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Basics of Biochemistry

Basics of Biochemistry

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Basics of Biochemistry

· Enzymes discovered by Eduard Buchner – 1897.

· Protein natue of enzymes discovered by J. Sumner.

· ATP structure – Fiske and Subba Rao.

· Photo synthetic system and aerobic heterotropic system feed each other and called “Syntropy” (between Carbon & energy cycle).

· The exchange of O2 between photosynthetic system and hetero trophic system accompanies “Carbon cycle”.

· In living system ‘S’ is present mainly in the form of “Mercapto” groups in S – containing amino acids.

· Smooth E.R – Lipid synthesis.

· Plasmalemma – Responsible for the uptake and elimination of water maintains homeostasis.

· Cytosol: Site of glyconeogenesis; hydrolysis of fats to glycerol and fatty acids. Cellwall – Shape and rigidity.

· Endomembrane system: Membrane bound enzymes.

· Origin of cellular energy – Solar energy.

· A typical example of double helix – DNA and Amylase.

Triple helix – Collagen.

Single helix – RNA

· In animals nitrogen is not stored as ammonia; it is excreted as urine.

· All the biosynthetic reactions commence with one (or) another of a small group of molecules called “Key precursor metabolites” numbering of 12 – 75 building blocks.

· Assymmetric carbon atom “Chiral” in nature.

· Free energy  G =  H –  TS.
H = molar heat energy (or) enthalpy
T = Temperature; S = Entropy.

· If  G = -Ve exergonic;  G = +Ve – endergonic
 G =  G0 + RTln Keq.
 G = Standard free energy.
R = Gas constant = 8.31 J/mol/K.
T = Absolute Temperature
Ln = Natural logarithem
Keq = equilibrium constant.

· The tendency of any particular atom ion (or) molecule to loose one.
Electron – Red – OX potential.

· An example of active transport is sulphate uptake by plant roots from the soil.

· The uptake of glucose by erythrocytes is passive uptake.

· PGA is transported as DHAP across the chloroplast membrane.

· Hydrophilic molecules move across the membrane as “Hydrophobic tail”

· In animals sugars transport as ‘glucose’.
Plants – Sucrose
Insects – Trehalase.

· Storage – animals – glycogen; Plants – Starch.

· High energy compounds are those which release energy after hydelysis (or) phosphate bond energy compounds.

· Non – phosphory lated high energy compounds. – Acetyl COA – Thiolester.

· “ketoenol toutomerism” cause high energy in “Enolphosphates”.

· Type of bond in ATP, ADP – pyrophosphate.
Acetal COA – Thiol ester
Glucose 6 P – 1P – Phosphate ester.
1, 3 diphosphoglycerate – Acyl phosphate.

· Phosphocreatine and phosphor argentine” serve as storage reservoir of chemical energy in muscle. Hydroxyl apetite basic material in bone.

· At C4 – right side OH Glucose; Left side OH galactose.
C2 – right side OH Glucose; Left side OH mannase
C5 – right side OH R – sugar; Left side OH – S – Sugar

· Heteropoly saccharide – heparin – Small molecular weight polysaccharide. Large molecular weight – Hyaluronic acid.

· 5 ring structure – furan; 6 ring – Pyran.

· “Hemiketals” are formed if the sugar contains a “Ketone group” in place of aldehyde.

· “Chair” form is more stable than the boat form.

· When monosaccharides react with concentration acid like H2SO4 “furfural” (or) its derivaties are formed.

· When glucose oxidize with bromine water + KMnO4 it give gluconic acid with strong oxidizing agent like concentration HNO3 it gives “glucuronic acid”.

· Galactose give – Mucid acid.


· Glucose =_____________Fractose and Mannose.
                    Through “Enediol”

· Change in specific rotation is called – Muta rotation.
a and b glucose in the proportion of 33% and 66%.

· Maltose – a 1- 4 linkage – in germinated cereals – 2 glucose molecules.

Isomaltose – a -1-6 linkage; Lactose – b, a (1-4) linkage.

