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I. Vitamins
II. Types of Vitamins
a. Fat-Soluble
b. Water Soluble
III. Coenzymes
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I. VITAMINS
❖Vitamins are low molecular weight organic compounds required in
small amounts in the diet.
❖Most of the vitamins are not synthesized in the human body but are
synthesized by the plants.
❖Though most of them are present in the diet as such, some are
present as precursors known as provitamins.
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VITAMIN D
1. • Increases protein synthesis in intestinal cells.
2. • Activates active transport of calcium by intestinal
cells.
3. • Increases release of calcium by mitochondria.
4. • Promotes normal bone calcification.
5. • Regulates phosphorus and calcium metabolism.
6. • Increases renal tubular reabsorption of calcium.
7. • It does not have any coenzyme activity.
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a. B1 – thiamine
b. B2 – riboflavin
c. B3 – Pantothenic acid
d. B5 – Niacin
e. B6 – Pyridoxine
f. B7 – biotin
g. B9 – folic acid
h. B12 - Cobalamin
✓Inositol, cholic, and para-aminobenzoic acid are vitamin-like
substances sometimes classified as part of the B complex, but no
convincing evidence has been shown so far to be included as vitamins.
2. Vitamin C
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III. COENZYMES
✓COENZYMES- An organic molecule that associates with enzymes
and affects their activity.
✓SUBSTRATE- A molecule that is acted upon, and chemically
changed, by an enzyme.
✓ APOENZYMES- is the protein part of an enzyme.
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III. COENZYMES
https://www.biologyonline.com/dictionary/apoenzyme
III. COENZYMES
https://biologyreader.com/difference-between-cofactor-and-coenzyme.html
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III. COENZYMES
Mechanism of Coenzyme Action
1. Coenzyme accelerates the enzymatic reaction by helping the formation of the product
(s) by acting as acceptor for one of the products.
2. The substrate combines with the apoenzyme to form activated complex.
3. But this combination takes place in the presence of coenzyme.
4. The bond in the substrate is strained and ruptured when one of the cleavage products
is directly transferred to the coenzyme, which has suitable receptor site in its
structure.
5. The other cleavage product now dissociates from the apoenzyme liberating the
enzyme protein for fresh reaction.
6. The cleavage product attached to the coenzyme is next released from the surface of
the coenzyme after the completion of enzyme action.
7. Now both apoenzyme and coenzyme are regenerated to their original form and are
ready for fresh reaction.
8. A prosthetic group also acts in a similar fashion with the difference that the prosthetic
group is firmly attached to the surface of the apoenzyme.
https://biologyreader.com/difference-between-cofactor-and-coenzyme.html
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III. COENZYMES
The structure and coenzyme functions of B-complex group
vitamins:
1. Thiamine
-The two important reactions in which funthiamine
pyrophosphate (TPP) ctions as coenzyme are:
❑ • Oxidative decarboxylation of a-keto acids such as pyruvate
and a ketoglutarate.
❑ • Transketolase reaction.
III. COENZYMES
2. Riboflavin
❑-The flavin mononucleotide (FMN) and
flavin adenine dinucleotide (FAD) are
the two-coenzyme forms of riboflavin.
❑ FMN and FAD serve as prosthetic groups
of oxidation-reduction enzymes known as
flavoenzymes or flavoproteins.
❑They are usually tightly, but not covalently,
bound to the protein.
❑Many flavoproteins contain one or more
metals as additional cofactors and are
known as the metalloflavoproteins.
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III. COENZYMES
3. Niacin
❑The coenzyme forms of Nicotinamide adenine dinucleotideacin are
(NAD+) and with phosphate group is NADP+ which function as the
coenzymes of a large number of oxidoreductases collectively called as
pyridine-linked dehydrogenases.
❑These coenzymes are bound to the dehydrogenase protein relatively
loosely during the catalytic cycle and therefore serve as substrate than as
prosthetic group.
❑They function as electron acceptors during the enzymatic removal of
hydrogen atoms from specific substrate molecules
III. COENZYMES
4. Pyridoxine
❑The coenzyme form of pyridoxine is
known as pyridoxal phosphate (PP)
❑The most common type of reaction
requiring PP as a coenzyme is
transamination.
❑Enzymes catalyzing such reactions are
known as transaminases or
aminotransferases.
❑PP also acts as coenzyme in the
decarboxylation, desulfuration, transulfuration
reactions associated with amino acid
metabolism.
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III. COENZYMES
5. Panthothenic Acid
❑The coenzyme form of pantothenic acid is coenzyme A and is
represented as CoASH.
❑The thiol group (-SH) acts as a carrier of acyl group.
❑The function of coenzyme A is to serve as a carrier of acyl group
in reactions associated with fatty acid oxidation, fatty acid
synthesis, pyruvate oxidation and biological acetylations.
❑It is also involved in many biosynthetic processes such. as
synthesis of cholesterol, terpenes and steroids.
III. COENZYMES
6. Biotin
❑The important function of biotin is its role as co enzyme for carboxylase,
which catalyzes carbon dioxide fixation or carboxylation reaction.
❑The epsilon amino group of lysine in carboxylase enzymes combines with
the carboxyl group of biotin to form covalently linked biotinyl carboxyl
carrier protein (BCCP or biocytin).
❑This serves as an intermediate carrier of carbon dioxide.
❑The carboxylation of acetyl CoA to malonyl CoA in presence of acetyl CoA
carboxylase requires biotin as coenzyme.
❑Propionyl carboxylase and pyruvate carboxylase are also associated with
biotin.
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III. COENZYMES
7. Folic Acid
❑The coenzyme form of folic acid is tetra hydro folic acid.
❑Tetrahydro folic acid is associated with one carbon metabolism.
❑The tetrahydro folic acid serves as a carrier of single carbon
moieties such as formyl, methenyl, methylene, formyl or methyl
group.
❑It is involved in the biosynthesis of purines, pyrimidines, serine,
methionine and glycine.
III. COENZYMES
8. Lipoic Acid
❑The oxidized and reduced
forms of lipoic acid.
❑Lipoic acid functions as a
coenzyme in pyruvate and
a-ketoglutarate
dehydrogenase
multienzyme complexes.
https://www.researchgate.net/publication/321755087_Potential_Therapeutic_Effec
ts_of_Lipoic_Acid_on_Memory_Deficits_Related_to_Aging_and_Neurodegeneration
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III. COENZYMES
9. Cobalamin
❑The 5-deoxyadenosyl cobalamin
and methyl cobalamin function as
coenzyme forms and are required
for the action of several enzymes.
❑Methyl malonyl CoA mutase uses
5-deoxyadenosyl cobalamin as
coenzyme.
❑Methyl cobalamin functions as a
carrier of methyl group to
homocysteine and convert it to
methionine
https://www.researchgate.net/profile/Bettina-Riedel
5/publication/237237924/figure/fig1/AS:339893000654868@1458048214953/Structu
re-of-cobalamin_W640.jpg
III. COENZYMES
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ANNOUNCEMENTS:
1. Group Reporting = TBA
Topics to be uploaded today in LMS.
Group yourselves, then choose your topic.
2. Final Exam = TBA
3. Remaining Requirements
a. Problem Set 3
c. Reporting
d. Final Exam
REFERENCES:
1. Gajera, H.P. (2008). Fundamentals of Bicohemistry A Textbook.
International Book Distributing
2. https://www.cnet.com/health/nutrition/the-best-food-sources-of-
every-vitamin-and-mineral/
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