Enzymes Complete Notes PDF

Vandana Janghel, Assistant Professor, SVITS, Bilaspur, (C.G.) ENZYMES Definition: Enzymes are biological Catalysts synthesized by living cell which increase the rate of metabolic reactions. Almost all biological reactions involve Enzymes....

Vandana Janghel, Assistant Professor, SVITS, Bilaspur, (C.G.) ENZYMES Definition: Enzymes are biological Catalysts synthesized by living cell which increase the rate of metabolic reactions. Almost all biological reactions involve Enzymes. Some examples of Enzymes are: Lactase: Breaks down Lactose into Glucose and Galactose. Catalase: Breaks Hydrogen Peroxide down into Water and Oxygen. Hexokinase: Glycolysis “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" Properties of Enzymes facebook group and then go to file section 1. All enzymes are Globular Proteins with a specific Tertiary Shape 2. They are high molecular weight compounds( ranging from 10,000 to 2,000,000) made up principally of chains of amino acids linked together by peptide bonds. 3. Specific in nature. They are usually specific to only one reaction. 4. Colloidal and thermo-labile in character. 5. The part of the Enzyme that acts a Catalyst is called the Active Site. 6. The Active Site of an Enzyme is Complementary to the Substrate it catalyses. 7. When a reaction involving an Enzyme occurs, a Substrate is turned into a Product. 8. Enzymes can be denatured and precipitated with salts, solvents and other reagents. 9. This entire active complex (functional unit) is referred to as the holoenzyme which is made up of apoenzyme (protein portion) plus the cofactor (coenzyme, prosthetic group or metal-ion activator). Holoenzyme = Apoenzyme + Cofactor (Active enzyme) (Protein part) (Non-Protein part) “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section  Vandana Janghel, Assistant Professor, SVITS, Bilaspur, (C.G.) Classification of Enzymes The International Union of Biochemistry (I.U.B.) according to these Enzymes is classified into six classes, according to the reaction they catalyzed Sr.No. Class Reaction Catalyzed Example 1 Oxido- Oxidation Reduction Oxidases, Reductae, Dehydrogenases Reductases (Transfer of electrons) AH2 + B A + BH2 2 Transferases Transfer of functional groups Phosphorylases, Transaminase, A-X + B A + B-X Hexokinase, Transmethylases 3 Hydrolases Hydrolysis Amylases, Lipases, Fumarase, Enolase, A-B + H2O AH + BOH 4 Lyases Addition Elimination Aldolase, Fumarase, Citrate Synthase, Addition of groups or removal of Decarboxylase groups (water, ammonia, co2) A-B + X-Y AX-BY 5 Isomerases Interconversion of isomer Mutase, Epimerase, A A’ 6 Ligases Condensation Reactions require DNA Ligase, Glutamine synthetase ATP A+ B A-B ATP ADP + Pi Table 1: Classification of Enzyme “Solution-Pharmacy” believes in SHARING, not in selling Enzyme kinetics Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" Michaelis-Menten Plot facebook group and then go to file section The enzyme (E) and substrate (S) combine with each other to form unstable Enzyme substrate complex (ES) for the formation of product. K1 K3 S+ E ES P+E K2 K1, K2, K3 represent the velocity constant (rate constant) for the respective reaction. When the maximum velocity has been reached, the entire available enzyme has been converted to ES, the enzyme substrate complex. This point on the graph is designated as Vmax. “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section  Vandana Janghel, Assistant Professor, SVITS, Bilaspur, (C.G.) Km or Michaelis-Menten constant is defined as the substrate concentration to produce half maximum velocity in an enzyme catalyzed reaction. Formula: Km = K2+ K3 K1 “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section Fig: Effect of Substrate Concentration on Enzyme Velocity The following equation is obtained after suitable algebraic manipulation. V = Vmax [S] ………… (1) Km+[S] “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra V = Measured velocity at any time You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section S = Substrate concentration at this time Vmax = Maximum velocity Km = Michaelis- Menten constant Km, (or Brig’s and Haldane’s Constant) Let us assume that the measured velocity (V) is equal to 1/2 Vmax. Equation 1 substituted as follows 1Vmax = Vmax [S] 2 Km+[S] Km + [S] = 2 Vmax [S] Vmax Km + [S] = 2[S] Km = [S] “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section  Vandana Janghel, Assistant Professor, SVITS, Bilaspur, (C.G.) 1. Low km indicates a strong affinity between enzyme and substrate. 