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BIOLOGICAL ROLE OF VITAMIN-A
1. Retinol and retinoic acid have role in
   normal reproduction
2. Retinal has a role in visual cycle
3. Retinoic acid has a role in glycoprotein
   synthesis
4. Roll in MPS synthesis
5. Vitamin-A is needed for mitochondrial
   membrane function
6. Anti cancer role: β-carotene is an
   antioxidant and trap peroxy free radicals
   in tissues at low partial pressure of O 2
7. Role in reproduction
8. Bone and teeth formation is slow
BIOCHEMICAL ACTIONS OF
           CHOLECALCIFEROL
1. Vitamin-D promotes absorption of Ca ++ and
   P by the intestine. It stimulates the
   synthesis of a specific Ca++ binding protein
   by intestinal epithelium.
2. Vitamin-D induces the synthesis of specific
   Ca++ binding protein in bones
3. Vitamin-D regulates the Ca++ level by
   reabsorbing Ca++ through the kidney
4. Vitamin-D promotes mineralization of
   bones through deposition of Ca++ and P in
   growing bones.
5. Vitamin-D increases the reabsorption of
   PO4 through renal tubules.
6. Vitamin-D acts as coenzyme for alkaline
   phosphatase
7. Vitamin-D is responsible for enameling of
   the teeth. Its deficiency leads to irregular
   and rough teeth
8. Vitamin-D promotes growth in general and
   is essential for normal health. BMR is
   decreased in vitamin-D deficiency. The
   deficiency of vitamin-D leads to the
   repeated attacks of respiratory diseases.
BIOCHEMICAL ACTIONS OF
         VITAMIN-E
1. Antioxidant role: Vitamin-E is the most
   potent natural antioxidant.
2. Removal of Free radicals: Vitamin-E
   removes free radicals, prevents their
   peroxidative effects on unsaturated lipids
   of membrane and thus maintains integrity
   of membranes.
3. Protective role: i. Vitamin-E prevents
   massive hepatic necrosis produced on diet
   deficient in sulphur containing aminoacids.
4. Role in reproduction: It is required for
   normal reproduction, muscle integrity and
   for resistance of erythrocytes to hemolysis.
5. Role in Heme Synthesis: Vitamin-E also
   takes part in the synthesis of heme.
   Vitamin-E induces enzymes ALA-synthase
   and ALA-dehydratase.
6. A derivative of vitamin-E is said to be
   necessary for the synthesis of CoQ which
   is the component of mitochondrial electron
   transport chain.
BIOLOGICAL ACTIONS OF VITAMIN-K
1. Vitamin-K is needed for formation of
   proconvertin: It is needed for the formation
   of prothrombin. Deficiency of vitamin K
   decreases proconvertin level in blood.
2. Vitamin-K modifies prothrombin: Vitamin-K
   is a coenzyme in modification of
   prothrombin to thrombin.
3. Vitamin-K modifies other clotting factors
   also: Vitamin K is needed for maintenance
   of normal levels of blood clotting factors II,
   VII, IX and X. All these factors are
   synthesized in the liver in their zymogen
   forms. Their conversion to biologically
   active forms depends upon vitamin K. The
   activation involves carboxylation of
   glutamyl residues in the molecules of
   these factors (including prothrombin also)
   to form dicarboxylic glutamyl residue.
4. Vitamin-K is needed for carboxylation of
   glutamyl residue of Ca++ binding transport
   between the flavin coenzyme and the
   cytochrome system.
FACTORS CAUSING VITAMIN-K
             DEFICIENCY:
•   Surgical removal of intestine:
•   Liquid paraffin:
•   Antibiotic therapy for a long time:
•   Vitamin-K antagonists: Heparin and warfarin
BIOCHEMICAL FUNCTIONS:
              THIAMINE
•    TPP [cocaroxylase] being an essential
     part of the decarboxylating
     dehydrogenases acts as a cofactor in
     many important reactions in carbohydrate
     metabolism i.e., dehydrogenase [PDH]
     complex and α-ketoglutarate
     dehydrogenase [αKGDH] complex
i.   Oxidative Decarboxylation of α-ketoacids
ii. Conversion of α-Ketoglutarate to succinyl-
     SCoA
iii. TPP acts as coenzyme in reactions
     catalyzed by transketolase
iv. Tryptophan metabolism:

           Tryptophan pyrrolase
Tryptophan            N-formylkynurenine
                   O2
v. TPP is a coenzyme for mitochondrial
     branched chain α-ketoacid
     dehydrogenases [decarboxylases] which
     oxidatively decarboxylate α-ketoacids
     formed in the catabolsim of valine, leucine
     and isoleucline.
