AKTUBiochemistry BP203 TNotes

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AKTUBiochemistry [BP203T] Notes
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DOI: 10.13140/RG.2.2.22051.20004
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Dr. Hardesh K. Maurya, Biochemistry (BP203T)-2020
AKTU BIOCHEMISTRY [BP203T] COMPLETE NOTE
[As per AKTU syllabus]
Unit I
Biomolecules: Introduction, classification, chemical nature and biological role of carbohydrate,
lipids, nucleic acids, amino acids and proteins.
Bioenergetics: Concept of free energy, endergonic and exergonic reaction, Relationship between free energy,
enthalpy and entropy; Redox potential. Energy rich compounds; classification; biological significances of ATP
and cyclic AMP.
Unit II
Carbohydrate metabolism: Glycolysis- Pathway, energetics and significance. Citric acid cycle- Pathway,
energetics and significance. HMP shunt and its significance; Glucose-6-Phosphate dehydrogenase
(G6PD) deficiency. Glycogen metabolism Pathways and glycogen storage diseases (GSD) Gluconeogenesis
Pathway and its significance. Hormonal regulation of blood glucose level and Diabetes mellitus.
Biological oxidation: Electron transport chain (ETC) and its mechanism. Oxidative phosphorylation & its
mechanism and substrate level phosphorylation. Inhibitors ETC and oxidative phosphorylation/Uncouplers.
Unit III
Lipid metabolism: β-Oxidation of saturated fatty acid (Palmitic acid). Formation and utilization of ketone
bodies; ketoacidosis. De novo synthesis of fatty acids (Palmitic acid). Biological significance of cholesterol
and conversion of cholesterol into bile acids, steroid hormone and vitamin D. Disorder of lipid metabolism:
Hypercholesterolemia, atherosclerosis, fatty liver and obesity.
Amino acid metabolism: General reactions of amino acid metabolism: Transamination, deamination
& decarboxylation, urea cycle and its disorders. Catabolism of phenylalanine and tyrosine and their metabolic
disorders (Phenyketonuria, Albinism, alkeptonuria, tyrosinemia). Synthesis and significance of biological
substances; 5-HT, melatonin, dopamine, noradrenaline, adrenaline. Catabolism of heme; hyperbilirubinemia
and jaundice.
Unit IV
Nucleic acid metabolism and genetic information transfer: Biosynthesis of purine and pyrimidine
nucleotides. Catabolism of purine nucleotides and Hyperuricemia and Gout disease. Organization of
mammalian genome. Structure of DNA and RNA and their functions DNA replication (semi conservative
model) Transcription or RNA synthesis. Genetic code, Translation or Protein synthesis and inhibitors.
Unit V
Enzymes Introduction, properties, nomenclature and IUB classification of enzymes. Enzyme kinetics
(Michaelis plot, LineWeaver Burke plot) Enzyme inhibitors with examples. Regulation of enzymes: enzyme
induction and repression, allosteric enzymes regulation. Therapeutic and diagnostic applications of enzymes
and isoenzymes. Coenzymes –Structure and biochemical functions.
Disclaimer : These note is an only collection from various sources available on google and books for concise study purpose . The note is not revised, if any
confusion then consults a reference source for recheck.
1
BIOCHEMISTRY (BP 203 T)
Unit I [YouTube lecture link: https://www.youtube.com/watch?v=fDS_qJBMPVM&list=PLVLZCIcT1Dow4XtHW-wLdOdKfMvUjZTRb ]

Biomolecules: Introduction, classification, chemical nature and biological role of carbohydrate,
lipids, nucleic acids, amino acids and proteins.
Bioenergetics: Concept of free energy, endergonic and exergonic reaction, Relationship between free energy,
enthalpy and entropy; Redox potential. Energy rich compounds; classification; biological significances of ATP
and cyclic AMP.
BIOCHEMISTRY: Biochemistry, sometimes called biological chemistry, is the study of chemical processes within and
relating to living organisms. Biochemical processes give rise to the complexity of life.
Biomolecules
Introduction: Biomolecules include large macromolecules (or polyanions) such as proteins, carbohydrates, lipids and
nucleic acids, as well as small molecules such as primary metabolites, secondary metabolites, and natural products. A
more general name for this class of material is biological materials.
Classification: A diverse range of bimolecular are exist, In

biochemistry, the major class of biomolecules are carbohydrate,
proteins, lipids, nucleic acids, vitamins and harmones etc.
Biochemical role of carbohydrates:
1. Carbohydrates are important constituents of the cell structure of glycolipid, glycoproteins, heparin, cellulose starch etc.
2. Carbohydrates serve as an important source as well as a store of energy.
3. Carbohydrates are important starting material for many organic compounds like amino acids, nucleic and lipids.
4. Carbohydrates are the first storage form of energy, in the form of glycogen, to compensate for immediate energy
demands of body.
5. Carbohydrates are an important raw material for the production of products like glucose, maltose, enzymes, alcohols,
acids.
Chemical nature of carbohydrate:
a) Chemical nature: A carbohydrate is a biomolecule consisting of carbon (C), hydrogen (H) and oxygen (O) atoms,
usually with a hydrogen–oxygen atom ratio of 2:1 (as in water) and thus with the empirical
formula Cm(H2O)n (where m may be different from n).
Carbohydrates are divided into four major groups
i) Monosaccharides:
 Aldoses: Aldose contain aldehyde as one of their functional groups e.g. glucose, galactose.
 Ketoses: Ketoses contain ketone as one of their functional groups e.g. fructose, ribulose.
 Classification based on the number of carbon atoms: 1. Triose (3C, glyceraldehyde); 2. Tetrose (4C, Erythrose),
Pentose (5C, Xylose), Hexose (6C, Glucose, Fructose), Heptose (7C, Glucoheptose).
2
 Stereoisomerism: Carbohydrates contain 2n isomers (Where n=asymmetric carbon atoms).