2. High Km value reflects a weak affinity between them. 3. Km not dependent on the concentration of enzyme. Lineweaver–Burk double Reciprocal Plot The Lineweaver–Burk double reciprocal plot is a graphical representation of the Lineweaver– Burk equation of enzyme kinetics used to determine important terms in enzyme kinetics, such as Km and Vmax, Taking the reciprocal gives Fig: Lineweaver–Burk Double Reciprocal Plot V- Reaction velocity Km - Michaelis–Menten constant Vmax - Maximum reaction velocity [S] - Substrate concentration. The y-intercept of a graph is equivalent to the inverse of Vmax; the x-intercept of the graph represents −1/Km. It is also useful in understanding the effect of various enzyme inhibitions. “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section  Vandana Janghel, Assistant Professor, SVITS, Bilaspur, (C.G.) Enzyme Regulation Enzyme regulation is the process by which cells can turn off or turn on the activities of various metabolic pathways by regulating enzyme activity. Different types of enzyme regulation methods are: 1. Allosteric regulation 2. Compartmentation 3. Control of enzyme synthesis “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" 4. Active and inactive enzyme facebook group and then go to file section 5. Enzyme degradation 1. Allosteric regulation Some of the enzymes have additional site other than active site. This additional site is known as allosteric site. Such enzymes are known allosteric enzyme. Certain substance (allosteric modulator) binds at the allosteric site and regulates the enzyme activity.  When positive allosteric effector (Activator) binds at the allosteric site than the enzyme activity is increased.  When negative allosteric effector (inhibitor) binds at the allosteric site than the enzyme activity is inhibited.  Confirmational change in allosteric enzyme leading to inhibition or activation. Figure 1: Allosteric enzyme activity Allosteric Activator- Isocitrate Example  AcetylCoA carboxylase in fatty acid sysnthesis Allosteric Inhibitor- Palmitate “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section  Vandana Janghel, Assistant Professor, SVITS, Bilaspur, (C.G.)  Hexokinase in glycolysis its allosteric inhibitor is Glucose-6-Phospahte Allosteric Inhibitor- ATP  Phosphofructokinase in glycolysis Allosteric Activator- AMP, ADP Feedback regulation The process of inhibiting the first step by the final product is referred as feedback regulation. Feedback inhibition or end product inhibition is a specialized type of allosteric inhibition necessary to control metabolic pathways. 2. Control of enzyme synthesis Many rate limiting enzyme have short half life present in very low concentration. Constitutive enzyme- house keeping fairly constant live Adaptive enzyme- Concentration increases or decreases as per body needs and are well regulated. Induction and repression which ultimately determine the gene level through the mediation of hormones or other substance “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" Induction facebook group and then go to file section Induction means increase in the synthesis of enzyme. Example:  Insulin induces synthesis of glycogen synthetase, glucokinase, Phosphofructokinase, Protein kinase. These entire enzymes involve in the utilization of glucose.  