Sucrose – ab (1-2) Cellobiose -b, 1-4 linkage.

· Insulin is found in the roots of “Dahlia”.

· Main construction of supporting tissue – Cellulose.

· Skeleton of insects – Chitin, It is a polymer of N-acetyl glucose, 2-amine, b – 1-4 linkage.

· Protons which take up are located towards “Stroma”; Which release are located towards “laminar” side.

· Most abundant enzyme in nature – RUBISCO – RUBP carboxylase.

· Cereal hust – Hemicellulase.

· “Heparin” is the powerful inhibitor of blood clotting.

· Summer crystallized the enzyme “Urease” from Jack bean meal.

· Many reactions which are energetically favourable do not always proceed rapidly due to energy barrier.

· Iso enzymes – These are the multiple molecular forms of an enzyme and may differ in physical and chemical properties.

· Glycolytic enzymes of the Cytosol are also organized as one unit – “Metaboli”.

· Allosteric refers to another space.

· Michaelis – Menten’s equation

· Much more accurate determination of Vmax and valuable information of enzyme inhibitor – “Eadie – Hof stee plat”.

· Competative inhibitor increases the apparent Km for the substrate without effect on Vmax.

· Inhibition of succinic dehydrogonase by Malonic acid which is a structural analogue of ‘Succinic acid’ example of competitive inhibitor.

· Non-competative inhibitor reduces the Vmax.

· Enzyme activity double for every 100C raise.

· Enzyme activity unit S.I. – Katal.

Enzyme classification:-

· 1st class – II & III type of reaction IV – individual number of enzyme.

· Non-hydrolytic removal of a group enzyme – lyases.

· Formation of C-C; C-O; C-N; C-S bonds – ligases.

· Clarifying agent – Papain.

· Enzyme = Protein (Apoenzyme) + Non-Protein (Co-enzyme).

· Vitamins are structural components of Co-enzyme.

· Co-enzyme – A – Panthothenic acid (Vitamin); Biocytin – Biotin.

· Flavin nucteotides – Riboflavin (B2); TPP – Thiamine (B1).

· Co-enzyme B12 – Cyanocobalamine (B12); (Thaimine pyrophosphate B1)

· Pyridine nucleotide – Nicotinic acid.

· “Avidin” a protein from egg white binds Biotin.

· Cobalamine occurs only in animals.

Vitamin Function

b – Carotene (Provit of Vitamin A) Vision

Chele colciferol (Provit – Vitamin D) Binding of “Ca”.

Tocopherols (Provit – E) Antioxidant.

Phylloquinone (Vitamin – K) Blood clotting.

· The amins acids reacts directly with a prosthetic group to from “Schiff’s” base.

· Ascorbic acid utilized mostly in “Hydroxylation reactions”.

· Non – protein amino acids – L.a amino acids.

· Biocytin is the prosthetic group of “Carboxylating enzymes”.

· “Ferridoxin” is the electron donor in NH3 formation.

· 24 molecules of ATP are required for one molecule of nitrogen fixed.

· Nitrogen fixing gone – “nif gene”.

· Water is ultimate source of electrons in Nitrate reduction.

· “Sirahaem” an iron porphyrin which is embedded in the enzyme protein is involved in electron transfer.

· ‘S’ containing A.A – Cystine; Cystine, methgonine.

· Succinic acid on transamination gives Aspartic acid, Phenyl alanine,

· Aromatic A.A. – Phenyl alanine.

· Hetero cyclic A.A. – Tryptophan, Histidine.

· Tryptophan contain an Imidole ring and Histidine contain Imidazole ring.

· Imino acids – Proline; Hydroxy proline.

· Dicarboxylic A.A.- Aspartic acid; glutamic acid.

· Amino acid action with benzaldehyde produces “Schiff’s base”.

· “Ninhydrin” is a powerful oxidizing agent it causes oxidative decorboxylation.

· The pH at which the AA has a net charges of zero is called “Iso electric point”.

· At this pH the AA has the least water solubility.

