Hsslive-xi-zoology-ch-4-biomolecules PDF

Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS-Areekode Biomolecule Micromolecules have molecular weight less than...

Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS-Areekode Biomolecule Micromolecules have molecular weight less than 1000 Da. Introduction b) Acid insoluble pool The acid insoluble fraction,  The living organisms are made of different has only four types of organic compounds i.e., types of compound  Proteins,  The chemical analysis reveals that it is  Nucleic acids, composed of elements like C,H,O,  Polysaccharides and  A piece of non living matter also contains  Lipids. same type of elements  But the molecular weights of lipids do not  In fact the living things and non living things exceed 800 Da, come under acid insoluble fraction. Because Cell membrane and other are made up of same elements membranes are broken into pieces during  However the relative abundance of Carbon, the experiment , and form vesicles which are hydrogen is higher in the living organism not water soluble. Therefore, these than in non living matter membrane fragments in the form of vesicles get separated along with the acid insoluble pool and hence in the macromolecular fraction.Therefore lipids are not strictly macromolecule.  The acid insoluble fraction has molecular weight greater than 10000 Da. Analysis of inorganic elements and compounds in the living tissue How to analyze chemicalcomposition? All the carbon compounds that we get from living tissues can be called Analysis of Organic elements and compounds in ‘biomolecules’. However, living organisms have the living tissue also got inorganic elements and compounds in them. A slightly different but destructive  Take any living tissue (a vegetable or a piece experiment has to be done. One weighs a small of liver, etc.) and grind it in Trichloroacetic amount of a living tissue (say a leaf or liver and acid (Cl3CCOOH) using a mortar and a pestle. this is called wet weight) and dry it. All the  We obtain a thick slurry. water,evaporates. The remaining material gives  If we were to strain this through a cheese dry weight. Now if the tissue is fully burnt, all the cloth or cotton we would obtain two carbon compounds are oxidised to gaseous form fractions. (CO2, water vapour) and are removed. What is a)The filtrate or, the acid-soluble pool remaining is called ‘ash’. This ash contains in (micromolecule/biomolecule ) organic elements (like calcium, magnesium etc). b) The retentate or the acid-insoluble fraction Inorganic compounds like sulphate, phosphate, (Biomacromolecule ). etc., are also seen in the acid-soluble fraction. a)Acid soluble pool Scientists have found thousands of organic compounds in the acid-soluble pool. There is one feature common to all those compounds found in the acid soluble pool. They have molecular weights ranging from 18 to around 800 daltons (Da) approximately. SOHSS-AREEKODE/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS-Areekode The acid soluble pool represents roughly Eg :2 In our skeletal muscle, under anaerobic the cytoplasmic composition. The condtions, lactic acid is formed. But under macromolecules from cytoplasm and organelles normal aerobic condtions pyruvic acid is become the acid insoluble fraction. Together formed. they represent the entire chemical composition Eg: 3. In yeast, during fermentation, the same of living tissues or organism. pathway leads to the production of ethanol (Alcohol). Biomolecules, i.e., chemical compounds found in Primary and secondary metabolites living organisms are of two types. One, those  Metabolites are organic compounds which have molecular weights less than one constantly utilzed in various metabolic thousand dalton and are usually referred to as activities in the cells. micromolecules or simply biomolecules while There are two types of metabolites those which are found in the acid insoluble a)Primary metabolites: fraction are called macromolecules or  It is essential to the growth of the cell. biomacromolecules.  Primary metabolites have identifiable functions and play known roles in normal physiologial processes  They are produced continuously during the growth phase and are involved in primary metabolic processes Eg: proteins, nucleic acids, and polysaccharides b)Secondary metabolites:  They are the compounds which are derived by pathways from primary metabolic routs, and are not essential to sustain the life of cells.  