eka Birte-Anad i) fgeste fester oper series Zoology # rod: ‘ W : Cry ear sau Ray hapter 35 sul bus Chapter 4/3: ‘Gnergy and laws of transformation, Activation énergy, 2 inzyme: Structure, Function and Factors affecting their activity, 3. Cofactors and Coenzyme: . 4. ATP 5. How cells convert Energy? An overview WHAT IS ENERGY? 5 Fhe capacity to do work is called energy. Work is the transfer of energy. Energy ‘can also be transformed. For example, a plant can transform solar energy into chemical energy. The plant-e4n then be burned in a steam generator, Thus its ehergy is transformed inje“the energy of motion. Energy has many forms: @ The heat from a furnace @ The.sound of a jet plai @ The electric current, @ The radioactivity ira heart pacemaker (CT scan machine). ~ @ The pull of a magnet. ‘ States of Energy aa exists in two states: Kinetic energy: The energy due to motion is called kinetic energy. Fot example, thundering waterfall 4 heat Potential energy: The, stored energy is called potential energy. Energy i «chemical bonds is a form of potential energy in a living animal. Animals use’ the bond energy in organic: molecules in biological work. Much of the work an animal involves the transformation of potential energy to kinetic energy in its cells. ‘at lights a bulb.i i 4> Eneigy, Enzyme: Life's Driving and Contréiling function Measurement of energy Energy is measured in terms of thermodynamics. The commoply use the kilocalorie or calorie | i (a) A kilocalorie (Keal) isAhe amount of heat required to raise temperature of 1 kg of water by 17€. Itis equal to 1,000 calories. A daily intake of energy for an average persoh is approximately 2,000;to 2,59 kcal. (b) A calorie (c) is thé amount of heat required to raise the temperature of 1 g (1 cc) of water 1° C from 14.5 to 15.5° C. THE LAWS OF ENERGY TRANSFORMATIONS ‘at production. The study of energy is called d unit for measuring heat in an animal is There age two laws of thermodynamic: 4.” First law of thermodynamics : It is also called the law of energy conservation, It states that energy can neither be created nor destroyed, it can only be transformed from one form to another. For example, electrical energy passes through a.hot plate to produce heat energy. Or it can be tydnsformed from potential to kinetic energy. For example a squirrel eats a yrut and then uses this energy to climb a. tree. But energy can never be lost’or created. Thus, the total amount of energy in the universe remains constaft. 2 Second law of thermodynamics It states that all objects in the universe tend ‘to become more disordered and that the total amount of disorder in the universe is foo increasing. The measure of this degree of disorganization is called ehtropy. For example, natural gas is burnt{n a stove. Potential chemical energy Js stored in the bonds of the gas moleciles. This energy is converted into light (the blue flame) and heat. Some of fhe heat energy can be used to boil water on the stove. Some energy is lost in the kitchen. This energy is no longer available to do work. This unusable energy increased entropy. * a ACTIVATION ENERGY The minimum amount of free energy to start q chemical rea activation energy. Most chemical reactions require an input energy to start. For. example a match is lit. Its heat energy is used to start.wood burning in a fireplace, Input energy must break existing chemical bonds in @ chemical reaction, Then this energy form new bonds. This input energy is called activation energy in thermodynamics. There are two types of reactions: i fa) Exergonic reaction: The reactions in which net release of energy take } place is called exergoniic reaction. The reactants contain more energy than the products. The amount of this excess energy is called free energy. This energy is greater than the activation energy required to initiate’a re Itistel iled exergonic. jorgonic reaction yonis reactions. cased into the environment These reactions occur spontaneously and are which absorb energy are called contains more energy than the reactants. egy from the environment than is ontanaously. So thay are called The The pr Tene Fig: (a) An exergonic react energy Lower ——————> Hiahe v (aD Reactanis Lam). - Product has (56) tower > Hgner er one n Activation energy Energy released during product formation Product Se Start dl End Fig: Activation energy verted to product substance in a n period of time is leper reaction does. not d the amount of acti called reaction rate. The reaction rate of an exergonic : Action rate and catalysis ‘ne amount of reactant substance con ji" nd'on the releas vation energy requ ed energy. Its reaction rate depends on red for the starting of reaction. A few | energy hurdle. Therefore, larger the in overcoming the initial f a chemical reaction, the mo fixed. For example, when certain molecules succeed activation energy © However, activation, energies are not re-slowly the reaction occurs. chemical eerT a iy . 