 D and L isomerism: Spatial position of second last position of hydroxyl group decides D (right side) and L (left
side) configuration of carbohydrates as shown in example.
 Epimers: an epimer is a stereoisomer that differs in configuration at any single stereogenic center. E.g Glucose
and mannose are epimers at C2 while glucose and galactose are epimers at C4.
 Pyranose and furanose ring structures: Furanose is the five membered ring with the 1-4 carbons serving as the
ether bonds. Pyranose is the six membered ring with the 1-5 carbons serving as the ether bonds.
 Anomers: Anomers are cyclic monosaccharides or glycosides that are epimers, differing from each other in the
configuration of C-1 if they are aldoses or in the configuration at C-2 if they are ketoses. The epimeric carbon
in anomers are known as anomeric carbon or anomeric center.
 Mutarotation: Inter conversion of of α and β anomers of glucose in solution along with the change in their
optical activity are called mutarotation.
 Reaction of glucose:
3
 Osazone formation: Osazones are a class of carbohydrate derivatives formed when sugars are reacted with excess
of phenylhydrazine.
ii) Disaccharides:
 A disaccharide (also called a double sugar or bivose) is the sugar formed when two monosaccharides (simple
sugars) are joined by glycosidic linkage.
 Like monosaccharides, disaccharides are soluble in water.
 Three common examples are sucrose (in cane sugar), lactose (in milk), and maltose (in wheat) which have
common formula C12H22O11
 Reducing sugar: A reducing sugar is any sugar that is capable of acting as a reducing agent because it has a free
aldehyde group or a free ketone group. All monosaccharides are reducing sugars, along with some disaccharides
(lactose, maltose), oligosaccharides, and polysaccharides. Non-reducing sugars do not have an OH group
attached to the anomeric carbon so they cannot reduce other compounds eg. sucrose
 Sucrose is also called invert sugar because levo rotation of fructose (hydrolysis product) is greater then dextro
rotation of glucose after hydrolysis. The process is called inversion.
iii) Oligosaccharides:
 An oligosaccharide is a saccharide polymer containing a small number of monosaccharides. E. g. maltose,

panose.
4
 Oligosaccharides can have many functions including cell recognition and cell binding. For example, glycolipids
have an important role in the immune response.

iv) Polysaccharides: long chains of monosaccharides joined together are collectively called polysaccharides. It are two
type a) Homopolysaccharides: it contain only single type of monosaccharide chain: starch (amylase and amylopectin),
glycogen, dextran, cellulose.
b) Heteropolysaccharides: it contains one or more monosaccharide chains as their basic units: heparin, chitin.
5
LIPIDS
Introduction: A lipid is a type of organic molecule found in living things. It is oily or waxy and insoluble in water. Fats are
made from lipid molecules. Lipids are long chains of carbon and hydrogen molecules.
Chemical Nature: 1.The basic unit of lipids is triglyceride (glycerol and fatty acids). 2. Lipids have hydrophobic
hydrocarbon chains. 3. Soluble in organic solvents. 4.
Classification:
Fatty acids: Fatty acids are carboxylic acids with hydrocarbon side chains (4 to 36 carbon).
The fatty acids are broadly classified as follows:
6
a) Saturated fatty acids: it contains only single corbon bond chain and a carboxlic group:
Eg. Palmitic acid: CH3(CH2)14COOH
b) Unsaturated fatty acids: It also contains double bonds with single corbon bond and carboxlic group. Eg Oleic acid (cis
isomer): CH3CH=CH(CH2)7COOH.
Cyclic Fatty acids: containing ring in their structure Eg: Hydnocarpic acid.
Essential Fatty acids: These acids can not be synthesized by the body and therefore should be supplied in the diet. Eg
Linoleic acid, Linolenic acid, archidonic acid.
Fats: Fats are esters of fatty acids and glycerin also calles triacyl glycerols.
Simple Triacyl glycerol contains the same fatty acid in all three postions. Eg. Tripalmitin.
Mixed triacyl glycerol: they contain two or more different fatty acids.
Tests to determine purity of fat sample are acid value (rancidity measurement), Saponification number (fatty acid
measurement), Iodine number (unsaturation measurement) and Reichert-Meissl number (volatile fatty acid
measurement).
Phospholipids: They contain phosphoric acid in addition to alcohol, nitrogen base and fatty acids eg. Phosphotidic acid.
Glycolipids: It contains three different molecules, namely amino alcohol, fatty acid and a carbohydrate eg. Nervon
Lipoproteins: Molecular complexs of lipids and proteins are called as lipoproteins. The protein part is called apoprotein
the major functions are transport and delivery of the lipids.
Steriods: Compounds containing cyclopentanoperhydrophenanthrene nucleus in their structre are called as steroids. eg.
Cholesterol, aldosterol (Figure).
Biological role of lipids:
7
Nucleic acid
Chemical Nature: Nucleic acids are polymer of nucleotides Eg. DNA and RNA. Nucleic acids are made of nitrogenous
base, pentose sugar and a phosphate group and contain C, O, N and P elements. Biological role: DNA is the basic
molecule of heredity. While RNA molecules is responsible for protein synthesis
Amino acids
Chemical Nature: Amino acids are a group of organic compounds containing two functional groups carboxyl and
amino.
Zwitter ions: In the solution of pH (7.4), amino acids worked as dipolar ion (Zwitter ion). In the dipolar form of an
amino acid molecule, the amino group is ionized (-NH3+) and carboxyl group is dissociated (-COO-).
Classification of amino acids: Amino acids can be classified in different ways
a) Classification based on structure: i) Containing aliphatic side chains, eg. Glycine (Gly), Alanine (Ala), ii) Containing
hydroxyl group, eg serine (Ser). iii) Containing sulfur, eg cystine (Cys). iv) Acid amino acid, eg aspartic acid, v) Basic
amino acid, eg. Eg Lysine (Lys). vi) Aromatic amino acid eg. Phenyl alanine (Phe), vii) Imino acids, eg proline.
b) Classification based on Polarity: i) Non polar: They are also known as hydrophobic or water hating amino acids. Eg
alanine. ii) Polar amino acids:
they are also known as
hydrophilic amino acids or
water loving amino acids. Eg.
Glycine.
c) Classification based on the