These compounds do not have a continuous production Metabolism  Many of secondary metabolites are useful to  The sum total of all chemical reactions taking ‘human welfare’ (e.g., rubber, drugs, spices, place in a living organism is called scents and pigments). metabolism  Some secondary metabolites have ecological  Majority of these metabolic reactions are importance always linked to some other reactions. This series of linked reactions is called metabolic pathways (So a multistep chemical reactions, when each of the step is catalysed by the same enzyme complex or different enzyme is called a metabolic pathway.)  Another feature of these metabolic reactions is that every chemical reaction is a catalysed reactions and it is catalysed by enzymes.  Eg: 1. In Glycolysis, glucose becomes Pyruvic acid through ten different enzymes catalysed metabolic reactions. SOHSS-AREEKODE/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS-Areekode Difference between primary metabolites and secondary metabolites Primary metabolites Secondary metabolites They are involved in They are not directly normal growth involved in growth ,development and development and reproduction reproduction Examples include Amino Examples included acids,sugars.. pigments,alkaloids… Essential to sustain life Not essential to sustain of organism the life of cells. They are produced These compounds do continuously during the not have a continuous growth phase production SOHSS-AREEKODE/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS SOHSS-Areekode  1. AMINO ACIDS Amino acids are building blocks of Classification of amino acids a)Based on number of amino and carboxyl proteins. groups, amino acidss are classified into  Amino acids are organic compou compounds i)Acidic amino acids containing an amino group an acidic group Eg:Glutamic Glutamic acid as substituents on the same carbon i.e., the ii)Basic amino acids αcarbon.. Hence, they are called α-amino Eg: Lysine acids. They are substituted methanes methanes. iii)Neutral aminoacids:  There are four substituent groups Eg: Valine occupying the four valency positions. Theseare hydrogen, carboxyl group, b)Aromatic romatic amino acids amino group and a variable group Eg: Tyrosine, designated as R group. Phenylalanine, Tryptophan c)Based )Based on the need to the human body , Amino acidss are also classified into a)Essential amino acids acid b)Non Essential ssential amino acids a)Essential amino acids acid The amino acids acid that cannot be synthesized in our body and it should be  Based on the nature of R group there are provided through food is called essential amino many amino acids. However, those which acids. Dietary proteins are the source of essential occur in proteins are only of twenty types. amino acids b)Non essentialamino amino acids acid The amino acids acid that can be synthesized in our body and no need to be supplied through food is called non essential amino acids ZWITTER ION A particular property of amino acids is the ionizable nature of –NH2 and –COOH groups. Hence in solutions of different pHs, the structure of amino acids changes. changes At a particular pH (Isoelctric point) of solution, amino acids occur as a dipolar ions with +ve and –ve ve charge in the same molecule. They are called Zwitter ions 2. PROTEINS  Proteins are polypeptides formed of number of amino acids acid linked together by means of Peptide bond. bond  Each protein is a polymer of amino acids  Peptide bond is formed for is formed when the carboxyl (-COOH)COOH) group of one amino acid reacts with the amino (-NH2) ( SOHSS-AREEKODE/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS-Areekode group of the next amino acid with the elimination of a water (the process is called dehydration)  As there are 20 types of amino acids (e.g., alanine, cysteine, proline, tryptophan, lysine, etc.), a protein is a heteropolymer and not a homopolymer. A homopolymer has only one type of monomer repeating ‘n’ b)Secondary structure of protein number of times.Proteins are formed of  If the polypeptide is coiled to form of a helix number of different kinds amino acids and (similar to a revolving staircase) the structure hence proteins are called heteropolymers. is called secondary structure of protein.  In proteins, only right handed helices are observed. c)Tertiary structure of protein  If protein chain is also folded upon itself like a hollow woolen ball, giving rise to the tertiary structure. 