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Enzymes in Medicine and Healthcare

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Properties of Enzymes (PPT)

Properties of Enzymes PPT | Characteristics of Enzymes PPT | Properties of Enzymes, Catalytic Property, Catalytic Power, Turnover Number of Enzymes, Enzymes with Highest Turnover number – Catalase, Enzyme with Lowest Turnover Number- Lysozyme, Specificity of Enzymes, Optical Specificity, Group Specificity, Absolute Specificity, Geometrical Specificity, Reversibility of Enzymatic Reactions, Irreversible Enzymatic reactions, Sensitivity to Heat and Temperature, Thermolabile Enzymes, Thermo-stable Enzymes, Optimum Temperature, Optimum pH of Enzymes.

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Apr 01, 2019

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ENZYMES. Biological catalysts which speed up the rate of reaction without becoming part of the reaction but themselves cannot initiate any chemical reaction Enzymes : First name is of substrate second, ending in “ASE” indicating type of reaction catalyzed Clarify the reaction , e.g.

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• ascorbic acid
• single carbon carrier
• biotin pyruvate
• d enzyme co
• phosphate group

Presentation Transcript

ENZYMES • Biological catalysts which speed up the rate of reaction without becoming part of the reaction but themselves cannot initiate any chemical reaction • Enzymes : First name is of substrate second, ending in “ASE” indicating type of reaction catalyzed • Clarify the reaction , e.g. • L- Malate + NAD  Pyruvate + NADH-H + CO2 • Malate NAD oxidoreductase (Decarboxylating) • IUB Classification and Numbering • Six major classes and 4-13 subclasses • Numbering 1.2.3.4.5.6

ENZYMES Nomenclature • Oxidoreductases • Enzymes acting on CH-OH group • Alcohol NAD oxidoreductase [Alcohol dehydrogenase] • Alcohol + NAD= Aldehyde or Ketone + NADH.H • Glucose+ ATP =Glucose-6 phosphate + ADP • ATP.D.Hexose – 6 Phosphotransferase (Hexokinase)

CO-FACTORS OF ENZYMES

COENZYMES • Heat stable, low molecular weight organic compounds non-covalently linked with enzymes & can be separated. APO + CO = Holoenzyme • If covalently linked to apoenzymes = prosthetic group • Act as intermediate or ultimate acceptor in group transfer enzyme catalyzed reactions D-G + A A-G + D Enzyme Co-Enzyme D A Co-En-G

CO-ENZYMES REDUCTION OF NAD+ TO NADH.H+ Lactic acid + NAD Pyruvic acid + NADH-H+ Malic acid + NAD Oxalo acetic acid + NADH -H+ Glucose-6-phosphate + NADP 6-Phosphoglucon- olactone +NADPH-H+ REDUCTION OF FAD OR FMN TO FADH2 OR FMNH2 FMN is co enzyme for Cytochrome C oxidase, L.Amino acid dehydrogenase FAD is co-enzyme for xanthene oxidase, acyl-CoA dehydrogenase LDH Malic dehydrogenase G-6-P.D

CO-ENZYMES Thiamine Pyrophosphate: Co-enzyme for oxidative decarboxylation for ketoacids Pyruvate Acetyl CoA Pyruvate +TPP Acetalaldehyde -TPP complex+Co2 Alpha ketogluterate+6 CoA-SH Succinyl CoA + Co2 Ribose-5 Po4 + Xylulose-5-Po4 Sedoheptulose 7-Po4 + 3 phosphoglyceraldehyde CoA NAD NADH-H+ Pyruvate dehydrogenase Pyruvate decarboxylase -ketogluteratedehydrogenase NAD NADH-H+ Transketolase

CO-ENZYMES Biotin • Part of multiunit enzymes causing carboxylation reactions. Acts as carrier of CO2 Acetyl CoA+HCo3 + ATP Malonyl-CoA Pyruvate+ HCo3 + ATP Oxaloacetate+ ADP+Pi NH4 +HCo3 + 2ATP CarbamoylPO4 + 2 ADP+ 2 Pi Synthesis of Purines and Pyrimidines Acetylcarboxylase Enz-Biotin-COO- Enz-Biotin Pyruvate carboxylase .Biotin Carbamoyl Po4.Synthetase - Biotin