vi. In the nervous system: TPP is a cofactor
     for the synthesis of acetylcholine.
vii. TPP also acts as a coenzyme [co-
     carboxylase] for pyruvate carboxylase in
     yeast for non-oxidative decaroxylation of
     pyruvate to acetaldehyde.
BIOCHEMICAL FUNCTIONS OF
          RIBOFLAVIN:
A- Biochemical role of FMN as a coenzyme
1. FMN as a part of redox potential
2. FMN is a coenzyme for L-amino acid
   oxidases:
3. FMN being a part of Cut. C reductase
4. FMN also accepts 2H+ from NADH+H+
5. FMN is a coenzyme for Warburg’s yellow
   enzyme [a component of respiratory chain]
B- FAD is a coenzyme for the following
   enzyme:
Like FMN, FAD is also is a part of
   mitochondrial respiratory chain
1. D-aminoacid oxidases: The enzymes
   catalyze reaction similar to L-aminoacid
   oxidases but with FAD as coenzyme.
2. Aldehyde oxidase
3. Acyl-CoA dehydrogenase of the β
   oxidation of fatty acids
4. Succinate dehydrogenase, an enzyme of
   citric acids cycle and converts succinate
   to fumarate in mitochondria
5. Xanthine oxidase present in milk, small
   intestine, kidney and liver has Mo as its
   activator ion converts urine bases to uric
   acid
6. Glucose oxidase prepared from fungi
7. Glycine oxidase which oxidatively
   deaminates glycine to glyoxylic acid and
   ammonia
NIACIN
  NAD+ and NADH are coenzymes of niacin:
A- NAD+ containing dehydrogenases are:
1. Isocitrate dehydrogenase of mitochondrial
   origin.
2. Alcohol dehydrogenase
3. Lactate dehydrogenase
4. Malate dehydrogenase of citric acid cycle.
   Malate               Oxaloacetate
5. Glyceraldehyde-3-P dehyrogenase of
   glycolysis
6. Pyrurate dehydrogenase complex
7. α-ketoglutarate dehydrogenase of citric
   acid cycle.
8. β-hydroxy fatty acyl-coA dehydrogenase of
   β-oxidation of fatty acids
B- NADP+ containing dehydrogenases are:
1. Isocitrate dehydrogenase of extra
   mitochondrial origin.
2. Glucose-6-phosphate dehydrogenase of
   HMP-shunt
3. β-ketoacyl reductase in the fatty acid
   synthesis
4. HMG-CoA reductase in cholesterol
   synthesis
     HMG-CoA → Mevalonate
5. Enoyl reductase of fatty acid synthase
   complex
BIOCHEMICAL ACTIONS:
          PANTO THENIC ACID
1. Formation of active acetate [Acetyl-CoA]:
   CoA-SH
2. Formation of acetyl-ACP and malonyl-
   ACP
3. Role in oxidation of fatty acids, formation
   of fats and phospholipids:
4. Heme Synthesis: Ative succinate
   [succinyl-CoA] is product of oxidative
   decarboxylation of α-oxoglutarate in TCA
   cycle. Succinyl-CoA and glycine is needed
   for the synthesis of heme.
BIOCHEMICAL FUNTIONS OF
        PYRIDOXINE:
1. As co-transaminase: It acts as a
   coenzyme in transamination reactions.
   GOT [AST] and GPT [ALT] are
   transaminases which need PLP as
   coenzyme for their actions
2. As co-decarboxylase: It also functions as
   a coenzyme in non-oxidative
   decarboxylation of some aminoacids or
   their derivatives.