3-dimensional view of a protein. This complex folding is influenced by various interactions between the amino acid side chains, including hydrogen and  Collagen is the most abundant protein in disulphide linkage. animal world  Tertiary structure is absolutely  Ribulosebisphosphate Carboxylase- necessary for the many biological Oxygenase (RuBisCO) is the most activities of proteins. abundant protein in the whole of the biosphere STRUCTURE OF PROTEINS  Biologists describe the protein structure at four levels d)Quaternary structure a)Primary structure of proteins  If proteins are formed of more than one  This is the simplest level and refers to the polypeptide chain or subunits The manner sequence of amino acids linked together by in which these individual folded peptide bonds in a polypeptide chain. polypeptides or subunits are arranged with  Here the amino acids are arranged in a line. respect to each other (e.g. linear string of spheres, spheres arranged one upon each  If a protein is imagined as a line, the left end other in the form of a cube or plate etc.) is represented by the first amino acid and the the architecture of a protein otherwise right end represented by the last amino acid. called the quaternary structure of a protein.  The first amino acid is also called as N- Eg: adult Haemoglobin consist of 4 subunits. terminal amino acid. The last amino acid is It consist of 2α and 2β chain. called the C-terminal amino acid.  The primary structure of protein gives the positional information of amino acids in a protein (ie. which is the first amino acid, which is second, and so on ) SOHSS-AREEKODE/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS SOHSS-Areekode (b)Arachidonicacid: It has 20 carbon atoms including the carboxyl carbon.  Fatty acids could be i) Saturated-it is without double bond ii) Unsaturated-It It is with one or more C=C double bonds). b)Glycerol  Another simple lipid is glycerol which is trihydroxy propane c)Triglycerides (Fats and Oils) Many lipids have both glycerol and fatty acids. Here the fatty acids are found esterified with glycerol. They can be i)Monoglycerides= onoglycerides= 1 Fatty acids+ 1 Glycerol ii)Diglycerides= 2 fatty acids+ 1glycerol iii)Triglecerides= 3 fatty acids+1 glycyerol gl 3. LIPIDS  Lipids are water Insoluble  Lipids come in a variety of structures, ranging from relatively simple to quite complex:  They could be simple like fatty acids, Glycerol, and complex like triglycerides and  These are also called fats and oils based on phospholipids melting point.  Some tissues especially the neural tissues  Oils have lower melting point (e.g., gingely have lipids with more complex structures oil) and hence remain as a oil in winters. a)Fatty acids.  Fats have high melting point and occur in A fatty acid has a carboxyl group attached solid form in room temperature. to an R group.  Some lipids have phosphorous and a phosphorylated organic compound in them. The R group could be a methyl ((–CH3), or Theseare phospholipids. phospholipids They are found in ethyl (–C2H5) C2H5) or higher number of –CH2 groups cell membrane. (1 carbon to 19 carbons). Eg: Lecithin For example (a)Palmiticacid : It has 16 carbons including carboxyl carbon. SOHSS-AREEKODE/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS SOHSS-Areekode 4. Polysaccharide(Carbohydrates) (Carbohydrates)  Acid insoluble macromolecule  There are more complex polysaccharides in  Polysaccharides are long chains of sugars. nature. They have as building blocks, amino- sugars and chemically modified sugars (e.g., glucosamine, N-acetyl acetyl galactosamine, etc.). 5)Exoskeletons of arthropods have a complex polysaccharide called chitin. These complex polysaccharides are mostly homo polymers.  In a polysaccharide chain (say glycogen), the right end is called the reducing end and the 5. Nucleic acids left end is called the non-reducing reducing end.  They are threads containing different  Nucleic acids are macro molecule and found monosaccharides as building blocks. in the acid insoluble part. For example,  Nucleic acids act as the genetic material in all 1)Cellulose organisms. It is a polymeric polysaccharide consisting  Nucleic acids are polynucleotides (Formed of of only one type of monosaccharide monosaccharide.i.e., glucose. number of nucleotides) nucleotides Cellulose is a homopolymer. Plant cell walls are  A nucleotide has three chemically distinct made of cellulose. Paper made from plant pulp components. and cotton fibre is cellulosic  A heterocyclic compound, 2)Starch  A monosaccharide It is a variant of this but present as a store  A phosphoric acid or phosphate. house of energy in plant tissues. It is also a  The heterocyclic compounds homopolymer of glucose.  