine
Neurologic symptoms have been observed at intakes of greater than 2 g/day.
Substantial improvement, but not complete recovery, occurs when the vitamin is
discontinued.

Source of vitamin B6
Rich sources are dried yeast, rice polishing, wheat germs, cereals, legumes
(pulses), oil seeds, egg, milk, meat, fish and green leafy vegetables. A part of Bo
requirement is met by the bacterial synthesis in the intestine.

Requirement of B6
It is recommended that adults need 1 to 2 mg/day. During pregnancy and
lactation, the requirement is increased to 2.5 mg/day.

Thiamine (vitamin B1)

Thiamine pyrophosphate (TPP) is the biologically active form of the vitamin,

formed by the transfer of a pyrophosphate group from ATP to thiamine. Thiamine
pyrophosphate serves as a coenzyme in the formation or degradation of a-
ketols by transketolase and in the oxidative decarboxylation of a-keto acids.

Deficiency of thiamin (B1)

Thiamin (vitamin B1, aneurin) deficiency results in the disease called beri-beri,
which has been classically considered to exist in dry (paralytic) and wet
(oedematous) forms. Beriberi occurs in human-milk-fed infants whose nursing
mothers are deficient. It also occurs in adults with high carbohydrate intakes
mainly from milled rice and with intakes of anti-thiamin factors. Beri-beri is still
endemic in Asia. In velatively industrialized nations, the neurologic reflections of
Wernicke-Korsakoff syndrome are frequently associated with chronic
alcoholism with limited food consumption. Some cases of thiamin deficiency
have been observed with patients who are hyper-metabolic, are on parenteral
nutrition, are undergoing chronic renal dialysis, or have undergone a
gastrectomy.
Requirement of thiamine
vitamin B₁ requirements ranges between (1-1.5)mg/day. Thiamine is useful in the
treatment of beriberi, alcoholic polyneuritis, neuritis of pregnancy and neuritis of
old age.

Niacin (B3)
Niacin, or nicotinic acid, is a substituted pyridine derivative. The biologically
active coenzyme forms are nicotinamide adenine dinucleotide (NAD) and its
phosphorylated derivative, nicotinamide adenine dinucleotide phosphate
(NADP+) Nicotinamide, a derivative of nicotinic acid that contains an amide
instead of a carboxyl group, also occurs in the diet. Nicotinamide is readily
deaminated in the body and, therefore, is nutritionally equivalent to nicotinic
acid. NAD and NADP* serve as coenzymes in oxidation-reduction reactions in
which the coenzyme undergoes reduction of the pyridine ring by accepting a
hydride ion (hydrogen atom plus one electron. The reduced forms of NAD and
NADP are NADH and NADPH. respectively.

Sources of niacin
Niacin is found in unrefined and enriched grains and cereal, milk, and lean
meats, especially liver. Limited quantities of niacin can also be obtained from the
metabolism of tryptophan.
Function of niacin
Niacin is chemically synonymous with nicotinic acid although the term is also
used for its amide (nicotinamide). Nicotinamide is the other form of the vitamin,
which does not have the pharmacologic action of the acid that is administered at
high doses to lower blood lipids. It is the amide form that exists within the redox-
active co-enzymes, nicotinamide adenine dinucleotide.
(NAD) and its phosphate (NADP), which function in dehydrogenase-reductase
systems requiring transfer of a hydride ion. NAD is also required for non-redox
adenosine diphosphate-ribose transfer reactions involved in DNA repair and
calcium mobilisation. NAD functions in intracellular respiration and with
enzymes involved in the oxidation of fuel substrates such as glyceraldehyde 3-
phosphate, lactate, alcohol, 3-hydroxybutyrate, and pyruvate. NADP functions in
reductive biosynthesis such as fatty acid and steroid synthesis and in the
oxidation of glucose- 6-phosphate to ribose-5-phosphate in the pentose
phosphate pathway.
Deficiency of niacin
Niacin (nicotinic acid) deficiency classically results in pellagra, which is a chronic
wasting disease associated with a characteristic erythematous dermatitis that is
bilateral and symmetrical, a dementia after mental changes including insomnia
and apathy preceding an overt encephalopathy, and diarrhoea resulting from
inflammation of the intestinal mucous surfaces. Pellagra-like syndromes
occurring in the absence of a dietary niacin deficiency are also attributable to
disturbances in tryptophan metabolism (e.g., Hartnup disease with impaired
absorption of the amino acid and carcinoid syndrome where the major catabolic
pathway routes to 5-hydroxytryptophan). Pellagra also occurs in people with
chronic alcoholism.

Riboflavin (vitamin B2)

The two biologically active forms are flavin mononucleotide (FMN) and flavin
adenine dinucleotide (FAD), formed by the transfer of an AMP moiety from ATP to
FMN and FAD are each capable of reversibly accepting two hydrogen atoms,
forming FMNH₂ or FADH2. FMN and FAD are bound tightly- sometimes covalently
to flavoenzymes that catalyze the oxidation or reduction of a substrate.
Functions of riboflavin Conversion of riboflavin to flavin mononucleotide (FMN)
and further to the predominant flavin adenine dinucleotide (FAD) occurs before
these flavins form complexes with numerous flavoprotein dehydrogenases and
oxidases. These flavocoenzymes (FMN and FAD) participate in oxidation-
reduction reactions in metabolic pathways and in energy production via the
respiratory chain.
Toxicity
Riboflavin toxicity is not a problem because of limited intestinal absorption.
Dietary sources of riboflavin
Rich sources are liver, dried yeast, egg, whole milk and milk powder. Good
sources are fish, whole cereals, legumes, and green leafy vegetables. Riboflavin
toxicity is not a problem because of limited intestinal absorption.
Daily requirement
Adults on sedentary work require about 1.5 mg/day. During pregnancy and
lactation, an additional 0.2-0.4 is required.
Biotin (B7)
Biotin is a coenzyme in carboxylation reactions, in which it serves as a carrier of
activated carbon dioxide for the mechanism of biotin-dependent carboxylations).
Biotin is covalently bound to the e-amino groups of lysine residues of biotin-
dependent enzymes. Biotin deficiency does not occur naturally because vitamins
are widely distributed in food. Also, a large percentage of the biotin requirement
in humans is supplied by intestinal bacteria. However, the addition of raw egg-
white to the diet as a source of protein induces symptoms of biotin deficiency,
namely, dermatitis, glossitis, loss of appetite, and nausea. Raw egg white contains
a glycoprotein avidin which tightly binds biotin and prevents its absorption from
the intestine. However, with a normal diet, it has been estimated that 20 eggs per
day would be required to induce deficiency syndrome. Thus, inclusion of an
occasional raw egg in the diet does not lead to biotin deficiency.

Functions of biotin
Biotin functions as a co-enzyme within several carboxylases after the carboxyl
function of the vitamin becomes amide linked to the ɛ-amino of specific lysyl
residues of the apoenzymes. In humans and other mammals, biotin operates
within four carboxylases. Three of the four biotin dependent carboxylases are
mitochondrial (pyruvate carboxylase, methylcrotonyl-CoA carboxylase, and
propionyl-CoA carboxylase) whereas the fourth (acetyl- CoA carboxylase) is
found both in mitochondria and the cytosol. In all these cases biotin serves as
carrier for the transfer of active bicarbonate into a substrate to generate a
carboxyl product.

Toxicity
Toxicity is not a problem because of limited intestinal absorption of biotin.