Tyrosine            Tyramine + CO2
Histidine           Histamine + CO2

3. As Ala-synthase: in the synthesis of δ-
   aminolevulinic acid which is an
   intermediate in heme synthesis
4. As coenzyme in the conversion of
   tryptophan to niacin.
5. Interconversion of glycine and serine by
   hydroxymethyl transferase.
6. In transulphuration reactions, where
    transfer of-SH group takes place, B 6 is
    needed.
7. In synthesis of sphingosine
8. Intramitochondrial fatty acid synthesis
9. Intestinal absorption of aminoacids
10. Transport of K+. B6 is reported to promote
    transport of K+ across the membrane.
11. Synthesis of CoA-SH from pantothenic
    acid needs B6. in B6 deficiency CoA level of
    the liver is decreased.
12. B6 acts as a coenzyme for glycine
    Synthase.
BIOCHEMICAL FUNCTIONS OF
          BIOTIN
Biotin is a prosthetic group of some
   enzymes catalyzing CO2 transfer or CO2
   fixation reactions.
1. Formation of malonyl-CoA from acety-
   CoA and CO2
2. Pyruvate carboxylase Reaction: Here
   pyruvate forms oxaloacetate.
3. Formation of carbamoyl-PO4: NH3, CO2
   and ATP requires biotin to form
   carbamyl-PO4 in presence of carbamyl-
   PO4 synthetase.
4. Formation of β-methylglutaconyl-CoA
   from β-methylcrotonyl-CoA. It is an
   intermediate reaction in leucine
   metabolism
5. Biotin influences other enzyme systems
   e.g. succinate dehydrogenase,
   decarboxylase and aminoacid
   deaminases. Here CO2 is used for the
   formation of aspartic acid, serine and
   threonine.
6. Propionyl-CoA carboxylase reaction
   requires biotin
                  ATP
Propionyl-CoA+CO2 →   Methylmalonyl-CoA
                 ADP+Pi
COENZYME FORMS OF FOLIC
           ACID:
1. Tetrahydrofolic acid, FH4:
2. Folinic acid:
3. Rhizopterin:
METABOLIC ROLE (ONE
     CARBON METABOLISM):
FH4 is the coenzyme form of folic acid and it
 acts as coenzyme in transfer and
 utilization of one carbon moiety [C1]
One Carbon Donor and Acceptor
 Compounds:
One carbon donor group       One carbon acceptor group

Formimino group of           N-formyl methionine of
formimino glu [from his].    transfer-RNA.
Methyl group of methionine. Glycine to form serine.

Methyl group of methionine. Glycine to form serine.

Methyl group of thymine.     Uracil to form thymine.


β-carbon of serine.          Ethanolamine to form choline.

Gly, trp, ALA and acetone,   Positions 2 and 8 of purin ring.
                             Histidine synthesis.
FOLATE ANTAGONISTS:
1.   SULFONAMIDES
2.   TRIMETHOPRIM:
3.   PYRIMETHAMINE:
4.   AMINOPTERIN AND AMETHOPTERIN:
BIOCHEMICAL FUNCTIONS OF
            B12
1. Methylmalonyl-CoA-isomerase: It
   catalyzes the reaction using B12 as a
   coenzyme
Methylmalonyl-CoA → succinyl-CoA
2. Methionine synthase or homocysteine
   methyl transferase requires B12 as
   coenzyme:
3. Conversion of Ribonucleotide to
   deoxyribonucleotide also needs B12. It is
   important in the synthesis of DNA hence
   deficiency of B12 leads to the defective
   synthesis of DNA.
4. Role as Hemopoietic Factor: Like folic acid,
   vitamin B12 is also concerned with
   hemopoiesis and is needed for maturation
   of RBCs.
5. Abnormal Homocysteine Level: In
   vitamin B12 deficiency, Homocysteine
   Conversion to methionine a block so that
   homocysteine is accumulated, leading to
   homocystienuria. Homocysteine level in
   blood is related with myocardial
   infarction. So1, B12 is protective against
   cardiac disease.