The heterocyclic compounds in nucleic 3.Glycogen : acids are the nitrogenous bases named Animals have another variant called adenine, guanine, uracil, cytosine, and glycogen. It is also a homopolymer of glucose. It thymine. has branches as shown in the form of a cartoon  Adenine and Guanine are substituted purines  Uracil, cytosine, and thymine are ‘ substituted pyrimidines.  The skeletal heterocyclic ring is called as purine andd pyrimidine respectively. 4.Inulin It is a polymer of fructose.  The sugar found in polynucleotides is either ribose (a monosaccharide pentose) or 2’ Starch forms helical secondary structures. starch deoxyribose. A nucleic acid containing can hold I2 molecules in the helical portion. The deoxyribose is called deoxyribonucleic acid starch-I2 is blue in colour.. Cellulose does not (DNA) while that which contains ribose is contain complex helices and hence cannot hold called ribonucleic ic acid (RNA) I2. SOHSS-AREEKODE/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS-Areekode  Nucleic acids are of two types DNA and RNA  There are two hydrogen bonds between A DNA (Deoxy ribonucleic acid ) and T and three hydrogen bonds between G  DNA is formed of two polynucleotides. Each and C. poly nucleotides are formed of number of  At each step of ascent, the strand turns nucleotides. 36°.One full turn of the helical strand would  A Single nucleotide is formed of nucleoside involve ten steps or ten base pairs. The pitch and phosphate. would be 34Å. The rise per base pair would be Eg: Adenylic acid, thymidylic acid, guanylic 3.4Å. This form of DNA with the above acid, uridylic acid and cytidylic acid are mentioned salient features is called B-DNA. nucleotides  In a nucleic acid a phosphate moiety links the 3’-carbon of one sugar of one nucleotide to the 5’-carbon of the sugar of the succeeding nucleotide. The bond between the phosphate and hydroxyl group of sugar is an ester bond. As there is one such ester bond on either side, it is called phosphodiester bond Watson crick Model of DNA  This model says that DNA exists as a double helix. The two strands of polynucleotides are antiparallel i.e., run in the opposite direction.  The backbone is formed by the sugar  A nucleoside formed of sugar and nitrogen phosphate-sugar chain. base  The nitrogen bases are projected more or  Eg: less perpendicular to this backbone but Adenosine, Guanosine, Thymidine, Uridine face inside. and Cytidine are nucleosides.  A and G of one strand compulsorily base pairs with T and C, respectively, on the other strand.  There are two hydrogen bonds between A and T and three hydrogen bonds between G and C.  Each strand appears like a helical staircase.  Sugar in DNA is deoxyribose and sugar in RNA is ribose  Nitrogen bases are heterocyclic compounds.It is of two types, purines (Double rings ) and Pyramidine (Single ring).  Purines include Adenine, Guanine,  Pyramidine include Uracil, Cytosine and Thymine  Nitrogen bases in DNA are Adenine, guanine,thymine,Cytosine  Nitrogen bases in RNA is Adenine, guanine, uracil ,Cytosine SOHSS-AREEKODE/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS-Areekode Physical Process and Chemical Process 6. Enzymes Chemical compounds undergo two types  Enzymes are biological catalyst capable of of changes namely physical change and chemical promoting biochemical reactions within a change living system. Physical Reaction Chemical Reaction  Almost all enzymes are proteins. A physical change when bonds are broken  Enzymes are composed of one or several simply refers to a and new bonds are formed change in shape without during transformation, this polypeptide chains. breaking of bonds. will be called a chemical  But some nucleic acids behave like enzymes reaction` are called Ribozymes (Non Protein enzyme) Example: ice melts into Example: Substrate : water, or when water  Ba(OH)2 + H2SO4 → Substance upon which the enzyme act. Or The becomes a vapour BaSO4 + 2H2O is an chemical which is converted into a product is inorganic chemical called a ‘substrate reaction Active site :  Hydrolysis of starch into An active site of an enzyme is a crevice or pocket glucose is an organic into which the substrate fits. Thus enzymes, chemical reaction through their active site, catalyse reactions at a high rate. Active sit is the substrate binding Rate of a physical or chemical process site of an enzyme  Rate of a physical or chemical process refers End product : to the amount of product formed per unit The substance obtained at the end of enzymatic time. It can be expressed as reactions  Enzymes are damaged at high temperature (Above 40o c)  Some enzymes isolated from organism who normally live under extreme high  A general rule of thumb is that rate doubles temperature (like hot vents ) are stable and or decreases by half for every 10°C change in retain their catalytic power even at high either direction. temperature (80-90 c).  