4 Life's Driving and Controlling function 4> Energy. Er ; bonds are stressed, they may break more easily. The lowering of the activation of energy of a reaction is called catalysis. Catalysts — : Any substance that performs catalysis is called a catalyst. A catalyst is a substance’ that accelerates the rate of a chemical reaction The reaction proceeds at a lower environmental temperature by decreasing the activation energy. But catalyst itself is not used up in the reaction. The catalysts are always enzymes in cells. 4 Transition z state {initia state) Amount of energy Lower (Final state) Start end Time . Fig: Catalysis reduces the activation energy ENZYMES: BIOLOGICAL CATALYSTS eae nn Tn enzyme is a biological catalyst that can accelerate a specific chemical reaction by lowering the activation energy but remain unaltered in the process. Most enzymes are proteins. Some are nucleic acids (RNA) like ribozymes. Enzymes have enormous catalytic power. They greatly increase the tate at which specific chemical reactions take place: tue Role of enzyme in Catalysis The metabolism of an animal is controlled specifically at some points. Catalysis takes place at this point. Therefore, catalysis is one of the most, important functions in life. Catalysis is a series of chemical processes. These bbrocesses are regulated by the ehzymes. Thus the same reaction can occur without enzyme. But it will occur at a much slower rate. The enzymes remain unaltered. So enzyme can be used again and again. * 2, Specificity of enzyme . An enzyme is extremely selective for the reaction. The reactants of enzymatic reactions are called substrates. 7The of 4, 4 uu Enzyme substrate reaction at a rate compatible with life. The enzymes channel molecules into specific chemical pathways. So the metabolism proceeds under these different conditi Master Success series Zoolagy Ar ie precise “fit” between an enzyme and its specific suostrate is necessary for catalysis, For example, cellular concentrations of many feactants must be kept at ‘ow levels. it avoids undesirable side reactions. At the same time, concentrations enzyme must be kept high for the required reactions. Thus the reaction occurs ~~ Nomenclature of enzyme All enzyme nathes end with the suffix ase. They are named after their substrate. Bui several digestive enzy tule, For ex were discovered earlier. They do not follow this mple, pepsin and lrypsin y ENZYME STRUCTURE Enzyr are three dimeisicinal globular protein molecules or nucleic acids. They JUp the chemical reaction in the living organisms. It has at least one surface region. This region has a crevice or pocket. This crevice occupies only a small portion of the surface of enzymes. This crevice is known as the enzyme’s active site. : oe Active site has a specific shape. Therefore, a substrate molecule fits into it ina very specific way. Weak chemical forces like hydrogen bonds keep this substrate in place. : The substrate binds with the enzyme. It changes the shape of enzyme. This phenomenon is called induced fit. The attachment of the active site with the substrate brings chemical groups of the active site into positions. It increases their ability to work on the substrate and to catalyze the chemical reaction. When the reaction is completed, the product of the catalyzed reaction is released. The f° enzyme resumes its initial conformation (shape). It is ready to catalyze another [| hemical reaction. ' _/ ena FUNCTION : L A substrate molecule binds with the active site of enzyme, Thus enzyme- |: substrate complex (ES) is formed. This is the first step in-enzyme catalysis. vos 2 Enzyine + Substrate ~——» Enzyme substrate complex —» Enzyme + Product The unstable amino acid groups of the enzyme form certain bonds with the 4g, substrate. Thus enzyme-substrate compléx is formed. : . These side groups distort the substrate bonds. So it lower the activation energy needed to break the bonds. . The bonds break. It releases the substrate. | . The substrate now reacts to produce the final product and release the enzyme. |susstaie Fig: Enzyme action FACTORS AFFECTING ENZYME ACTIVITY | Some factors alter the three-dimensional shape of 3n enzyme. Thus they the activity of enzyme. Two factors affe: activity. These are t and pH. . 