Demyelination and Neurological Deficits: In
 B12 deficiency, methylation of
 phosphatidyl ethanolamine to phosphatidyl
 choline is not adequate. This leads to
 deficient formation

Of myelin sheaths of nerves, demyelination
 and neurological lesions.
CAUSES OF B12 DEFICIENCY:
1. Nutritional B12 deficiency.
2. Decrease in absorption due to non-
   availability of absorptive sufface caused
   by gastrectomy, resection of ileum, blind
   loop syndrome.
3. Elderly people are unable to absorb B 12
4. Addisonian anemia is pernicious [fatal]
   without any remedy. It is manifested in
   persons 40 years of age. It is an
   autoimmune disease and antibodies are
   formed against IF. The deficiency of IF
   leads to defective absorption of B12.
5. Atrophy of gastric epithelium: It leads to
   decreased IF and decreased absorption
   of B12.
6. Drugs: Some drugs interfere with
   absorption of B12. These are phenphormin,
   cholchicine, neomycine, ethanol and KCl.
7. Increased requirement of B12 in pregnancy
   is common cause for vitamin B12
   deficiency.
BIOCHEMICAL FUNCTIONS OF
      ASCORBIC ACID:
1. Vitamin C acts as a reducing agent:
2. The oxidation of p-hydroxphenyl
   pyruvate to homogentisate in the
   metabolism of tyrosine needs the
   presence of vitamin V and Cu+2
3. Role in iron absorption: Ascorbic acid
   present in food reduces the inorganic Fe +
   ++
      (ic) to Fe++ (ous) form.
4. Vitamin-C acts as a coenzyme for
   hydroxylases. Hydroxylation reactions
   are involved in the synthesis of collagen
   and other compounds:
5. Formation of carnitine in liver by
   hydroxylation of γ-butyrobetaine involves
   vitamin-C, α-ketoglutarate, Fe++ and a
   dioxygenase.
6. Vitamin-C required for the normal
   function of adrenal cortex.
7. The formation of FH4 from folate needs
   vitamin-C. Tetrahydrofolate [FH4] is a
   coenzyme from of folate.
8. Ascorbic acid is necessary for the
   formation of tissue ferritin.
9. Vitamin C is needed for the functional
   activity of fibroblast, osteoblast, and
   consequently for the synthesis of MPS of
   connective tissues, osteoid tissues,
   dentine tissues and intracellular
   substance involved in the cementing of
   capillaries.

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Biological role of vitamin MUHAMMAD MUSTANSAR

  • 1.
  • 2. BIOLOGICAL ROLE OF VITAMIN-A 1. Retinol and retinoic acid have role in normal reproduction 2. Retinal has a role in visual cycle 3. Retinoic acid has a role in glycoprotein synthesis 4. Roll in MPS synthesis 5. Vitamin-A is needed for mitochondrial membrane function
  • 3. 6. Anti cancer role: β-carotene is an antioxidant and trap peroxy free radicals in tissues at low partial pressure of O 2 7. Role in reproduction 8. Bone and teeth formation is slow
  • 4. BIOCHEMICAL ACTIONS OF CHOLECALCIFEROL 1. Vitamin-D promotes absorption of Ca ++ and P by the intestine. It stimulates the synthesis of a specific Ca++ binding protein by intestinal epithelium. 2. Vitamin-D induces the synthesis of specific Ca++ binding protein in bones 3. Vitamin-D regulates the Ca++ level by reabsorbing Ca++ through the kidney
  • 5. 4. Vitamin-D promotes mineralization of bones through deposition of Ca++ and P in growing bones. 5. Vitamin-D increases the reabsorption of PO4 through renal tubules. 6. Vitamin-D acts as coenzyme for alkaline phosphatase 7. Vitamin-D is responsible for enameling of the teeth. Its deficiency leads to irregular and rough teeth
  • 6. 8. Vitamin-D promotes growth in general and is essential for normal health. BMR is decreased in vitamin-D deficiency. The deficiency of vitamin-D leads to the repeated attacks of respiratory diseases.
  • 7. BIOCHEMICAL ACTIONS OF VITAMIN-E 1. Antioxidant role: Vitamin-E is the most potent natural antioxidant. 2. Removal of Free radicals: Vitamin-E removes free radicals, prevents their peroxidative effects on unsaturated lipids of membrane and thus maintains integrity of membranes.