Catalysed reactions proceed at rates vastly  Thermal stability is thus an important quality higher than that of uncatalysed ones. of such enzymes isolated from thermophilic  When enzyme catalysed reactions are organisms. observed, the rate would be vastly higher than the same but uncatalysed reaction. Nature of Enzyme action For example Each enzyme (E) has a substrate (S) binding site in its molecule so that ahighly reactive enzyme-substrate complex (ES) is produced. Thiscomplex is short-lived and  In the absence of any enzyme this reaction is dissociates into its product(s) P. very slow, with about 200 molecules of H2CO3 The catalytic cycle of an enzyme being formed in an hour. However, by using action can be described in the followingsteps: the enzyme present within the cytoplasm 1. First, the substrate binds to the active site of called carbonic anhydrase, the reaction the enzyme, fitting into the active site. speeds dramatically with about 600,000 2. The binding of the substrate induces the molecules being formed every second. The enzyme to alter its shape,fitting more tightly enzyme has accelerated the reaction rate by around the substrate. about 10 million times. The power of 3. The active site of the enzyme, now in close enzymes is incredible indeed! proximity of the substrate breaks the chemical bonds of the substrate and thenew enzyme- product complex is formed. SOHSS-AREEKODE/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS-Areekode 4. The enzyme releases the products of the  The difference in average energy content of reaction and the free enzyme is ready to bind ‘S’ from that of this transition state is called to another molecule of the substrate andrun ‘activation energy’ through the catalytic cycle once again  Activation energy is defined as the minimum amount of extra energy required by a reacting molecule to get converted into product.  Enzymes perform a very important task by lowering the activation energy of the reaction (the energy put in for the reaction to begin). This lowering of energy allows the biological reaction to proceed very quickly at a very low temperature which is bearable by living organisms.  Enzymes eventually bring down this energy barrier making the transition of ‘S’ to ‘P’ more Concept of activation energy easy. Factors affecting enzyme activity The activity of an enzyme can be affected by a change in the conditions which can alter the tertiary structure of the protein.  These include temperature, pH, change in substrate concentration or binding of specific chemicals that regulate its activity a)Temperature and pH  In the above graph the y-axis represents the potential energy content.  The x-axis represents the progression of the structural transformation or states through  Enzymes generally function in a narrow the ‘transition state’. range of temperature and pH.  Here we can see two things. The energy level  Each enzyme shows its highest activity at a difference between S and P. particulartemperature and pH called the  If ‘P’ is at a lower level than ‘S’, the reaction optimum temperature and optimum pH. is an exothermic reaction. One need not  Activity declines both below and above the supply energy (by heating) in order to form optimum value. the product. However, whether it is an  Low temperature preserves the enzyme in a exothermic or spontaneous reaction or an temporarily inactive state where as high endothermic or energy requiring reaction, the temperature destroys enzymatic activity ‘S’ has to go through a much higher energy because proteins are denatured by heat. state or transition state. b) Concentration of Substrate  With the increase in substrate concentration, the velocity of the enzymatic reaction rises at SOHSS-AREEKODE/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS-Areekode first. The reaction ultimately reaches a maximum velocity (Vmax) which is not Classification and Nomenclature of exceeded by any further rise in concentration Enzymes of the substrate. Thousands of enzymes have been  This is because the enzyme molecules are discovered, isolated and studied. Mostof these fewer than the substrate molecules and after enzymes have been classified into different saturation of these molecules, there are no groups based on the type of reactions they free enzyme molecules to bind with the catalyse. Enzymes are divided into 6 classes each additional substrate molecules with 4-13 subclasses and named accordingly by a four-digit number. 