Hormone cortisol induces synthesis of pyruvate carboxylase, tryptophan oxygenase. Repression Repression means decreases in the synthesis of enzyme. In many case substrate can repress the synthesis of enzyme. Example: Repression of pyruvate carboxylase by glucose: Pyruvate carboxylase is the key enzyme for glucose synthesis from non carbohydrate source like pyruvate and aminoacids. If there is sufficient glucose is available, there is no necessities for its synthesis. “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section  Vandana Janghel, Assistant Professor, SVITS, Bilaspur, (C.G.) Enzyme Inhibitors Definition: Enzyme inhibitor is defined as the substance which bind with the enzyme and slows down or stops the normal catalytic function of an enzyme Three Threetypes Typesofofenzyme Enzymeinhibition Inhibition Reversible inhibition Irreversible inhibition Allosteric inhibit ion Competitive inhibition Non-competitive inhibition Uncompetitive inhibition 1. Reversible inhibition The enzyme inhibition can be reversed if the inhibitor is removed. The inhibitor binds none covalently with the enzyme. i. Reversible Competitive Inhibition The inhibitor competes with the substrate and binds at the active site of the enzyme but do not undergo any catalysis because inhibitors have structure resemblance with substrate. “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" Example facebook group and then go to file section 1. Malonic acid, glutaric acid and oxalic acid have structural similarities with succinic acid Competitively inhibit succinic acid for the binding at the active site of succinate dehydrogenase CH2COOH CH2COOH CH2COOH CH2 Succinic acid CH2COOH Malonic acid E+S ES E+P +I EI  Enzyme- HMGCoA reductase Substrate - HMGCoA Inhibitor-Lovastatin, Provastatin  Ethanol is given in methanol poisoning. Competitively inhibit method for binding to active site of aldehyde dehydrogenase “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section  Vandana Janghel, Assistant Professor, SVITS, Bilaspur, (C.G.) “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section Enzyme Substrate Enzyme + Substrate Complex Enzyme Inhibitor Enzyme Inhibitor similar to substrate Substrate Replace the substrate Enzyme Inhibitor fit in the place of substrate and thus reaction become slowly Inhibitor Enzyme + Inhibitor Complex Inhibitor takes substrate place and bind itself Fig: Competitive Inhibition ii. Reversible non-competitive inhibitor: Inhibitor binds at a site other than the active site of the enzyme, change the shape of the enzyme and thus the active site, Substrate cannot fit into active site thus decreasing enzyme activity. The inhibitor has no structural resemblance with the substrate Example Heavy metals ions (Pb2+ & Hg2+) non competitively inhibit the enzyme by binding to –SH of Cysteine, away from active site. iii. Reversible un-competitive inhibitor: Inhibitor binds to the ES complex and not to the free enzyme Example “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra Placental alkaline phosphate by phenylalanine You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section 2. Irreversible inhibitor An irreversible inhibitor inactivates an enzyme by binding to its active site by a strong covalent bond.  Permanently deactivates the enzyme  Irreversible inhibitors do not resemble substrates  This process cannot be reversed  These inhibitors are usually toxic substance  Vandana Janghel, Assistant Professor, SVITS, Bilaspur, (C.G.) Examples  Organophosphate insecticides (melathion) inhibit acetylcholine esterase (nerve conduction) paralysis of vital body function.  Fluoride inhibits enolase and glycolysis.  Iodoacetate is an irreversible inhibitor of the enzyme papain and glyceraldehydes 3 phospahte dehydrogenase.  Cyanide inhibits cytochrome oxidase (bind to Fe atom) of Electron transport chain.  