  • 8. 3. Protective role: i. Vitamin-E prevents massive hepatic necrosis produced on diet deficient in sulphur containing aminoacids. 4. Role in reproduction: It is required for normal reproduction, muscle integrity and for resistance of erythrocytes to hemolysis. 5. Role in Heme Synthesis: Vitamin-E also takes part in the synthesis of heme. Vitamin-E induces enzymes ALA-synthase and ALA-dehydratase.
  • 9. 6. A derivative of vitamin-E is said to be necessary for the synthesis of CoQ which is the component of mitochondrial electron transport chain.
  • 10. BIOLOGICAL ACTIONS OF VITAMIN-K 1. Vitamin-K is needed for formation of proconvertin: It is needed for the formation of prothrombin. Deficiency of vitamin K decreases proconvertin level in blood. 2. Vitamin-K modifies prothrombin: Vitamin-K is a coenzyme in modification of prothrombin to thrombin.
  • 11. 3. Vitamin-K modifies other clotting factors also: Vitamin K is needed for maintenance of normal levels of blood clotting factors II, VII, IX and X. All these factors are synthesized in the liver in their zymogen forms. Their conversion to biologically active forms depends upon vitamin K. The activation involves carboxylation of glutamyl residues in the molecules of these factors (including prothrombin also) to form dicarboxylic glutamyl residue.
  • 12. 4. Vitamin-K is needed for carboxylation of glutamyl residue of Ca++ binding transport between the flavin coenzyme and the cytochrome system.
  • 13. FACTORS CAUSING VITAMIN-K DEFICIENCY: • Surgical removal of intestine: • Liquid paraffin: • Antibiotic therapy for a long time: • Vitamin-K antagonists: Heparin and warfarin
  • 14. BIOCHEMICAL FUNCTIONS: THIAMINE • TPP [cocaroxylase] being an essential part of the decarboxylating dehydrogenases acts as a cofactor in many important reactions in carbohydrate metabolism i.e., dehydrogenase [PDH] complex and α-ketoglutarate dehydrogenase [αKGDH] complex i. Oxidative Decarboxylation of α-ketoacids
  • 15. ii. Conversion of α-Ketoglutarate to succinyl- SCoA iii. TPP acts as coenzyme in reactions catalyzed by transketolase iv. Tryptophan metabolism: Tryptophan pyrrolase Tryptophan N-formylkynurenine O2
  • 16. v. TPP is a coenzyme for mitochondrial branched chain α-ketoacid dehydrogenases [decarboxylases] which oxidatively decarboxylate α-ketoacids formed in the catabolsim of valine, leucine and isoleucline. vi. In the nervous system: TPP is a cofactor for the synthesis of acetylcholine. vii. TPP also acts as a coenzyme [co- carboxylase] for pyruvate carboxylase in yeast for non-oxidative decaroxylation of pyruvate to acetaldehyde.