nutritional requirement: i)
Essential amino acids:
Essential amino acids cannot
be made by the body. As a
result, they must come from
food. The 9 essential amino
acids are: histidine, isoleucine,
leucine, lysine, methionine,
phenylalanine, threonine,
tryptophan, and valine. ii) Non
essential amino acids: An
amino acid that can be made
by humans and so is not
essential to the human diet.
There are 11 nonessential
amino
acids: alanine, arginine, aspara
gine, aspartic
acid, cysteine, glutamic
acid, glutamine, glycine, prolin
8
e, serine, and tyrosine.
Proteins
Chemical Nature: 1. Proteins are heteropolymers of straight chain amino acids containing element C, H and N.
2. Proteins react with acids or enzymes to form peptides and free amino
acids (hydrolysis)
3. They provide structural support to cells.
4. Non-covalent bonds break with heat (denaturation).
5. Proteins have molecular weight ranging from 5000 to 3000000.
Classification:
Structure of Protein: Protein structures are classified into four special types as given below.
Biological role of protein: 1. Enzymes are proteins which catalyzed the rate of reactions. 2. They help in transport and
storage of materials like haemoglobin, myglobin, albumin etc. 3. Actin and myosin are contractile proteins in muscle. 4.
They act as protective like keratins. 5. They act as supportive like collagen. 6. They act as defensive function like
immunoglobulins. 7. Receptor proteins generate and transmit nerve impulses.
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Dr. Hardesh K. Maurya, Biochemistry (BP203T)
(BP203T)-2020
Bioenergetics
Bioenergetics: The study of the transformation of energy in living organisms.
Concepts of Free energy: It is defined as “the amount of energy available

le during the chemical reaction to do the cellular
work”
Endergonic and exergonic reaction:
Relationship between free energy, enthalpy and

entropy: Free energy is also known as Gibbs energy.
As per Gibbs free energy, the driving force of chemical
is of two components viz. driving to words stability and
drives towords disorder and is identified in Gibbs
equation:
Where G=G= change in Gibbs free energy (Net driving force), H= enthalpy (Driven
towards stability), S= entropy (Drive towards disorder. Reaction is spontaneous if G
G is less the zero (negative). At
equilibrium G is zero.
Enthalpy: It is a total heat content of a system.

system H=E+PV
Entropy:: It is defined as the measure of disorder or

uncertainty in a system. S=Q/t
Redox potential: It is also known as oxidation and

reduction potential. It is important biochemical reaction
which is used to characterize the free energy cost and
direction of reaction involving electron transfer. Redox potential is represented by Nernst equation.
Energy rich compounds: i) Biochemical compounds releasing free energy during hydrolysis can be classified into two
classes. I) High energy compound, II) Low energy compound ii) Molecules containing high
high-energy bonds ( ) are
themselves energy-rich compounds.. These energy-rich
compounds are the cell's currency; they can be used to
power energy-consuming
consuming biochemical reactions.
reactions If the energy of
hydrolysis of compound is more than 7.3 k cal/mole,
cal/mole it is referred
as the high energy compound and if the energy of

10
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hydrolysis of compound
mpound is less than 7.3 kcal/mol, then it is a low energy compound {ADP to AMP conversion (6.6
Cal/mol); Glucose-1-phosphote
phosphote (5.0 cal/mol) etc.
Biological significances of ATP:
The Adenosine triphosphate (ATP)) molecule is the

nucleotide known in biochemistry
mistry as the "molecular
currency" of intracellular energy transfer; that is, ATP is
able to store and transport chemical energy within
cells. ATP also plays an important role in the synthesis of
nucleic acids. ATP can be hydrolysed to ADP, Which can
be further
rther hydrolysed to AMP.
Coupling of reaction:: An unfavorable reaction

(endergonic) can be driven by coupling of reaction to
favorable reaction.eg.
Biological significances of cyclic AMP:

AMP
1) Cyclic adenosine monophosphate (cAMP) is a second

messenger that
hat is important in many biological processes. 2)
cAMP is derived from ATP and used for intracellular signal transduction in many different
organisms, transmission the cAMP dependent pathway. 3) In humans, cyclic AMP works by
activating cAMP-dependent protein ein kinase. Cyclic AMP binds to specific locations on the
regulatory units of the protein kinase, and causes dissociation between the regulatory and
catalytic subunits Thus it activates the catalytic units and enables them to phosphorylate
substrate proteins. 4) It regulate T cell function. 5) It also enhancees the release ofinsulin.
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Unit II [YouTube lecture link: https://www.youtube.com/watch?v=fDS_qJBMPVM&list=PLVLZCIcT1Dow4XtHW

https://www.youtube.com/watch?v=fDS_qJBMPVM&list=PLVLZCIcT1Dow4XtHW-wLdOdKfMvUjZTRb ]
Carbohydrate metabolism: Glycolysis-
Glycolysis Pathway, energetics and significance. Citric acid cycle
cycle- Pathway,
energetics and significance. HMP shunt and its significance; Glucose-6-Phosphate
Glucose Phosphate dehydrogenase
(G6PD) deficiency. Glycogen metabolism Pathways and glycogen storage diseases (GSD) Gluconeogenesis
Pathway and its significance. Hormonal regulation of blood glucose level and Diabetes mellitus.
Biological oxidation: Electron transport chain (ETC) and its mechanism. Oxidative
ative phosphorylation & its
mechanism and substrate level phosphorylation. Inhibitors ETC and oxidative phosphorylation/Uncouplers.
Carbohydrate metabolism: It is a biochemical and metabolic process.