Penicillin inhibits serine containing enzyme in bacteria thus inhibit cell wall synthesis. Non Competitive Inhibitor “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section Enzyme Substrate Enzyme + Substrate Complex Enzyme Inhibitor Enzyme Inhibitor Changes the structure of enzyme No fit No reaction Enzyme + Inhibitor Complex Inhibitor Enzyme Substrate Inhibitor attached to the Enzyme Fig: Non competitive Inhibition 3. Allosteric inhibitor Some of the enzymes have additional site other than active site. This additional site is known as allosteric site. Such enzyme known allosteric enzyme. Positive allosteric effector (Activator) increase the enzyme activity and negative allosteric effector (inhibitor) inhibite enzyme activity Example Allosteric Activator- Isocitrate AcetylCoA carboxylase in fatty acid sysnthesis Allosteric Inhibitor- Palmitate “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section  Vandana Janghel, Assistant Professor, SVITS, Bilaspur, (C.G.) Allosteric Activator- AMP, ADP Phosphofructokinase in glycolysis Allosteric Inhibitor- ATP Hexokinase in glycolysis its allosteric inhibitor is Glucose-6-Phospahte “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section  Vandana Janghel, Assistant Professor, SVITS, Bilaspur, (C.G.) Application of Enzymes Therapeutic application 1. Enzymes act as anti-clotting agents (Clearing blood clot) (Myocardial Infarction - heart attack) Examples: Urokinase and Streptokinase Enzyme Therapeutic Use Asparaginase Leukaemia Collagenase Skin ulcers Glutaminase Leukaemia Hyaluronidase Heart attack Lysozyme Antibiotic Rhodanase Cyanide poisoning Ribonuclease Antiviral Lactamase Penicillin allergy Streptokinase Blood clots Trypsin Inflammation Uricase Gout Urokinase Blood clots Table 1: Therapeutic application of enzyme 2. Recombinant enzyme Example: (Lysosomal storage disaese)- Fabry (alpha galactosidase), Pompe disease (Alpha glucosidase). 3. Enzymes can be used for Aiding Digestion. Example: Amylases, Proteases and Lipase. 4. They can also be used as Deworming agents. Example: Papain. Diagnostic application 1. Glucose oxidase with peroxidase: To detect the level of glucose. 2. Amylase: The activity of serum amylase is increased in acute pancreatitis. 3. ALT (Alanine transaminase)/SGPT (serum glutamate pyruvate transaminase): is elevated in acute hepatitis of viral or toxic origin jaundice and cirrhosis of liver. Vandana Janghel, Asst. Professor, SVITS, BSP, (C.G.)  Vandana Janghel, Assistant Professor, SVITS, Bilaspur, (C.G.) 4. AST (Aspartate transaminase)/SGOT (serum glutamate oxaloacetate transaminase): activity in serum is increased in myocardial infarction (heart attack) and also in liver disease. 5. Lactate dehydrogenase (LDH): Increased levels in the blood indicate myocardial infarction (MI). 6. Alakline phosphate: Elevated in bone (rickets, carcinoma of bone) and liver disease (obstructive jaundice) 7. Acid phosphatase: It is increased in cancer of prostate gland Sr. No Enzymes Disease in which Increased 1 SGPT, SGOT Liver disease 2 SGOT Heart attacks (MI) 3 Creatine phosphokinase Myocardial Infarction 4 Acid phosphatase Prostate gland 5 Alakline phosphate Rickets, carcinoma of bone) and liver disease (obstructive jaundice) 6 Lactate dehydrogenase (LDH) Myocardial infarction (MI). 7 Glucose oxidase with peroxidase Level of glucose 8 Amylase Acute pancreatitis Table 2: Diagnostic Application of Enzyme “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" Isoenzymes facebook group and then go to file section Definition: Multiple forms of an enzyme catalyzing the same reaction in different tissues in the body are isoenzymes. They differ in their physical and chemical properties Diagnostic application of Isoenzyme 1. Lactate dehydrogenase (LDH):  LDH consists of 5 isoenzymes (LDH1, LDH2, LDH3, LDH4, and LDH5). LDH Converts lactate to pyruvate “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" Lactate dehydrogenase facebook group and then go to file section Lactate Pyruvate Vandana Janghel, Asst. Professor, SVITS, BSP, (C.G.)  