  • 17. BIOCHEMICAL FUNCTIONS OF RIBOFLAVIN: A- Biochemical role of FMN as a coenzyme 1. FMN as a part of redox potential 2. FMN is a coenzyme for L-amino acid oxidases: 3. FMN being a part of Cut. C reductase 4. FMN also accepts 2H+ from NADH+H+ 5. FMN is a coenzyme for Warburg’s yellow enzyme [a component of respiratory chain]
  • 18. B- FAD is a coenzyme for the following enzyme: Like FMN, FAD is also is a part of mitochondrial respiratory chain 1. D-aminoacid oxidases: The enzymes catalyze reaction similar to L-aminoacid oxidases but with FAD as coenzyme. 2. Aldehyde oxidase 3. Acyl-CoA dehydrogenase of the β oxidation of fatty acids
  • 19. 4. Succinate dehydrogenase, an enzyme of citric acids cycle and converts succinate to fumarate in mitochondria 5. Xanthine oxidase present in milk, small intestine, kidney and liver has Mo as its activator ion converts urine bases to uric acid 6. Glucose oxidase prepared from fungi 7. Glycine oxidase which oxidatively deaminates glycine to glyoxylic acid and ammonia
  • 20. NIACIN NAD+ and NADH are coenzymes of niacin: A- NAD+ containing dehydrogenases are: 1. Isocitrate dehydrogenase of mitochondrial origin. 2. Alcohol dehydrogenase 3. Lactate dehydrogenase 4. Malate dehydrogenase of citric acid cycle. Malate Oxaloacetate
  • 21. 5. Glyceraldehyde-3-P dehyrogenase of glycolysis 6. Pyrurate dehydrogenase complex 7. α-ketoglutarate dehydrogenase of citric acid cycle. 8. β-hydroxy fatty acyl-coA dehydrogenase of β-oxidation of fatty acids
  • 22. B- NADP+ containing dehydrogenases are: 1. Isocitrate dehydrogenase of extra mitochondrial origin. 2. Glucose-6-phosphate dehydrogenase of HMP-shunt 3. β-ketoacyl reductase in the fatty acid synthesis 4. HMG-CoA reductase in cholesterol synthesis HMG-CoA → Mevalonate
  • 23. 5. Enoyl reductase of fatty acid synthase complex
  • 24. BIOCHEMICAL ACTIONS: PANTO THENIC ACID 1. Formation of active acetate [Acetyl-CoA]: CoA-SH 2. Formation of acetyl-ACP and malonyl- ACP 3. Role in oxidation of fatty acids, formation of fats and phospholipids:
  • 25. 4. Heme Synthesis: Ative succinate [succinyl-CoA] is product of oxidative decarboxylation of α-oxoglutarate in TCA cycle. Succinyl-CoA and glycine is needed for the synthesis of heme.
  • 26. BIOCHEMICAL FUNTIONS OF PYRIDOXINE: 1. As co-transaminase: It acts as a coenzyme in transamination reactions. GOT [AST] and GPT [ALT] are transaminases which need PLP as coenzyme for their actions 2. As co-decarboxylase: It also functions as a coenzyme in non-oxidative decarboxylation of some aminoacids or their derivatives.
  • 27. Tyrosine Tyramine + CO2 Histidine Histamine + CO2 3. As Ala-synthase: in the synthesis of δ- aminolevulinic acid which is an intermediate in heme synthesis 4. As coenzyme in the conversion of tryptophan to niacin. 5. Interconversion of glycine and serine by hydroxymethyl transferase.
  • 28. 6. In transulphuration reactions, where transfer of-SH group takes place, B 6 is needed. 7. In synthesis of sphingosine 8. Intramitochondrial fatty acid synthesis 9. Intestinal absorption of aminoacids 10. Transport of K+. B6 is reported to promote transport of K+ across the membrane.
  • 29. 11. Synthesis of CoA-SH from pantothenic acid needs B6. in B6 deficiency CoA level of the liver is decreased. 12. B6 acts as a coenzyme for glycine Synthase.
  • 30. BIOCHEMICAL FUNCTIONS OF BIOTIN Biotin is a prosthetic group of some enzymes catalyzing CO2 transfer or CO2 fixation reactions. 1. Formation of malonyl-CoA from acety- CoA and CO2 2. Pyruvate carboxylase Reaction: Here pyruvate forms oxaloacetate.
  • 31. 3. Formation of carbamoyl-PO4: NH3, CO2 and ATP requires biotin to form carbamyl-PO4 in presence of carbamyl- PO4 synthetase. 4. Formation of β-methylglutaconyl-CoA from β-methylcrotonyl-CoA. It is an intermediate reaction in leucine metabolism
  • 32. 5. Biotin influences other enzyme systems e.g. succinate dehydrogenase, decarboxylase and aminoacid deaminases. Here CO2 is used for the formation of aspartic acid, serine and threonine. 6. Propionyl-CoA carboxylase reaction requires biotin ATP Propionyl-CoA+CO2 → Methylmalonyl-CoA ADP+Pi
  • 33. COENZYME FORMS OF FOLIC ACID: 1. Tetrahydrofolic acid, FH4: 2. Folinic acid: 3. Rhizopterin:
  • 34. METABOLIC ROLE (ONE CARBON METABOLISM): FH4 is the coenzyme form of folic acid and it acts as coenzyme in transfer and utilization of one carbon moiety [C1] One Carbon Donor and Acceptor Compounds:
  • 35. One carbon donor group One carbon acceptor group Formimino group of N-formyl methionine of formimino glu [from his]. transfer-RNA. Methyl group of methionine. Glycine to form serine. Methyl group of methionine. Glycine to form serine. Methyl group of thymine. Uracil to form thymine. β-carbon of serine. Ethanolamine to form choline. Gly, trp, ALA and acetone, Positions 2 and 8 of purin ring. Histidine synthesis.