process. This is the cumulative step
step-wise
process by which breakdownown (catabolism), Formation (anabolism) and inter-conversion
inter conversion of carbohydrate takes
place in various living organisms.
The major pathways of carbohydrate metabolism are Glycolysis, Citric acid cycle, HMP shunt, and
Gluconeogenesis.
Glycolysis- Pathway [ Embden-Meyerhof

Meyerhof-Parnas (EMP) pathway]:
1) Glycolysis is a series of reactions that extract energy from glucose by splitting (in ten steps) it into two
three-carbon
carbon molecules called pyruvates.
2) Glycolysis (Aerobic,, in the presence of oxygen)

oxygen has ten steps.. Glycolysis takes place in the cyto
cytoplasm of
the cell, and it can be broken down into two main phases.
a) The energy-requiring phase: Glucose molecule break in two molecule GLAP ((Glyceraldehyde -3-
phosphate) and DHAP (Dihydroxy acetone phosphate) and consume
consume two ATP molecule.
b) Energy-releasing phase. In this phase, each three-carbon

three carbon sugar is converted into another three
three-carbon
molecule, pyruvate, through a series of reactions. In these reactions, four ATP and two NADH are overall
produced.
Overall, glycolysis converts one six-carbon

carbon molecule of glucose into two three-carbon
three carbon molecules of pyruvate.
The net products of this process are two molecules of pyruate, two molecules of ATP (4ATP-2ATP), 2
molecule of NADH (= 6 ATP molecule) and 2 molecule of water.
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Where: NAD= Nicotinamide adenine dinucleotide (coenzyme); NADH= Nicotinamide adenine

dinucleotide hydride (Reduced form).
Glycolysis- Pathway (Aerobic)
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Glycolysis- Pathway (Anaerobic): Anaerobic glycolysis is the transformation of glucose to lactate when
limited amounts of oxygen (O2) are available and produced overall 2 ATP (4-2).
Overall energy of glycolysis:
a)Total energetics in aerobic pathway= - 1 ATP (Step 1) - 1ATP (Step 3) + 6 ATP (by 2NAD, step 6) + 2ATP
(step 7) + 2 ATP (step 10) = 8 ATPs.
b) a)Total energetics in anaerobic pathway=

- 1 ATP (Step 1) - 1ATP (Step 3) + 6 ATP
(by 2NAD, step 6) + 2ATP (step 7) + 2 ATP
(step 10) - 6 ATP (by 2NAD, last step PA to
LA) = 2 ATPs.
Significance of the glycolysis pathway:

pathway
Citric acid cycle [Krebs cycle,, TCA

(Tricarboxlic acid) cycle]:
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1. After Glycolysis, Pyruvate inter in mitochondria.

mitochondria
2. Pyruate decarboxylated and converted in Acetyl CoA. CoA This step catalyzed by pyruvate dehydrogenase
enzyme. This reaction is a link between glycolysis and TCA (Tricarboxlic acid) cycle.
3. TCA cycle occurs inside the mitochondria and contains 8 steps in cycle as shown below.
(Where: GTP= Guanine triphosphate;; GDP= Guanine Diphosphate; FAD = Flavin adenine dinucleotide
dinucleotide;
FADH2= Flavin adenine dinucleotide dihydride; NAD= Nicotinamide adenine dinucleotide
dinucleotide; NADH=
Nicotinamide adenine dinucleotide hydride)
hydride
Enzymes in TCA cycle

4. Step I: Citrate synthase
5. Step II: Citrate aconitase
6. Step III: Isocitrate dehydrogenase
7. Step IV: α-Ketoglutrate dehydrogenase
hydrogenase
8. Step V: Succinyl CoA synthase
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9. Step VI: Succinate dehydrogenase

10 Step VII: Fumerase
11. Step VIII: Malate dehydrogenase
12. Energetics of TCA Cycle=
3ATP (1 NADH, Step 3) + 3ATP (1 NADH, Step 4) + 1ATP (1 GTP, Step 5) + 2ATP (1 FADH2, Step 6) +
3ATP (1 NADH, Step 7) = 12 ATP generated.
13. Overall TCA cycle produce 2CO2 molecule and generated 12 ATP.
14. Hence, 2 Acetyl Co A produce total energy= 12 x 2= 24.

24
Energetic in complete oxidation of a glucose molecule:
1. Aerobic glycolysis = 8 ATP
2. Oxidation of 2 molecule of Pyruvate = 6 ATP
3. TCA cycle = 24 ATP
NET energetic = 38 ATP
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HMP shunt [Hexose

Hexose monophosphate
monophosphate or Pentose phosphate pathway (PPP) or Phosphogluconate
oxidation pathway shunt] :-
1. This is an alternative
ternative pathway for glucose metabolism.
metabolism
2. This pathway occurs in cytoplasm of liver, adipose tissues adrenal cortex, thyroid, testis, etc.
3. This pathway is more anabolic in nature.
4. This process is known as shunt because the starting material is being

being diverted in some other pathway from
main step.
4. It has two distinct steps: a) Oxidative stage, b) Non oxidative stage.
Oxidative Stage
(Ribulose-5-phosphate-3-epimerase,
epimerase, Ribulose
Ribulose-5-phosphate-
isomerase, Transketolase, Transaldolase)
5. The Core reaction of HMP shunt is
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Assignment: Write the

difference between glycolysis
and HMP shunt
Glucose-6-Phosphate dehydrogenase (G6PD) deficiency:
1) G6PD is an enzyme which converts Glucose-6-phosphate