7 41. Temperature = The shape of a protein or nucleic acid is determiner by its hydrogen bonds Temperature disrupts hydrogen bonds. For example, the enzymes of most of birds and mammal have function in a narrow range of temperature. This range Is between 35 and 40° C : (a) Low Temperature: The bonds of protcin of enzymes are not flexible below 35° C. So it does not permit the change in shape. This change of shape is necessary for substrate to fit into a reactive site. (b) High Temperature: The bonds are too weak to hold the protein in proper position above 40°C. So enzyme can not maintain its shape. When proper shape is lost, the enzyme is destroyed. This loss of shape is called denaturation. ‘Optimal temperature i Salwar i Pepsin Smylass Tomzia sto i ee A 1 ( A /\ | Vo\ Enzyme activity L L Jit, 70 20° ~«30~—«a7 40 “100 2 | | I I | Fig: (a) Affect of temperature on enzyme action {b) Affect 6f pH on enzyme action PH value ——~ f £ is (00 low, the.H” ions combine with the R E80 it reduces their ability to bind with substrates. Acidic ‘oups of ihe enzyrr Environmers isenes Zoology A isster Succes: enzytnes, Attachment of a cofactor changes the shape of the protein ands s itto combine with its substrate ome enzymes function at a low pH For example ny has an optimal pH of 2. Pepsin has an amino acid sequence. This maintains its ionic and hydrogen bonds. So it can function at such m pH 9. This pH is found in the H of an enzyme shows the pH of iow p ¢ Trypsin is active in the more basic mediu srnall intestine of mammals. The optimum pI nody fluid. Enzymes are found in this fluid, ae ol Cofactor Fig: Action of cofactor OFACTORS AND COENZYMES fofactors ‘he metal ions which ar cbfactors. These metal ions ar ions change @ nonfunctioning act a cofactor changes the shape of the protein. It allow: with its substrate. The cofactors of other enzymes pal bonds between the enzyme and its substrate during enzy formation joenzymes : : tein, organic molecules that participate in enzym e loosely attached with the enzymes are called 2 Ca?, Mg?, Mn’, Cu”, and Zn?. These metal ive site to a functioning one. The attachment of 4 s the enzyme to combine Micipate in the temporary ime-substrate complex 3 nes are non pro’ in transporting electrons from oné 7 oenzyl c et reactions. They are often used i enzyme |to anoth Many vitamins like niacin and 1 her. These electrons are present in the form of hydrogen atoms. ‘iboflavin function as coenzymes. Or they are used {24 — DOCTOR Master Success series BOTANY D Syllabus 1. Diffusion, imbibitions, osmotic and osmoti 2, Water relations, (water potential, pressure I 3, Absorption and translocation of water. 4. 5. ic components * tential, matric potential) “Transpiration, factor affecting transpiration Stomatalsieture and funtion (Stonsa hysiology) DIFFUSION The movement of molecules fram called diffusion, Diffusion occurs 4 process. Diffusion continues ill dyna: thermodynamics. But itis a very slow process. The tae and the direction of diffusion of different sub in their cenceotration at different points. It is indeps ion Co lower concentration is It is a spontaneous lows laws of higher concentrati own the concentration gradient. mic couilibrivin ts achieved. it foll pstances depend apon the difference endent of the préseticc of other substances, equilltrlum Examples 1. Oxygen is utilized aid carbon dioxide is removed during respiration in a leaf, Thisis 3s of ce et 2, Petrol and perfume are vol 3. A crystal of copper sulphate is placed in a beaker of wate © diffusion medium produce resistance to the diffusing-particles. Greater the density of the medium, greater will be this resistance. Therefore, it slower the rate of diffusion. For . ~ example, diffusion of sugar molecules in water. Sugar dissolves rapidly in hot water than’. © “in cold water. The water molecules become ‘less dense at higher temperature. Therefore; diffuse through water with greater velocity. The density of a substance depends'upon its * molecular weight and the distance between.the molecules. The. distance-between the have least distances. Therefore, they have higher density and low rate of diffusion. © Graham’s law : a : © St states that the rates of diffusion of gases ate inversely proportional to the square 5 = The pressure exerted by the diffusing particles is imown.as diffusion pressure. This spiration tion, Translocation é Transp sa Carbon dioxide diffuses from the outer air, But oxygen diffuses in the reverse