  • 36. FOLATE ANTAGONISTS: 1. SULFONAMIDES 2. TRIMETHOPRIM: 3. PYRIMETHAMINE: 4. AMINOPTERIN AND AMETHOPTERIN:
  • 37. BIOCHEMICAL FUNCTIONS OF B12 1. Methylmalonyl-CoA-isomerase: It catalyzes the reaction using B12 as a coenzyme Methylmalonyl-CoA → succinyl-CoA 2. Methionine synthase or homocysteine methyl transferase requires B12 as coenzyme:
  • 38. 3. Conversion of Ribonucleotide to deoxyribonucleotide also needs B12. It is important in the synthesis of DNA hence deficiency of B12 leads to the defective synthesis of DNA. 4. Role as Hemopoietic Factor: Like folic acid, vitamin B12 is also concerned with hemopoiesis and is needed for maturation of RBCs.
  • 39. 5. Abnormal Homocysteine Level: In vitamin B12 deficiency, Homocysteine Conversion to methionine a block so that homocysteine is accumulated, leading to homocystienuria. Homocysteine level in blood is related with myocardial infarction. So1, B12 is protective against cardiac disease.
  • 40. Demyelination and Neurological Deficits: In B12 deficiency, methylation of phosphatidyl ethanolamine to phosphatidyl choline is not adequate. This leads to deficient formation Of myelin sheaths of nerves, demyelination and neurological lesions.
  • 41. CAUSES OF B12 DEFICIENCY: 1. Nutritional B12 deficiency. 2. Decrease in absorption due to non- availability of absorptive sufface caused by gastrectomy, resection of ileum, blind loop syndrome. 3. Elderly people are unable to absorb B 12
  • 42. 4. Addisonian anemia is pernicious [fatal] without any remedy. It is manifested in persons 40 years of age. It is an autoimmune disease and antibodies are formed against IF. The deficiency of IF leads to defective absorption of B12. 5. Atrophy of gastric epithelium: It leads to decreased IF and decreased absorption of B12.
  • 43. 6. Drugs: Some drugs interfere with absorption of B12. These are phenphormin, cholchicine, neomycine, ethanol and KCl. 7. Increased requirement of B12 in pregnancy is common cause for vitamin B12 deficiency.
  • 44. BIOCHEMICAL FUNCTIONS OF ASCORBIC ACID: 1. Vitamin C acts as a reducing agent: 2. The oxidation of p-hydroxphenyl pyruvate to homogentisate in the metabolism of tyrosine needs the presence of vitamin V and Cu+2 3. Role in iron absorption: Ascorbic acid present in food reduces the inorganic Fe + ++ (ic) to Fe++ (ous) form.
  • 45. 4. Vitamin-C acts as a coenzyme for hydroxylases. Hydroxylation reactions are involved in the synthesis of collagen and other compounds: 5. Formation of carnitine in liver by hydroxylation of γ-butyrobetaine involves vitamin-C, α-ketoglutarate, Fe++ and a dioxygenase. 6. Vitamin-C required for the normal function of adrenal cortex.
  • 46. 7. The formation of FH4 from folate needs vitamin-C. Tetrahydrofolate [FH4] is a coenzyme from of folate. 8. Ascorbic acid is necessary for the formation of tissue ferritin. 9. Vitamin C is needed for the functional activity of fibroblast, osteoblast, and consequently for the synthesis of MPS of connective tissues, osteoid tissues, dentine tissues and intracellular substance involved in the cementing of capillaries.