1.Oxidoreductases/dehydrogenases: Enzymes which catalyse oxidoreduction between two substrates S and S’ e.g., S reduced + S’ oxidised → S oxidised + S’ reduced. 2.Transferases: Enzymes catalysing a transfer of a group, G (other than hydrogen) between a pair of substrate S and S’ e.g., S - G + S’ → S + S’ - G 3.Hydrolases: Enzymes catalysing hydrolysis of ester, ether, peptide, glycosidic, C-C, C-halide or P-N bonds. c) Enzyme Inhibition  The activity of an enzyme is also sensitive to 4.Lyases: Enzymes that catalyse removal of the presence of specific chemicals that bind groups from substrates by mechanisms other to the enzyme than hydrolysis leaving double bonds.  The substance that shutoff the enzyme activities are called inhibitors and the process is called enzyme inhibition.  When the inhibitor closely resembles the substrate in its molecular structure and 5.Isomerases: Includes all enzymes catalysing inhibits the activity of the enzyme, it is inter-conversion of optical, geometric or known as competitive inhibitor. Due to its positional isomers. close structural similarity with the substrate, 6.Ligases: Enzymes catalysing the linking together the inhibitor competes with the substrate for of 2 compounds, the substrate binding site of the enzyme e.g.,enzymes which catalyse joining of C-O, C-S, C- (Active site). Consequently, the substrate N, P-O etc. bonds. cannot bind and as a result, the enzyme action declines, Co-factors e.g., Inhibition of succinic dehydrogenase by  The protein Part of an enzyme is called malonate which closely resembles the apoenzyme. substrate succinate in structure.  The non protein part of enzyme is called  Such competitive inhibitors are often used in cofactor. cofactors are bound to the enzyme to the control of bacterial pathogens. make the enzyme catalytically active  Three kinds of cofactors may be identified: a)prosthetic groups b)co-enzymes c)metal ions. SOHSS-AREEKODE/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS-Areekode a)Prosthetic groups: They are organic compounds and are distinguished from other cofactors in that they are tightly bound to the apoenzyme. Example: in peroxidase and catalase, which catalyze the breakdown of hydrogen peroxide to water and oxygen, haem is the prosthetic group and it is a part of the active site of the enzyme. b)Co-enzymes : They are also organic compounds but their association with the apoenzyme is only transient, usually occurring during the course of catalysis. co-enzymes serve as co-factors in a number of different enzyme catalyzed reactions The essential chemical components of many coenzymes are vitamins, e.g., coenzyme nicotinamide adeninedinucleotide (NAD) and NADP contain the vitamin niacin. c)Metal ions : A number of enzymes require metal ions for their activity which form coordination bonds with side chains at the active site and at the same time form one or more cordination bonds with the substrate, e.g., zinc is a cofactor for the proteolytic enzyme carboxypeptidase. Catalytic activity is lost when the co-factor is removed from the enzyme which testifies that they play a crucial role in the catalytic activity of the enzyme. SOHSS-AREEKODE/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS-AREEKODE BIOMOLECULE 11. (a) Identify the level of protein structure in the given diagram (HSE-JUNE-2022)(3) 1. Name the nucleotide form of guanine. (b) Name two levels of protein structure which (HSE-March 2024)(1) are not three dimensional. 