directlon. ile liquids. Ca halene balls are volatile latile liquids. Camphor and napht i way, Their odour can be detected from gome distant : 2> Diffusion, Osmas's, Absor CO; collects in the intercellular spaces of the le intercellular spaces into the solids, They diffuse in the same hy +. It slowly digsolves. The have lesser surface of the crystal has greater concentration, But other parts of : : concentration of copper Se ‘Therefore, the molecules of copper ule ia from surface to other part. \fler some time the crystal disappears. Its molecures evenly distributed throughout the surrounding liquid. Factors affecting the diffusion Following factors are responsible for diffusion: 1. Chemical potential All the three states of matter solid, liquid and gas are made up of molecules. These molecules possess kinetic energy or free energy at temperature above -273°C. The total kinetic energy of the molecules is called chemical potential. Therefore, the molecules are in constant motion, They collide with one another. Thus molecules of a substance try to move from the region of their higher concentration or higher kinetic energy to the region of their lower concentration or lower kinetic energy. Thus diffusion directly depends on the chemical potential. Temperature and pressure affects the chemical potential. Therefore they also affect the rate of diffusion. 2, Density The density of the diffusion medium also affects the rate of diffusion. The molecules of its resistance to the diffusing sugar molecules decteases. Thus'the sugar molecule can, molecules is the greatest in gases. Therefore, gases:have the lowest density. The solids . roots of their densities. Graham’s law is applied on the diffusion of, gases.. ‘Where r and rp are the rate of diffusion’‘and dy and dp are their densities. _- 3, Diffusion pressure . - :‘ar Success series BOTANY D . rectly proportional to the concentration or the number of diffusing particles. se concentration of diffusing particles in a system, the greater Is their diffusion the diffusion-pressure of coppet sulphate particl is the high rystal. But it is the lowest in the other regions. | sulphate diffuse from the ‘region of their greater diffusion pressure to lesser diffusion near the dissolvir particles of cope! the region of th ssure. eee] oae ee Sd Fob cy Seo 190° C9300 20 wor yO, @02e, ge 00 09 a” 2)? /920,.9.0900,0,° peo aed | 00? 20%, la 0 o 09} @ 90900 2%0 %0 | : A barrler Fig: Process of diffusion Importance of diffusion in plants Diffusion is very important process in plants. i ‘. 1. Plants transfer food particles from phloem and water particles from xylem through diffusion. 2. They get carbon dioxid through stomata and mesophyll cells. Photosynthesis also includes diffusion in a number of steps. Root absorbs weter and salts from the soil. ‘This water is transferred from roots to eaves throuigh the process of diffusion.” 5, Fungi absorb digested food by the process of diffusion. IMBIBITION The special type of diffusion in which an imbibant absorbs water on its surface without.dissolving in it is called imbibition, Water movement is along 2 concentration gradient in imbibition. Therefore, imbibition is a special type of diffusion. In imbibition, water is absorbed by solids-colloids. It causes an enormous increase in volume. Water potential gradient between’ absorbent {imbibant) and liquid imbibed is essential for imbibition. Imbibition occurs when a wetting fluid displaces a non-welting fluid. t | imbibant (adsorbent) is a hydrophilic surfaces like protein, starch or clay, Different | types of organic substances have different imbibing capacities, Proteins have a-very high imbibing capacity then starch and cellulose. Therefore, proteinaceous pea seeds swell more on imbibition than starchy wheat seeds, The-force generated by the imbibants is called imbibition pressure or metric potentia ‘The metric potential is similar to solute patential. The direction of water movement is from a region of higher water potential to ‘one of lower water potential. Hydrogen bonding is responsible for binding (adsorption) of water molecules to the hydrophilic. surfaces. : Significance of imbibition . . The insoluble, solid, hydrophilic-protoplasmic. and cell wall constituents absorb water by imbibition. . © t Je and release oxygen through difision. This diffusion occurs ae| | 2 Diffusion, Osmosis, Absorption, Translocation & Transpiration, '. Dey plant material tke dry wood is placed in water. It swells and its increases, Barley Seed Germination htatin 2 Dry Pea seeds are placed