· At this pH the AA acquires a special from called “Zwitter ion” (or) “Inner salt form”.

· A molecule than cannot superimposed on its mirror image is called “Chiral molecule”.

· The aromatic amino acids are formed in “Shikimate pathway”.

· The biological activity of protein depend on the maintenance of “folded structure”.

· Secondary structure of proteins in the form of a – Helix and b – pleated.

· Contractice protein – Myosin, Transport protein – Haemoglobin.

Structural protein – Collages, Hormones – Insulin.

Toxin – Ricin, Protective proteins – Antiboides.

Enzyme – Hexakinase.

· Solubility of proteins is increased by addition of salts like NaCl is salting in.

· There is tendency of denaturated proteins to come together and form a large precipitation, which comes out of the solution and this is called “Coagulation”. Eg: blood cloting.


· Lipids are stored in animals in ‘adipose tissues’.

· Complex lipids contain fatty acids; simple lipids do not contain fatty acids.

· Fatty acids are the fundamental building blocks of stored fats. Many structural units are straight chain “aliphatic monocarboxylic acid”.

· In plants triacyl glycerols are stored in the oil bodies as “Spherosomes” of seeds. In animals fats are stored in the “Adipose tissue”.

· Deficiency of essential fatty acids cause disease called “phrynoderma”.

· All double bonds are “Cistype”.

· The alcohol of acyl lipids is “Sphingosine” (or) its derivaties.

· Cutin and suberin (Waxes) are the polymers of “Hydroxy fatty acids”.

· Major lipids of gram +ve bacteria are phosphotidyl glycerol and ‘Phosphotidyl ethanolamine”.

· Starting material for fatty acid synthesis – Acetyl COA.

· Fatty acid synthesis is in “Cytosol” in animals and in “Plastids” in plants.

· All the enzymes employed in the synthesis of “triacyl glycerol” are present in E.R.

· “Phosphotidic acid” is the precursor for all acyl glucerol.

· Any phenols are formed from the amino acid “Phenyl alanine”.

· Colourfest anthocyanins of fruits – “Flavanoids”.

· Tannins are astringent phenols.

· Toxic substance “Bona” is present in the Lankapappu (or) Kesari pappu

Toxic effect of Bona – Lathyrus.

· Catabolic path ways are generally regulated by “Feed back inhibition”.

· In animals b oxidation occurs in Mitochondria and in plants is glyoxysomes.


· The monomer composition of the protein polymer constitutes the primary structure.

· In the b – pleated sheet the H-bonding is perpendicular to the axis of the chain.

· Sickle cell anaemia is due to the substitution of glutamic acid in the b- chain of haemoglobin by – Valine.

· Number of double bonds in steric acid – O; oleic acid -1; Linoleic -2, Linolenic acid -3.

· The ‘N’ base in Lecithin is – Choline.

· The co enzyme pyriodoxal phosphate is involved during catabolism of amino acids and for transamination.

· The source of protein nitrogen in ruminants is urea.

· Type of bond in triacyl glycerol – labile bond.

· The major conponents of the total energy of system which can do work under isothermal condition is known as “Enthalpy”.

· The major components of cutin and suberin are the products of the omega oxidation.

· The chemical substance involved in the transmission of nerve impulses is “Acetyl choline”.

· The metabolism of foreign compounds – Xenobiotic metabolism.

· In the fatty acid biosynthesis plants add further double bonds between the exixting double bond and the methyl end in animals Hydroxyl group.

· Isoprenoids, the polymers of C-5 units are synthesized by Mevolonate pathway.

· Chemical which interfere with chlorophyll formation are used as Laser herbicides.

· AA’s are joined by a peptide bond with the elimination of water molecule.

· The reactions which do not proceed of their own and require an external source of energy are called “Coupled reactions”.

· Non-reducing sugar – Sucrose.

· The double bonds in fatty acids are separated by Methylene group.

· The building block of terpene is IPP.

· A typical example of non-nucleic acid caffeine.

· Tryptophan synthetase – Gibberellin.

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