Vandana Janghel, Assistant Professor, SVITS, Bilaspur, (C.G.)  LDH1 isoenzyme is more prevalent in heart muscle and LDH5 found in skeletal muscle & liver.  LDH1 is much greater than LDH2 in serum indicates heart muscle damage.  LDH5 increased activity in serum is an indicator of liver disease. 2. Creatine phosphokinase exist as 3 isoenzymes (CPK1, CPK2, CPK3) CPK Phosphocreatine Creatine  Each isoenzyme is a dimer composed of two subunit M (Muscle) and B (brain) or both.  CPK2 (MB) is the earliest indication of myocardial infarction (within 6-18) “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" 3. Isoenzyme of alkaline phosphate (ALP) facebook group and then go to file section  ALP is a monomer, the isoenzyme are due to the difference in the carbohydrate content α1-ALP, α2- heat labile ALP, α1-heat stable ALP etc.  Increase in α2- heat labile ALP indicates hepatitis where as Pre-β-ALP indicates bone disease. “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section Vandana Janghel, Asst. Professor, SVITS, BSP, (C.G.)  Vandana Janghel, Assistant Professor, SVITS, Bilaspur, (C.G.) Coenzymes Coenzymes Definition: Coenzymes are the non protein organic low molecular weight molecules that are required by the certain enzyme to carry out catalysis (reaction). Coenzymes enhances the action of enzyme. The functional unit of enzyme is referred as holoenzyme which is made up of apoenzyme (protein portion) plus the cofactor (coenzyme, prosthetic group or metal-ion activator). Holoenzyme = Apoenzyme + Cofactor (Active enzyme) (Protein part) (Non-Protein part) Cofactors are inorganic substance that are required to increase the rate of catalysis (Enzyme activity) e.g. Ca2+, Mg2+, Mn2+ Sr.No. Vitamin Coenzymes Biochemical function Example 1 Thiamine (B1) Thiamine pyrophosphate (TPP) Aldehyde or keto group Transketolase in HMP tranfer shunt 2 Riboflavin (B2) Flavin mononucleotide (FMN) Redox reaction Succinate to fumarate Flavin adenine dinucleotide (FAD) (Hydrogen and electron require succinate transfer) dehydrogenase and Require for energy FAD in TCA cycle production Involve in carbohydrate, lipid, protein and purine metabolism beside Electron transport chain 3 Niacin, Nicotinamide adenine dinucleotide Redox reaction NADH- Lactate Niacinamide and Nicotinamide adenine (Hydrogen and electron dehydrogenase (B3) dinucleotide phosphate (NAD and transfer) NADPH- Glucose 6 NADP) NADH is oxidized to phosphate generate ATP for dehydrogenase biosynthetic reaction 4 Pyridoxine (B6) Pyridoxal phosphate Transamination, Histidine to histamine deamination, require PLP decarboxylation 5 Cobalamine Coenzyme B12 Isomerization Methylmalonyl-CoA to (B12) (Methyl cobalamine) succinyl-CoA Vandana Janghel, Asst. Professor, SVITS, BSP, (C.G.)  Vandana Janghel, Assistant Professor, SVITS, Bilaspur, (C.G.) 6 Folic Acid Tetrahydrofolate (THF) 1 carbon transfer (accept Homocycteine to or donate) methionine Synthesis of purine and Require homocysteine pyrimidine methyl tranferase and THF 7 Biotin (B7) Biocytin Carboxylation Pyruvate to Cell cycle regulation oxaloacetate Fatty acid synthesis 8 Pantothenic acid Coenzyme A (CoASH) Acyl transferase Fatty acid to acetyl (B5) CoA require CoASH and thiokinase 9 Lipoic acid Lipoate Oxidation Pyruvate dehydrogenase complex Other Coenzymes Sr.No Coenzyme Biochemical function 1 Adenosine triphosphate (ATP) Donate phosphate adenosine diphosphate and adenosine monophosphate 2 Cytidine diphosphate (CDP) Phospholipids synthesis Carrier of choline and ethanolamine 3 Uridine diphosphate (UDP) Carrier of monosaccharide (glucose and galactose for glycogen synthesis) “Solution-Pharmacy” believes in SHARING, not in selling Available on- YouTube-Facebook (Group and Page) & Instagram YouTube Link- https://www.youtube.com/c/SOLUTIONpushpendra You can download all of our uploaded study materials by joining our "Solution-Pharmacy" facebook group and then go to file section Vandana Janghel, Asst. Professor, SVITS, BSP, (C.G.)