in Water, These also swell, It helps in the germination of seed, 3. IF the imbibant is dried and then (imbibition pressure), Th put in water, it can develop a high pressure the wooden door or w in He bressure imbibes water. For example, imbibition oeeurs'in ow frame during humid weather or rainy season, It becomes difficult to close door ater imbibition 4 Imbibition also. mainiains genetic. clock that controls circadian rhythms’ in Arabidopsis thaliana and other plans,» 5. The grafted tis uring grafting of tissues | Get waler through imbibition, & Ambibition has also role in absorption of waies by : 1991 a initial stages. _ OSMOSIS : | The movement of solv ‘ent molecules from the ri ‘gion of higher concentration to the region of lower concentration ( lc membrane is called osmosis, Demoustration of osmosis Althistle funnel is filled with arubber membrane, The thistle of the thistle funnel dips under water, The level of sugar sol down the level of sugar solution after about 24tours, [tis ab: } solution in the thistle funnel moved down ward. It shows that osmosis occur thrpugh the [semi permeable membrane, After some time; the concentration of sugar molecules and ‘water molecules will be the same both in the beaker and the thistle furinel: Thetefore, the rough semi permeabl icentrated solution of sucros 0 sé. Its mouth is closed with funnel is inverted in beaker Containing water, The mouth eer le lution is marked, Again note served that the levellof sugar - osmosis will stop. Factors affecting the osmosis : : 1. Osmotic pressure (OP) ; The maximum pressure that develops when a solutio n is separated. from its solvent by a semi permeable membrane’is called osmotic pressure..It is also called osmotic28 poctor potential. At moves t aster Succass series BOTANY O he solvent inward. 10% solution of sugar in water differentially permeable membrane pure water Fig: ‘Demonstration of diffusion 2, Diffusion pressure (DP) The diffusio. pressure of wateris more than the diffusion pressure of solution. Therefore, osmosis occurs from higher diffusion pressure (0 lower diffusion pressure of solvent. The difference of diffusion pressures of solvent molecules and its solution is called diffusion pressure deficit (DPD). Osmosis occurs only. when the value of DPD is more than zero. 3, Turgor pressure (TP) . The pressure exerted by the cell sap on the cell wall of-plant cell is called turgor pressure; It opposes the process of ‘osmosis. Thus theré is following relations between DPD, OP and TP La DPD = OP-7P Mechanism of osmosis : aos eable membrane. It is Osmosis is the movenent of a solvent across @ semi-perm: movement toward a higher concentration of solute. In biological systems, solvent is typically water. But osmosis can occur in other liquids dnd even gases. : Let we submerge a cell in water, The water molecules pass through the cell membrane from an area of low solute concentration to high solute concentration. For example, if the ‘cell is submerged in saltwater, water molecules move out of the ‘cell. If a cell is submerged in freshwater, water molecules move into the cell. In some cases, membrane has a volume of pure water on both sides. Now water molecules pass in and out in each directjon at exactly the same rate. There is no net flow of water through the membrane. H E Old concepts : taceoeding to old concepts, two mechanisms were responsible for driving osmosis. These 5 are:ter ow | is, Absorplion, Translocation & Transpiration 2 Diffusion, Osmasis jon of water on the highs i y solute. Thus there is lower concentration 01 ai 2) Dilution of water by solute. fusion of water along a anal e 2. Therefore a di solute concentration side of the menibran: concentration gradient : i It caus b) Attraction of solute for water. It \ ech concentration side of the membrane. ‘Thetefore, net mover oe ‘ i , Therefore, Both these mechanisms are not well supported by experimental evidences. these are note accepted as true mechanisms'of osmosis. New concept ' noe eae ic According to new concepts, Osmosis, unlike diffusion, requires a force. ae pressure is the main support for osmosis in many plants. The osmotic a Bs ; raises the turgor pressure. Turgor pressure is exerted against the cell wall. Water continues to enter until turgor pressure become equal the osmotic pressure. Now it creates asteady state. : a) We place a plant cell in a solution that is hypertonic relative to the cytoplasm. | Now water moves out of the cell. The cell shrinks. Therefore, cell becomes flaccid. Ih extreme cases, the cell becomes plasmolyzed. The