CO-ENZYMES Ascorbic acid (Vitamin C) • Strong reducing agent • Required for hydroxylation of proline into hydroxyproline for synthesis of collagen • Conversion of tyrosine into dopamine and into catecholamines (adrenaline and noradrenalin) • Bile acid formation • Conversion of cholesterol into 7-hydroxylcholesterol • Maintain metallic co-factors like Cu+ in Monooxygenases and Fe in dioxygenases in reduced form • Conversion of cholesterol into steroid hormone in adrenal cortex • Absorption of iron by reducing into reduced form which is can be easily absorbed • Acts as antioxidant in GIT by preventing formation of nitrosamines during digestion

CO-ENZYMES • Folic acid • Active form is tetrahydrofolate which acts as single carbon carrier for synthesis of various compounds like pyrimidines and purines e.g. conversion of dUMP (deoxyuridylate) into dTMP (deoxythymidylate) • Vitamin B12 • Acts as co-enzyme in groups rearrangements in isomerases e.g. conversion of methyl malonyl CoA into succinyl-CoA by enzyme methylmalonyl-CoA mutase • Converts homocystein into methionine • Act as maturation factor for RBCs

CLASSIFICATION OF ENZYMES • Formulated by the enzyme commission of I.U.B six major classes & 4-13 subclasses of each major class, based on the type of reactions catalyzed. • Oxidoreductases • Catalyzing oxidation reduction reactions • Transferases • Catalyzing group transfer • Hydrolases • Catalyzing hydrolytic breakdown

CLASSIFICATION OF ENZYMES 4. Lyases • Catalyzing removal of groups by mechanism other than hydrolysis and leaving behind double bonds or adding groups to already existing double bonds. 5. Isomerases • Catalyzing interconversion of isomers 6. Ligases • Catalyzing formation of bonds and new compounds 1.Oxidoreductases • Catalyzing oxidation reduction reaction where one substrate is oxidized and other is reduced

CLASSIFICATION OF ENZYMES(OXIDOREDUCTASES) Oxidases.Catalyzing oxidation of the substrate and atomic oxygen acts as recipient of hydrogen e.g. Ascorbic acid oxidase, Cytochrome oxidase, Tyrosinase ½ O2 H2 O Ascorbic acid Oxidase Ascorbic acid Dehydro ascorbic acid

CLASSIFICATION OF ENZYMES(OXIDOREDUCTASES) Aerobic Dehydrogenases. Catalyzing oxidation of the substrate and molecular oxygen acts as recipients of hydrogen e.g. Glucose oxidase, L amino acid dehydrogenase, Xanthene dehydrogenase O2 H2 O2 glucose Oxidase Glucose Gluconolactone

CLASSIFICATION OF ENZYMES(OXIDOREDUCTASES) Anaerobic Dehydrogenases. Catalyzing oxidation of the substrate and coenzymes act as recipients of hydrogen e.g. Lactate Dehydrogenase with NAD and Glucose 6 phosphate dehydrogenase with NADP Lactate dehydrogenase Lactic acid Pyruvic acid + NAD + NADH – H+

CLASSIFICATION OF ENZYMES(OXIDOREDUCTASES) Oxygenases . Catalyzing oxidation of the substrate and oxygen is added to the substrate eg are Homogentisate oxygenase, L Tryptophan dioxygenase Phenylalanine Hydroxylase Phenylalanine Tyrosine NADPH – H+ + O2 NADP + H2O

TRANSFERASES Transaminases. Catalyzing transfer of amino group between an amino acid and a ketoacid e.g. Aspartate Transaminase (AST), Alanine Transaminase (ALT) Aspartate Transaminase (AST) Glutamic acid +  Ketoglutaric acid + Oxalo acetic acid Aspartic acid Alanine Transaminase (ALT) Glutamic acid +  ketoglutaric acid + Pyruvic acid Alanine

TRANSFERASES Transmethylases. Catalyzing transfer of methyl group between to substrates e.g. COMT Catechol O Methyltransferase (COMT) Noradrenaline Adrenaline + CH3 Transpeptidases. Catalyzing transfer of amino acids to substrates e.g. Benzyl-SCoA transpeptidase Benzyl-SCoA Transpeptidase Benzyl - SCoA Hippuric acid + Glycine

TRANSFERASES Phosphotransferases. Catalyzing transfer of phosphate group to substrates e.g. Hexokinase, Glucokinase 2.7.1.1 ATP D hexose- 6 Phosphotransferase [Hexokinase] ATP + Glucose Hexokinase ADP + D-Glucose –6-P Acetyltransferase. Catalyzing transfer of acetyl group to substrates e.g. Choline Acetyltransferase Acetyl-CoA+ Choline  CoA + Acetyl- Choline