2. Classify the following into polypeptides and (c) Give an example for protein having quaternary polysaccharides : (HSE-March 2024)(2) structure and justify your answer. (Trypsin, Inulin, Insulin, Chitin) 3. When substrate concentration increases, the velocity of enzymatic reaction rises at first. After attaining maximum velocity, it is not exceeded by any further rise in concentration of the substrate. Why ? (HSE-March 2024)(2) 4. Enzyme catalysing the linking together of two components comes under the group_______. (HSE-SEPT-2023)(1) 5. Schematic representation of an enzymatic reaction is given below (HSE-SEPT-2023)(2) 12. Name a protein enables glucose transport into cells. (HSE-SAY/IMP-JAN.-2022)(1) (a) Name ‘S’ and ‘P’ in the above reaction. 13. (a) Identify the following nitrogen bases A and B. (b) Write any two factors affecting enzyme (b) Write the nucleosides of these. reactions 6. (i) Define co-factors. (HSE-SEPT-2023)(2) (ii) Write about any two types of co-factors. 7. General structure of amino acid is given : Draw the structure of the amino acids, (a) glycine and (b) Serine. (HSE-,MARCH-2023)(2) 8. Observe the illustration : (HSE-,MARCH-2023)(2) (HSE-SAY/IMP-JAN -2022)(2) 14. Catalytic activity is lost when the co-factors are removed from the enzyme. (a) What are co-factors ? (b) Name two kinds of co-factors (HSE-SAY/IMP-JAN -2022)(3) 15. Observe the graph and comment (a) Identify A & B and fill the blanks. (b) What happens when the co-factor is removed from the enzyme ? 9. Distinguish between : (HSE-,MARCH-2023)(3) (a) Nucleosides and Nucleotides (b)Primary metabolites and Secondary metabolites (c) Ligases and Lyases 10. Name the most abundant protein in animal world. (HSE-JUNE-2022)(1) (HSE-Sept-2021)(1) NAVAS CHEEMADAN/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS-AREEKODE 16. Write the structure of (HSE-Sept-2021)(2) b)Mention the other two levels of protein (a) Alanine (b) Glycine structure (HSE-March-2019)(2) 17. Non-protein constituents called co-factors are 23............ is the most abundant protein in the animal bound to the enzyme, to make it catalytically world. (HSE-March-2019)(1) active. (HSE-Sept-2021)(3) 24. General formula of amino acid is given below (a) Name the protein part of the enzyme. (HSE-Model-2019(3) (b) Mention any two kinds of co-factors with examples. (c) What happens to the catalytic activity of enzyme, when the co-factor is removed ? 18. Observe the following equation (a) Prepare the amino acid serine using this formula (b) Proteins carry many functions in living organism, Iist any four. a)Explain the catalytic cycle of the enzyme on (c) Give one word the basis of above equation (i) The nucleic acid that behave like enzymes b)Write any 2 factors affecting enzyme (ii) The organic compound tightly bound to the activity ? (HSE-Dec-2020)(3) apoenzyme 19. Which among the following is a primary (iii) The non-protein organic compound that are metabolite ? (HSE-March-2020)(1) tightly bound to the apoenzyme (iv) The protein part of the enzyme 25. Observe the graph given below 20. When substrate concentration increases, the (HSE-Aug-2018)(3) velocity of enzymatic reaction increases at first. After attaining a maximum velocity, it cannot be exceeded by further addition of substrates. Why ? (HSE-March-2020)(2) 21. Match the following (HSE-July-2019)(3) a) Identify the graph. b) Mention the role of Enzyme in this process. 26. The molecular structure of 2 amino acids are given below Name them. 22. Observe the diagram A and B given below (HSE-March-2018)(2) 27. a)Complete the diagrammatic a)What is ‘A’ and ‘B’? representation showing the nature of enzyme action : (HSE-March-2018)(3) NAVAS CHEEMADAN/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS SOHSS-AREEKODE (S,S’- Substrate ) B) S - G + S’ → S + S’ – G (S,S’- substrate,G-Group) substrate,G (HSE-July-2017)(2) b) List out any two factors affecting enzyme activity. 32. “ Proteins is a heteropolymer not a c)Based on the reaction formulae given homopolymer “. Substantiate Substant the below, identify the classes of the statement ? (HSE-July-2017)(2) enzymes. 33. Identify the given biomolecule (HSE-march-2017)(3) 28. a) Effect of change in concentration of substrate on enzyme activity is graphically represented' After reaching a maximum velocity (Vmax)" the reaction is not exceeded by any further rise in concentration of substrate' Explain" b) Mention any 2 other factors that affect enzyme activity ? (HSE-Model Model-2018)(3) 34. Select the wronglymatched wronglymatc pair from the following ? (HSE-March-2017)(1) Collagen Intercellular ground substance Insulin Hormone 29. Fill in the blanks suitably Antiody Sensory reception (HSE-Mo Model-2018)(2) Trypsin Enzyme In a proteins aminoacids are linked by ….