cell membrane disengages with the cell wall due to lack of water pressure on it in plasmolyzed céll. b) Now we place a plant cell in a solution that is hypotonic relative to place a pl \ypo! Now water moves into the cell. The cell swells to become turgid. Loa water Equal water coneenation outide concentrations inside tecel Bou ne eS less free water on the higher solute water toward the uk cytoplasm, High water concentration outside Plasmolyzed Flaccid Turgid | (ie concentrated {ie equal solute {le pure water or > solution outside) concentrations dilate solution inside & out); outside) Fig: Osmosis in plant eells Biological role or significance of osmosis : |. A large vacuole is present in plant cells. It is bounded by tonoplast. and out of vacuole through tonoplast by osmosis. ' 2. Osmosis is responsible for the ability of plant roots to draw water from the soil, Plants concentrate solutes in their root cells by active transport. Now water enters the roots Water move in,{ \ . \ : 30. DOCTOR Master Success series BOTANY D by osmosis. 3, Root pressure is caused by process of osmosis of water responsible for ascent of sap in many smaller plants. es 4, Osmo Regulation of Isoleucine synthesis ‘ckample of feedback Inhibition of an anabolic cca orod \ Sith that in enind, explain how ATP might be | Ca in feedback Inhibltlon of a catabolic pathway ae I For Suggested ansiers. + quaerene: Energy ot . | : i. 4 : » Scanned with Cphscanne : 1 tS :© pocTor Master Success series BOTANY D . . Syllabus Definition, re, classification and properties 1D NATURE OF ENZYME An enzymes a V catalyst (hat ¢ accelerate a: ‘ceifie chemical reaction by lowering, ‘ activation. energy but remain unaltered in the process: Most enzymes are proteins. Some are nucleic acids (RNA) like riboaymet Enzymes have enormous fe catalytic power- ‘They greatly increase the rate at which specific chemical reactions take place. Enzymes: have following components: Globular part, active site, cofactors, and coenzymes: Globular part roe main body of enzyme iS composed of globular protein, I has a large number of ais. Enzyme body sbows tetany RAPE red Declan inked by peptide b protein configuration: In his ease, polypeptide chain folds Up>” itself to form globule. protein. Polypeptide chain of tertiary structure iS held by disulphide ridge ot 3, f enzyme is very important for its. proper wh Th hydrophobic interaction. Globular ‘structure, of functioning. Loss 0 jestroys enzyme: 7 hetivesite d ¢ globular, structure of enzyme has at le crevice or pocket. Tis crevice ‘occupies only ig known as the enzyme’s active site, Acti substrate, molecule fits into it ina very. specific way- bonds keep this substrate in place. The active site of the enzymes is 1 regions. izes the specific substrate and forms enzyme 1 _gyBinding site: It_recognl complex. This reaction activates the catalytiv'site. ‘The activated catalytic site changes the substrate into products. pee site: dels of active site of enzymes ;yen about the activity of active site: ‘Two models are 2" Key and lock model } Emil Fischer proposed the Tock’ and key mo specific enzyme can transform on! f globular siructure d st one surface region. This region has @ small portion of the surface of enzymes. li vite has a specific shape. Therefore, Weak chemical forees like bydroge ade.up of tw subsiratt del in 1890. According to this. model jy specific substrate into products. According |: 4> Enzymes 8s this model, the active site is a rigid structure. It cannot be changed during any step ofthe © reaction, Later studies have not supported this model in all the reactions. - Induced fit model This model w: pnb Kestland in 1959, He proposed this rnodel on the basis of now evidences. He describeSNhat when a substrate combines with an enzyme, it induces changes in the at site. These changes enable the enzyme to perform its catalytic activity, : : Cofactor Catalytic site Coenzyme y ey ee 8 ce J , Apoenzyme ee ty Holoenzyme lar Fig: Structure of enzyme * a ee ce . : fe metal fous which are loosely attached with the enzymes are called cofactors. ‘These’ metal ions: are Ca", Mg?, Mn”, Cu'?, and Zn", These. metal ions change @ nonfunctioning active site tg a functioning one. The attachment of a cofactor changes the shape of the protein. It allows the enzyme to-combine with its substrate. The cofactors of other enzymes participate in the temporary bonds between the enzyme and its substrate during enzyme-substrate complex formation, Functions of cofactors «They are essential for proper functioning of