HYDROLASES • Catalyzing hydrolytic breakdown of different bonds. Most of the GIT enzymes belong to this class Enzymes hydrolyzing Carbohydrates Polysaccharidases Starch Amylase Maltose, Maltotrios, Dextrins Oligosaccharidases Dextrins Dextrinase Glucose Disacharidases Maltose, Lactose, Sucrose Disacharidases (Maltase, Lactase, Sucrase) Monosaccharides Enzymes Hydrolysing Lipids Triacyl glycerol Lipase Monoacyl glycerol + 2 F.F.A Cholesterol ester Cholesterol Free Cholesterol + FFA Esterase

HYDROLASES Phospholipids Phospholipase Lysophospholipids Lecithin Lysolecithin Enzymes Acting on Peptide Bonds Exopeptidases Carboxypeptidase Amino acids Aminopeptidase Endopeptidase e.g. Pepsin Smaller Peptides

HYDROLASES Tripeptidase : Tripeptide  A.A Dipeptidase: Dipeptide  AA Phosphatases i. Phosphomonoesterases: Glucose – 6.P. + H2O G 6. Phosphate Glucose +Pi Phosphatase ii. Phosphodiesterases: Removal of phosphate Group of diesters breakdown of 3’-5’ p linkages in cyclic AMP

LYASES • Catalyzing reactions in which groups are removed without hydrolysis leaving a double bond or add groups to already existing double bonds CH3. CO. COOH Pyruvate CH3. CHO+ CO2 (Acetaldehyde) (Pyruvate) Decarboxylase T.P.P COOH.CH = CH. COOH Fumerase COOH-CHOH. CH2-COOH (Malic Acid) (Fumaric acid)

ISOMERASES • Involved in inter conversion of pair of isomeric compounds • Glucose 6. P Phosphogluco glucose I.P Mutase • Glucose 6.P Phosphohexose Fructose 6.P Isomerase • All trans retinene Retinene 11- CIS retinene Isomerase • UDP glucose UDPG-4 UDP – Galactose Epimerase

LIGASES • Catalyze reactions in which linking together of two molecules occur coupled with the breakdown of a high energy phosphate bonds like ATP, GTP Acetate + CoA +ATP Acetyl CoA Acetyl CoA+AMP+PP Synthetase Succinate + CoA + ATP Succinyl CoA Succinyl CoA + ADP+ Pi Synthetase Pyruvate + CO2 + ATP Pyruvate Oxaloacetate + ADP + Pi Carboxylase Fatty acid + CoA + ATP Acyl CoA Acyl CoA (Activated fatty acid) + AMP + PiPi Synthetase

MECHANISM OF ACTION • S+E E-S P • D-G + A Enzyme (Enzyme – G) A-G + D ES • Factors affecting enzyme activity • Enzyme concentration • Substrate concentration • Temperature • pH • Enzyme inhibitors

MICHEALIS – MENTON EQUATION Vi = V max [S] Km + {S} Vi = Measured initial velocity V max = Maximum velocity S = Substrate Km = Michaelis constant Variations A. When (S) is much less than Km Vi = V max [S] OR V max [S] K [S] Km + {S} Km So Vi depends upon substrate concentration

ENZYME KINETICS • When substrate concentration is much greater than Km Vi = Vmax [S] or Vi = Vmax [S] Km + [S] [S] Or Vmax = Vi • When substrate concentration is equal to Km Vi = Vmax [S] or Vi = Vmax [S] Km + [S] [S] + [S] Or Vi = Vmax [S] or Vi = Vmax 2 [S] 2 So Vi = half of maximum velocity

Enzyme Catalysis • Catalysis by Proximity : Higher conc of “S” will increase their proximity to each other thereby promoting enhanced binding to enzyme resulting in increased catalysis • Acid-Base Catalysis : Ionizable functional gps of aminoacyl side chains & prosthetic gps can act as acids or bases. In “specific acid or base catalysis” rate of reaction is sensitive to changes in protons , but is independent of conc of other acids or bases present in the solution or at active site. In “general acid or base catalysis” reaction rates are sensitive to all acids & bases present .