Glucose into 6-
phosphogluconate and produce NADPH as byproduct (HMP shunt).
2) NADPH is utilized for the formation of RBCs.
3) Due to deficiency
eficiency of G6PD, NADPH production decrease and RBCs
are not formed as per requirement. Thus G6PD is most essential for formation of RBC.
4) This type of deficiency is cause jaundice in new born baby and hemolytic anemia.
5) G6PD deficiency is inherited as an X-linked

X disorder.
Glycogen metabolism Pathways:
1. Glycogen is a multibranched polysaccharide of

glucose.
2Glycogen
Glycogen metabolism has two pathways glycogenesis
and glycogenolysis
Glycogenesis:
1. Glucose is stored as glycogen in the liver and muscle cells in the biochemical process called as glycogenesis.
2. It takes place in the Cytosol (Liver, Muscles) and requires ATP and UTP (Uridine-5'
5'-triphosphate).
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3. Glycogenesis is activated during rest periods Lactic acid

cycle (Cori cycle) in the liver or high glucose level in blood or
in muscle.
4.Cori cycle refers to the metabolic pathway in which lactate

produced by anaerobic glycolysis in the muscles moves to the
liver
ver and is converted to glucose, which then returns to the
muscles.
Glycogenolysis:
1. Glycogen is broken down to

glucose whenever body needs
internal supply of glucose in the
biochemical process called as
glycogenolysis.
2. Glycogenolysis is a catabolic
process which occurs in the liver
and muscle cells.
Glycogen storage diseases

(GSD): It is a metabolic
disorder caused by enzyme
deficiencies affecting
either glycogen synthesis,
glycogen breakdown or glycolysis (glucose breakdown), typically
typic in muscles and/or liver cells.
GSD has two classes of cause: genetic and acquired. Genetic GSD is caused by any inborn error of
metabolism (genetically defective enzymes) involved in these processes. Acquired GSD is caused
by intoxication with the alkaloid castanospermine.
castanospermine Ex.
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Type Symptom Defective enzyme Organ affected Glycogen

Von Gierke’s disease Enlarged
nlarged liver and Glucose-6-phosphate Liver and Kidney Increased
kidneys
Pomp’s disease Enlarged liver and Α-1,4-glucosidase All organs Massive
hearts
Cori’s disease Enlarged liver, Amylo-1,6- Liver and Muscle Increased
swollen abdomen glucosidase
Anderson’s disease Enlarged liver Branching enzyme Liver Long outer branching
Mc Ardle’s disease Muscle cramps Phosphorylase Muscle Medium increased
Her’s disease Enlarged liver Phosphorylase Liver Increased
Tarui’s disease Muscle cramps Phosphofructokinase Muscle Increased
Gluconeogenesis Pathway:
1. It is a metabolic pathway in which synthesis of glucose molecule occurs from pyruvate, other non
non-
carbohydrate precursors and even in non photosynthetic organisms.
2. It occurs in liver and kidney.
3. It started by low glucose levels like starvation, acidosis, glucagon and glucocorticoids.
4. It is a reversible process off glycolysis, TCA and other cycles.
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Hormonal regulation of blood glucose level and Diabetes mellitus:

mellitus
Diabetes: Diabetes disease is associated with regulation of blood glucose. There are two main forms of
diabetes
a) Type I diabetes [Juvenile-onset

onset or insulin-dependent
i diabetes mellitus (IDDM)]: Type I diabetes people
cannot produce insulin and need insulin injection.
b) Type II diabetes [adult onset or non insulin-dependent

insulin diabetes mellitus (NIDDM)]
(NIDDM)]: It occurs when cells
become resistant to the effect of insulin over a long period of time. Three are two major forms of type II
diabete
i) Late onset associated with obesity: Which depend on obesity.
ii) Late onset not associated with obesity: Which does not depend on obesity.
Various terms of diabetes aree as follow
Pre-diabetes:: a stage between normal and diabetes.
Impaired fasting glucose (IFG): Normal fasting plasma

plasm glucose range= 100-125
125 mg/dl
Impaired glucose tolerance (IGT):: Slightly higher than normal glucose level (140-199
199 mg/dl after 2 h after
intake 75 grams of glucose).
Oral Glucose tolerance test (OGIT): a test of glucose level after 2 h after intake of 75 grams of glucose.
Glycated haemoglobin: Glucose derived products of normal adult haemoglobin (Hb) is known as glycated
haemoglobin eg Hb1c used to study glucose level. Sometime fructosamine can also use instead of Hb1c.
21
Microalbuminuria: Increase of albumin exreaction in diabetic patients more than normal range 2.5-3.0 mg/dl.
Plasm C-peptide: this peptide is obtained by the cleaved of pre-pro-insulin.
Metabolic changes in diabetes:
1. Hyperglycemia: Hyperglycemia refers to high levels of sugar, or glucose, in the blood. It occurs when the
body does not produce or use enough insulin, which is a hormone that absorbs glucose into cells for use as
energy.
2. Ketoacidosis: In diabetes, presence of excess ketone bodies in the blood is observed.
3. Hypertriglyceridemia: In diabetes, increased levels of triglycerides are observed.
4. Hypercholesterolemia: also called high cholesterol, is the presence of high levels of cholesterol in the
blood.
5. Hypoglycemia: a condition when blood glucose levels fall below 45 mg/dl of a person.
6. Glycosuria: Presence of glucose in urine is termed as glycosuria.
Causes of diabetes:
1. Main factors are Heredity and Obesity
2. Various other factors are age, faculty immune system, physical trauma, drugs, pregnancy and viruses.
Regulation of blood glucose level: 1.The pancreas has a major role in controlling blood glucose level.
2. The islets of langerhans (in pancreas) monitor the concentration of blood glucose. During sudden change in
blood glucose level, either α-cells or β-cells are activated to release hormones (e. g. insulin) to respond and
return the blood glucose concentration in normal level.
3. Insulin is a peptide hormone produced in β-cells of islets of langerhans. It regulates the metabolism of
carbohydrates and fats by enhancing the formation of glycogen, proteins, lipids and amino acids from excess
blood glucose.
4. Glucagon is a hormone that secrets from α-cells of islets of langerhans. It shows activity opposite to that of
insulin.
5. Apart from pancreas, adrenal glands (eg Cortisol& Epinephrine: increase glucose), pituitary gland (eg.
ACTH & GH: increase glucose) and thyroid glands (thyroxine: increase glucose) also release hormones that
regulate blood level.
Biological oxidation: Biological oxidation is an energy-producing reaction in living cells, and it is coupled
with a reduction reaction.
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mechanism 1.The electronn transport chain is a series