enzymes. + The co-factors act as a bridge between the enzyme and substrate. They.often directly take part in the chemical reactions ‘during catalysis « the co-factors provide source of chemigal energy. This energy is sary to drive a reaction, 4... Cocnzymes and prosthetic groups Coenzymes are loosely attached non protein, organic mofeenles that patticipate in eazyme-catalyzed reactions, The covalently bonded non-protein part of enzyme is Coenaymes are oflen used in transporting electrons from one } called prosthetic group/| Ce me to another. These electrons are present 1n the form of hydrogen. atoms, Manyvatomins 1 B Allosteric site Some enzymes have special allosteric site. Some specific effectors can bind with ‘this allosteric site. Allosteric enzymes change their structure in response to binding of effectors. It is called allosteric modulation, This modulation can be direct or indirect. The effector may bind directly to binding sites in the enzyme. Or effector binds to other proteins or protein subunits. This:protein interacts wilh the allosteric enzyme ard thus influences catalytic activity. 6.7 Apoenzyme and holoenzyme Some enzymes require prosthetic group for their normal activities. Prosthetic group is 1 firmly bound to the enzyme. Tt activates the enzyme. The inactive enzyme without Ff prosthetic efoup is called apoenayme. The active enzyme with attached prosthetic group} as is called holoenzyme Apoonaye Cotactor (peoeinporton), (conproei portion, Inactive caclvetor 7... Types of-enzymes Enzymes of two types: (a) Intracellular enayines or endocinzymes: They at within the cell, The great majority of plant enzymes are endoenzymes. (6) Extracellular enzymes or exoenzymies: They diffuse out of the cell and act on some 66 pocTOR Master Success series BOTANY D ‘acin and riboflavin function as coenaymes. Or they are used to make coenaymes. Coenzymes transport energy in the form of hydrogen atoms from one enzyme to another. One of the mo’t important coenzymes in the cell is the hydrogen acceptor nicotinamide adenine dinucleotide (NAD). Jt is made from vitamin B. NAD / acquires ahydrogen atom from an enzyme and it reduces to NADH. The electron of the hydrogen atom contains energy. This energy is carried by NADH molecule. For example, Various foods are oxidized in the cell. The cell removes electrons from the food molecules. It transfers this electron to NAD. It reduces to NADH. i ‘Fig: Apoenzyme and holoenzyme Ani com’ Cyclic AMP a Regulator (nititor) Inactive form ofthe enzyme Fig: Allosteric site of enzyme Holoenzyme (whole enzyre), clive» 4 Enzymes engi and cacteria and in some of i i mes aré present in fungi ai ae la Oe Exley are produced by the living protoplasm. But they re environment of iving cll fr ther action do not require environment of a living cel ee CATALYSIS (MECHANISM OF ENZY ME ACTION) } (Out of syllabus only for Unive y of Baluchistan and TUB) H 1 Specificity of Enzymes : : 5 a specific chemical f . yyme has a specific chemical 35} Anenzyme is a three dimensional globular protein. Each one Lae Gh specificity, composition, It has specifie amino acids and has specific shape. ae iar aieate 1 toch enzyme recognizes and reacts with a specific substrate. It then dl ie 2 i again aid into product. In the end, the enzynié releases unaltered. Thus it can be use he again, : : | : Products Py Enzyme changes shape . ‘Supswate ——_gightfy as substrate binds (oo (8 re) ee dr ‘Substrate entering Enzymelsubswale —_Enzymedyroducts Products leaving acive ste of enzyine complex complex ‘cue site of enzyme ~ is out Fig: Mechanism of Catalysis wup | ® Chain of Enzymes | In some cases, enzymes act in series of chemical reactions." These enzymes are present in } 2 specific order to complete a metabolic pathway like respiration and photosynthesis. | Successive enzymes are present together in precise order. Thus one enzyme hands over F the substrate to another enzyme. In this way, they form an enzyme coenzyme chain. The - product formed by the one enzyme is transferred to the next enzyme. Finally the end- product is formed. } 3 Formation of enzyme substrate complex , j- Enzyme and substrate react with each other through active site, Active site is a definite +} charge bearing site of an enzyme, Amino acids are present in the polypeptide chain of | active site of enzyme. .Thesé amino acids form the charge and shape of the active site. 4 These amino acids come close to each other and form polypeptide chains. These amino | acids are brought closer. They are arranged in specific way by folding and