Enzyme Catalysis • Catalysis by Strain : Binding of Enzyme to substrates whose covalent bond are to be cleaved in an unfavorable configuration thereby exerting strain on the bonds ,stretching or distorting bonds. • Covalent Catalysis: Formation of transient covalent bond between enzyme & substrate(s) makes it more reactant & introduces a new faster pathway of catalysis with much lowered energy of activation. On completion of reaction, enzyme returns to its original state. Cysteine, serine or histidine residues on enzyme participate in covalent catalysis

ENZYME INHIBITION • Competitive inhibition • Non competitive inhibition • Irreversible inhibition Competitive inhibition • Inhibitors resemble substrate, Km is increased no change in Vmax • Succinate Enz Fumarate • Malonate (structural analog of Succinate ) Enz – inhibition no product • Drug Allopurinol, structural analog of Xanthene is used for treatment of gout /hyperuricemia as it is a competitive inhibitor of enzyme Xanthene oxidase which normally converts Xanthene into Uric acid • Addition of excess of normal [S] will reverse this inhibition

ENZYME INHIBITION NON COMPETITIVE INHIBITION • Inhibitor binds on separate site on enzyme therefore no competition with substrate. Vmax is reduced and no change in Km • Inhibitor can bind with either free enzyme or enzyme – substrate complex and in both cases render these inactive • Lead poisoning is an example of this inhibition and it inhibits enzyme Ferrochelatase which adds iron molecule to the centre of porphyrin ring in the synthesis of Hemoglobin

IRREVERSIBLE INHIBITION Permanent covalent linkage with enzyme rendering it irreversibly inhibited • Diisopropyl phospho fluoride (DIPF) • Iodoacetamide • Heavy metal [Ag+ Hg+2], Silver, Mercury • Oxidizing agents • Covalent linkage with enzyme: inactivation of enzyme • Kinetics are same as of non competitive inhibition, therefore difficult to distinguish between the two • Examples are insecticides which act as enzyme poisons for the insects & disinfectants used for micro-organisms

REGULATION OF ENZYME ACTIVITY • 3 main mechanism in regulation A. Rate of synthesis and degradation determine enzyme quantity synthesis Amino acids Enzyme Degradation

REGULATION OF ENZYME ACTIVITY B. INDUCTION OF ENZYME SYNTHESIS In bacteria  glucose  no Beta galactosidase lactose  induction of B-galactosidase In animals  Enzymes of Urea Cycle  HMG CoA reductase in Cholesterol synthesis  Sucrase or invertase for Sucrose

REGULATION OF ENZYME ACTIVITY C. REPRESSION OF ENZYME SYNTHESIS • In bacteria  glucose  repression of B- Galactosidase • S typhimurium  Histidine  Repression of enzyme for histidine : product feed back repression HMG CoA Reductase: Induction or stimulation of synthesis = fed state or insulin effect Repression of synthesis = fasting or starvation • Hormone sensitive Lipoprotein lipase : Induction or stimulation =adrenalin, cortisol, fasting, stress Repression = insulin, fed state

ALLOSTERIC REGULATION • Low molecular wt allosteric effectors structurally not similar to substrate E1 E2 E3 A  B  C  D Bind at sites other than active site leading to feed back inhibition Usually product or last small molecule before macromolecules in biosynthesis

PROENZYMES • Inactive enzymes initially secreted as large molecules, active site not exposed Pepsinogen HCl Pepsin Prochyomotrypsin Proteolysis Chymotrypsin 1 245 1 245 Trypsinogen Trypsin Enteropeptidase 1 15 16 245 πChymotrypsin 7 245 Trypsin active form 1 13 16 146 149 245 Chymotrypsin active

PROENZYMES • Required for control of catalytic activity of enzymes so that catalytic activities only occur when required • Pancreatic enzymes if all the time active  auto digestion of pancreas • Blood clot lysis enzymes only active when blood clot is formed

Examples of Pro enzymes • Pepsinogen • Trypsinogen • Profibrolysin

ISOENZYMES • Physically distinct forms or protomers of an oligmeric enzyme which can occur in different tissues of same organs, in different cell types, or in sub cellular compartments catalyzing same reaction. these can be separated by electrophoresis. •  Lactate dehydrogenase on electrophoresis gives 5 different bands and has 4 protomers

CK1 BB OCCURS IN BRAIN,SMOOTH MUSCLES of GIT AND URINARY TRACT CK2 MB MYOCARDIUM (35 %), SK MUSCLE (5%)  IN ACUTE MI CK3 MM OCCURS IN SK MUSCLES  IN MUSCLE DYSTROPHIES CREATININE KINASE (CK): 3 ISOENZYMES

LACTATE DEHYDROGENASE: 5 ISOENZYMES

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