Electron transport chain (ETC) and its mechanism:
of electron transporters embedded in the inner mitochondrial membrane that shuttles electrons from NADH
and FADH2 to molecular oxygen. In the process, protons are pumped from the mitochondrial ma matrix to the
intermembrane space and oxygen is reduced to form water.
water
2. ETC can be represented as follow
Where: 1. AH2: Reduced substrate; A: Oxidized substrate
2. NAD: Nicotinamide‐adenine
adenine dinucleotide (oxidized); NADH2 (nicotinamide
nicotinamide‐adenine dinucleotide
(reduced),
3. FMN: Flavin mononucleotide (oxidized);

(oxidized) FMNH2: Flavin mononucleotide (reduced)
4. Co Q: Coenzyme Q (ubiquinone); Co Q H2: Coenzyme Q (reduced).
5. FAD: Flavin adenine dinucleotide, FADH2: Flavin adenine dinucleotide (reduced)
6. Cyt b: Cytochrome b; Fe3+ (reduced sulphide) Fe2+ (oxidized sulphide)
7. Cyt c1: Cytochrome c1.
8. Cyt c: Cytochrome c.
9. Cyt a: Cytochrome a.
10. Cyt a3: Cytochrome a3.
Final product in ETC: H2O,, ATP and released of free energy during electron passage on inner mitochondria
mitochondria.
Significance: Releasing
eleasing of free energy for various metabolism process of our body.
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Cytochromes are proteins containing heme as a cofactor. They are classified according tto the type of heme
and its mode of binding. Four varieties are recognized as cytochromes a, cytochromes b, cytochromes c and
cytochrome d.
Oxidative phosphorylation & its mechanism: 1. Oxidative phosphorylation is the process in which ATP is
formed as a result
sult of the transfer of electrons from NADH or FADH 2 to O 2 by a series of electron carriers.
2. This is associated
ciated with ETC cycle which occurs in mitochondria.
3. It is the major source of ATP in aerobic organisms.
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4. The chemiosmotic theory explainss the mechanism of oxidative phosphorylation.
• When electrons are transported along the components of the ETC, the accompanying protons are released.
• Part of the free energy harvested during the ETC is used to pump protons out of the mitochondrial mat
matrix.
• The resulting uneven distribution of protons generates a pH gradient and a charge gradient across the inner
mitochondrial membrane.
• The electrochemical potential energy generated by these gradients is called as Proton Motive Force.
• The return of protons to the mitochondrial matrix is coupled to ATP synthesis by phosp
phosphorylation.
1. Oxidative step: NADH + H+ + O2  NAD+ + H2O
2. Phosphorylation step:
step ADP +Pi  ATP
3. Reduction step:: ½ O2 + 2 H+ + 2e-  H2O
 Redox loop or proton transportt mechanism used to explain the pumping of proton.
Substrate level phosphorylation: 1. Substrate-level

Substrate phosphorylation is a metabolic reaction that results in the
formation of ATP or GTP by conversion of a higher energy substrate (whether phosphate group attached or
not) into lower energy product and a using some of the released chemical energy,, the Gibbs free energy, to
transfer a phosphoryl (PO3) group to ADP or GDP from another phosphorylated compound.
2. It occurs in both aerobic and anaerobic conditions.

condit
3. It occurs in the cytosol and mitochondria.
4. Energy is generated from a coupled reaction.
5. It occurred in glycolysis and krebs cycle
Inhibitors of ETC and Oxidative Phosphorylation:
Inhibitors of ETC: The inhibitors bind to one of the components

components of electron transport chain and block the
transport of electrons as the results ATP synthesis become stopped.
stopped The most important known inhibitors of
the ETC are Amytal, Rotenone, Antimycin A, CO, Sodium Azide, and Cyanides
horylation: Inhibitors of oxidative phosphorylation are