coiling of f polypeptide chain. It occurs within the globular symmetry of enzyme. +. The active site of the enzymes is made up of two definite regions. ‘ ___ 4.4) Binding site: It helps the enzyme in recognition aid binding of proper substrate and arity =} form ES (enzyme substrate) complex. This reaction activates the catalytic site. b) Catalytic site: The activated catalytic site changes the substrate into products." pocTOR Master Suocess series BOTANY D catalysis. the enzyme ‘detach from the products unchanged. It remains unchanged n. The enzymes require aqueous medium for its activities. — f+ the reactio p+ S = ES =—_—_— Enzyme substrate Enzyme substrate. Enzyme Substrate Be : Complex 4 : Substrate C= a) t Aetiee she I 4 \_——~ i f \ ‘ : Key (substrate) Lock enzyme) d a Enzyme ; | p , : : 5 s th (b) EB 7 aa Lock Key Complex.” Enzyme-Substrate i Complex 8 Fig: Key and lock model a 4 | MODELS OF ENZYME ACTION JS and Lock Model Tisil Fischer proposed the lock and Key model in 1890. According ¢o this model @ nly specifie substrate into products. According to \f the specific enzyme can transform this model, the active sie isa rigid structure. It cannot be changed during any step of reaction. Later studies have not supported this model in all the reactions. It has following features: : : 1. Enzymes-are locks: Enzymes work like a lock in the chemical reaction process. The body contains many enzymes and many substrates. But correct enzyme must J efficiently locate and unite with its specific substrate, Each enzyme can attract its specific substrate and accelerate the chemical reaction. Then this reaction occurs in 4 the appropriate time span, i. zi Enzymes sites are keyholes: Each enzyme has active sites. It allows specific substrates to enter, Then it produces a chemical reaction product. The enzyme sites work like the keyhole in a lock. It is like the lock on a‘door. Thus only certain keys will fit in the keyholes. Finally, only one key will open the lock. Wrong key cannot 3 unlock the door. : ‘ach enzyme will only respond to one or two substrates. These Substrates are keys:, Each en substrates work like, keys for the- enzyme lock. The molecular structure of the ys38€ che rE “14, Inhibitors jam the lock: Inhibitors work oo “a Enzymes a substrate must correspond in size and shape to the active site on the enzyme. Then it produces the desired chemical response. Enzyme locates its appropriate substrate. Then the substrate enters the receptor site, Finally both the enzyme and substrate form complete union. Now chemical reaction can occur. . : like a key. They can enter the keyhole (active site), But théy cannot turn the lock, The inhibitors jam the active sites. Thus they cannot form product, They slow down or prevent the chemical reaction. Induced Fit Model 2-7! ; This model was proposed by Koshland in 1959.-He proposed this model on the basis of new evidences. He describes that when a substrate combines with’ an enzyme, it induces changes in the active site, These changes enable the enzyrae to perform its catalytic = activity. The induced-fil model is actually’ part of an‘earlicr lock and key model. [t was proposed by Emil Fischer in 1894. The lock and key model states that the substrate acts as a key to the lock of the active site, The active site and substrate are exact matches for each other. It is similar to puzzle pieces fitting together. In (his model. only a single substrate is the exact match for the enzyme, Once the enzyme finds its exact substrate, | the chemical reaction begins. The induced-fit model is considered more correct versior.. According to it. active site F and the substrate are initially not perfect matches for cach other. Rather, the substrate induces a change in shape in enzyme. Now enzyme becomes active. It changes the substrate into product, Induced fit mode! is: a hand-in-glove model. Here it may be difficult to insert the first finger into the proper place. But once done, the other fingers go ineasily. The glove is now properly aligned. Induced Fit Hypothesis a) Fig: Induced fit model CLASSIFICATION OF ENZYME F- NOMENCLATURE OF ENZYME Following roles are followed for the naming of enzymes: 1, Alll enzyme names end with the suffix ase. They are named after their sha For example urease’acts upon urea, The sucrase acts upon sucrose 2. They may be named on the nature: of the reaction that they catalyze. Sor example, oxidase promotes oxidation with the help of molecular oxygen. Dehydrogenase catalyses the removal of hydrogen. Isomerase: catalyses the transformation of a