(a)…In a polysacharides individual 35. Identify the given biomolecule that comes monosacharides are linked by…….(b)….. under fat (HSE-sept-2016)(1) 30. Identify the wrong statement from the following and correct it (HSE-July July-2017)(1) a)Lipds are not strictly macromolecule b)Cellulose is not a polysaccharide 31. Examples of 2 enzymatic reactions A and B are given.. Identify the class of enzyme in A and B A) S reduced + S’ oxidised → S oxidised + S’ reduced. NAVAS CHEEMADAN/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS-AREEKODE 36. a) Name the biomacromolecule (Polymer) in which peptide bond is present ? b)Name the bond present between phosphate and hydroxy group of sugar in nucleic acid ? (HSE-sept-2016)(2) 37. Metabolites are organic compunds constantly utilzed in various metabolic activities in the cells (HSE-March-2016)(2) a)What are the two types of metablites in the 42. Analyze the graph showing the activity of cells? an enzyme, influenced by temperature b)Give an example for each type of (HSE march-2015)(2) metabolites? 38. Enzymes are biocatalyst which regulate various biochemical reaction Illustrate the following reaction (HSE-March-2016)(2) 39. Compelete the following sequence with approprite words a)What is meant by optimum temperature? (HSE September-2015)(1) b)why does enzyme activity declines at too Amino acids:………(a)…….bond:protein low and at too high temperature? …(b)………: glycosidic bond : polysacharide 5. a. Why are proteins heteropolymers? 40. Based on the graph given below, explain b.Identify the proteins from the given list of the effect of concentration of substrate iomacromolecule and write its functions on enzyme activity (Cellulose,starch,antibody, inulin) (HSE September-2015)(2) c.Identify the type of protein structure of a and b (HSE August-2014)(3) 6. Symbolic presntation of a functional enzyme 41. Identify the protein structures, (a) and (B) is given below (HSE August-2014)(3) from the following figure (HSE March-2015)(1) NAVAS CHEEMADAN/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS-AREEKODE a.Write one difference between cofactor and apoenzyme? b.name the different types of cofactor c.what is the cofactor for the enzyme , carboxypeptidase 7. Name the chemical bond formed between the following (HSE March-2014)(1) a. Name the possible enzyme involved in this a. Amino acids in a protein moleucle reaction? b. Sugar and phosphate in a nucleic acid b. Where is its site of action 8. Distinguish between cofactor and coenzyme c. Mention any other factor which affects with an example for each? this enzyme (HSE March-2014)(2) d. Name another similar enzyme acting on 9. Oserve the graph and answer the following the same sustrate (HSE-SEPTEMBER-2013)(3) 12. Fill in the blanks (HSE September-2012)(1) Carbohydrate : sugar Proteins:………….. 13. Analyse the graph showing the activity of salivary amylase (HSE September-2012)(1) a.Find out the role of enzyme? b.Mention any two factors that influence the activity of an enzyme and state their influences? a.Which is the optimum temperature for 10. salivary amylase from the graph? b.Why the activity declines below the optimum value ? 14. Non protein constituent called cofactor are bound to the enzyme to make the enzyme (HSE MARCH-2013)(1.5) catalytically activity (HSE March-2011)(3) a. Identify this compound? a.Name the protein portion of the enzyme b. Name the bond produced when another b.What happens to the catalytic activity when compound of the same category combine the cofactor is removed from the enzyme? with this? c.Mention any two kinds of cofactor with c. If a number of such molecule bonded examples? together , what will e the resultant molecule ? 11. Oserve the graph shoing the activity of an enzyme influenced by pH (HSE march-2013)(2) NAVAS CHEEMADAN/2024  Join Now: https://join.hsslive.in Downloaded from https://www.hsslive.in ® NAVAS CHEEMADAN SOHSS-AREEKODE 15. Observe the graph (HSE-March 2010) a.What is meant by ‘Vmax’ value? b.Why is ‘Vmax’ not exceeded by any further rise in the substrate concentration c.If a chemical substance closely resembling to that of a substrate is introduced into a reaction system, what will be the consequences? Sustantiate 16. Fill in the blanks coloumns with the correct terms/sentenc (HSE march-2009) (2) A B …………(1)………. Catalyse oxiod reduction between 2 sustrate Transferase …………(2)……….. Lyases Catalyse hydrolysis of ester, glycosidic bond ………(3)………. Catalyse inter conversion of opical isomers Ligase ………(4)………. NAVAS CHEEMADAN/2024