Inhibitors of Oxidative Phosphorylation
25
• Complex I: Rotenone
• Complex II: Carboxin
• Complex III: Antimycin A
• Complex IV: Cyanide, Azide, Carbon monoxide
• ATP synthase: Oligomycin
• ATP-ADP translocase: Atractyloside (a plant glycoside)
Uncouplers
• Uncouplers inhibit oxidative phosphorylation.
• They ‘uncouple’ the ETC from oxidative phosphorylation.
• The ETC remains intact and electrons are transferred to O 2 to generate H2O. However, uncouplers carry
protons across the mitochondrial membrane making it ‘leaky’ for H+. The pH and electrical gradient is not
generated and ATP is not synthesized.
• In the presence of an uncoupling agent, energy released via the ETC is converted into heat.
• This mechanism is used by hibernating animals to stay warm in the winter, since they don’t need ATP for
anabolic processes while they are resting.
• Examples of uncouplers: Natural: Thermogenin or uncoupling protein (UCP). Synthetic: 2,4,-dinitrophenol.
26
Unit III
Lipid metabolism: β-Oxidation of saturated fatty acid (Palmitic acid). Formation and utilization of ketone
bodies; ketoacidosis. De novo synthesis of fatty acids (Palmitic acid). Biological significance of cholesterol
and conversion of cholesterol into bile acids, steroid hormone and vitamin D. Disorder of lipid metabolism:
Amino acid metabolism: General reactions of amino acid metabolism: Transamination, deamination
& decarboxylation, urea cycle and its disorders. Catabolism of phenylalanine and tyrosine and their metabolic
disorders (Phenyketonuria, Albinism, alkeptonuria, tyrosinemia). Synthesis and significance of biological
substances; 5-HT, melatonin, dopamine, noradrenaline, adrenaline. Catabolism of heme; hyperbilirubinemia
and jaundice.
Lipid metabolism: Lipid metabolism is the synthesis and degradation of lipids in cells, involving the
breakdown or storage of fats for energy and the synthesis of structural and functional lipids, such as those
involved in the construction of cell membranes. In animals, these fats are obtained from food or are
synthesized by the liver.
Oxidation of saturated fatty acid: There are three types of fatty acid oxidation
namely alpha (α), beta, and omega (ω). The oxidation of fatty acids is studied first
by Knoop in 1905. Hence it is also known as Knopp oxidation theory. Alpha
oxidation occurs at alpha carbon of fatty acids (in microsomal fraction of brain).
Similarly, Beta oxidation occurs at Beta (β) carbon in mitochondria and omega
(ω) oxidation occurs in microsomal fraction of liver.
β-Oxidation of saturated fatty acid (Palmitic acid): beta-oxidation is the
catabolic process by which fatty acid (Palmitic acid) molecules are broken down
in the mitochondria to generate acetyl-CoA, which enters the citric acid cycle and
NADH and FADH2, which are co-enzymes used in the electron transport chain.
The C-16 fatty acid palmitic acid undergoes 5 steps through this oxidative sequence and loses two
carbones as acetyl-CoA in each step. At the end of seven steps, two products obtained fatty acyl-Co A (14C)
and acetyl-Co A (2C) (See flow chart at next page) and generate high energy (129 ATP)
Energetic of β-Oxidation of Palmitic acid:
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28
Formation and utilization of ketone bodies: 1. Ketones and ketoacids are alternative fuels for the body that
are made when glucose is in short supply.
2. They are made in mitochondria of the liver cell from the breakdown of fats.
3. Ketones are formed when there is not enough sugar or glucose to supply the body's fuel needs. This occurs
overnight, and during dieting or fasting.
4. Acetone, acetoacetate (true ketone bodies) and β-hydroxybutyrate are known ketone bodies. 5. The
production of ketone bodies is known as ketogenesis.
6. Insulin and glucose are regulating hormones of ketogenesis.
7. Beta- hydroxybutyrate and acetoacetate passes through membranes easily and hence they provide a source
of energy for brain.
Utilization: 1. Ketone bodies can be utilized as fuel in the heart, brain and muscle, but not in liver
2. Ketone bodies are transported from the liver to other tissues, where acetoacetate and β-hydroxybutyrate can
be reconverted to acetyl-CoA to produce reducing equivalents (NADH and FADH2), via the citric acid cycle.
29
Ketoacidosis: 1. The concentration of ketone bodies in blood should be 1mg/dl.
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2. If the concentration is increase than the

rate of utilization, the condition is known as
ketonemia.
3. In further stage,
tage, the ketone bodies are
excreated from the body through urine; this
condition is known as ketouria.
4. This two stages are together known as

ketosis.
5. When the ketosis is extreme and

uncontrolled, the stage is known as
ketoacidosis. It is a metabolic stage that
formed by the breakdown of stored fatty
acids and deamination of amnio acids.
6. The three common n causes of ketoacidosis

are alcohol (Alcohol ketoacidosis),
starvation (starvation ketoacidosis) and
diabetes (Diabetic ketoacidosis).
7. Symptoms:: extreme thirst, frequent

urination, dehydration, vomiting etc.
De novo synthesis of fatty acids (Palmitic

acid): 1. De novo synthesis refers to the
synthesis of complex molecules from simple
molecules.
2. It is a reverse process of beta-oxidation

oxidation
of fatty acids which occurs in cytoplasm of
cell in liver, kidney, adipose tissues etc.
3. In the synthesis of 16 C palmitate, only 2

C comes from acetyl Co A and 14 C comes
H !!!
from malonyl Co A.
4. ACP is represents acyl carrier proteins.
5. KSase is represents Beta-ketoacyl-ACP

ACP
synthase
6. The sequential reaction steps for de novo

synthesis of palmitic acid are given in Fig.
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Biological significance of cholesterol:
1. Cholesterol is waxy fatty substance (sterol) found in all cells of the

body.
2. The major sources of cholesterol include cheese, egg yolks, beef, pork,
fish etc.
2. It is essential to maintain both structural
tural integrity and fluidity of animal
cell membrane.
2. Cholesterol is a precursor for the synthesis of the steroid hormones, the bile acids, vitamin D, androgens and
estrogens.
3. It synthesized de novo in liver as well as in intestine etc.
Conversion acids: 1.The conversion of cholesterol into bile acids is formed by two
n of cholesterol into bile acids:
ways like classic pathway which occurs in microsomes in liver. Other alternative pathway for synthesis of bile
acids from cholesterol occurs in mitochondria.
2. Bile acids are biologically active molecules that promote absorption of dietary lipids in the intestine and
stimulate excretion of cholesterol.
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Conversion of cholesterol in steroid hormone: 1.Cholestrol is the major precursor for the for the
major steroids hormones.
2. The conversion of cholesterol to steroid hormones is known as steroidogenesis. These hormones are
produced in the adrenal cortex, testis, ovary and some peripheral tissues.
Conversion of cholesterol in vitamin D: Vitamin D is fat soluble lipids (secosteriod) and responsible for
increasing intestinal absorption of calcium, magnesium and phosphate. On exposure to sun light 7-
dehydrocholesterol is converted into cholecalciferol (Vit. D3) in the skin and finally converted into calcitriol
(See Figure at next page).
Disorder of lipid metabolism: Due to abnormalities in enzymes fatty acids so various disorder such as
Hypercholesterolemia: 1. It is the situation of high level of cholesterol present in the blood (> 200 mg/dl). 2.
It is also called high cholesterol. 3. It is a form of hyperlipidemia, high blood lipids, and hyperlipoproteinemia.
4. It has a high risk of coronary artery disease. 5. It is controlled by dietary intake of polyunsaturated fatty acid
that reduce the plasma cholesterol level. 6. Statin drugs used to reduce cholesterol synthesis.
33
Atherosclerosis: It is a disease in which

plaque builds up inside your arteries. Arteries
are blood vessels that carry oxygen-rich blood
to your heart and other parts of your body.
Plaque is made up of fat, cholesterol, calcium,
and other substances found in the blood.
Atherosclerosis often has no

symptoms until a plaque ruptures or the build-
up is severe enough to block blood flow.
A healthy diet and exercise can help.
Treatments include medication, procedures to
open blocked arteries and surgery.
Fatty liver:
It is the condition when the excessive fat deposit in the

liver and results deposition of toxic materials in the liver. This
condition is also known as hepatic steatosis. In this condition,
the weight of the liver increase about 10% than that of normal
weight and cause inflammation. Some common symptoms are
like poor appetite, weight loss, abdominal pain, fatigue
weakness etc. There are two type of fatty liver namely alcoholic
(due to drinking of heavy alcohol) and non-alcoholic (without
drinking alcohol).
Obesity: It is the medical condition in which excess body fat is accumulated (More than 20% excess fat
deposition in the body than normal body weight) in the body that causes an adverse effect on health. It is
defined by the body mass index (BMI). BMI is a simple index of weight for hight and used to know about
overweight and obesity. BMI= M (Mass)/H2 (height). 1. BMI: 35-40 Kg/m2 (sever obesity); 2. BMI: 45-50
(super obesity). The main causes of obesity are excess calorie food consumption. Obesity causes type II
diabetes, hypertension, high cholesterol etc.
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Amino acid metabolism
General reactions of amino acid metabolism:

metabol The breakdown method of proteins in amino acids is called
proteolysis which occurs in gastrointestinal tract. This amino acid further degraded by the methods such as
transamination, deamination and decarboxilation which occurs in the liver.
Transamination: It is the method through which α-amino

amino group loses from amino acid by degradation i.e.
transfer to an α-keto acid.. Eg. Alanine convertes in Pyruvate in the presence of enzame Alanine
aminotransferase
Alanine + α--ketoglutarate  Pyruvate + Gluta

Glutamate
Significance: 1. It is an exchange of amno nitrogen between the molecule without a net loss.
2. It is important for formation of non-essential

essential amino acids.
Deamination: 1. Deamination involves removal of amino group in the form of NH3.
2. Liberation off free ammonia from amino group of an amino acid coupled with oxidation takes place in
oxidative deamination. The reaction occurs in the liver and kidney. e.g the conversions of glutamate to α-
ketoglutarate occurs in the presence of enzymes glutamate dehydrogenase, e.g.
3. Non-oxidative deamination takes place by reduction, hydrolytic or intra molecular reactions.
Decarboxylation: It is the process by which carboxylic group

grou is removedd from the amino acid and biogenic
amines are formed.
Urea cycle and its disorders: The urea cycle is a biochemical

reaction by which highly toxic ammonia is converted into urea
and excreted from the body through urine. This cycle is also
known as ornithine cycle. The urea is absorbed first into the
blood stream then filtered by kidney and then excreted through
urine.. Various steps of urea cycle are shown in figure.
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Significance of urea cycle:: 1. Urea cycle is the first elucidated metabolic pathway.
2. The cycle is also known as Krebs-Henseleit

Henseleit urea cycle
3. Ornithin is the first member of the reaction and hence known as ornithin cycle.
4. Toxic ammonia is converted into non-toxic

non urea.
5. The excess nitrogen forms urea
6. It removes CO2 and NH3.
7. It recycles TCA cycle intermediate.
8. It recycles amino acids and keto acids.
9. Urea production takes place in liver, transported to kidney and excreted through urine.
Energetic of Urea cycle:: Urea cycle utilized overall 1,5 ATP.
Metabolic disorder of urea cycle:
Catabolism of phenylalanine and

tyrosine: 1. Phenylalanine is an
essential amino acid, however tyrosine
is non-essential. Both of them are
aromatic amino acids having similarity
in their structures. Phenylalanine is
converted in Tyrosine catalyzed by
enzyme phenylalanine hydroxylase.
37
2. The metabolism of phenylalanine and tyrosine is considered together.
3. During catabolism, phenylalanine and tyrosine are converted in fumerate (an intermediate of TCA cycle and
gluconeogenesis) and acetate (a ketone body from which fats can be synthesized).
4. Various step of metabolism of phenylalanine and tyrosine are as follow.
Metabolic disorders of phenylalanine and tyrosine (Phenyketonuria, Albinism, alkaptonuria,

tyrosinemia): Various common disorders are as follow
Phenyketonuria: Phenylketonuria (PKU) is an inborn error of metabolism that results in decreased metabolism of the
amino acid phenylalanine. Untreated, PKU can lead to intellectual disability,
seizures, behavioural problems, and mental disorders. It may also result in a
musty smell and lighter skin. Other names: Phenylalanine hydroxylase
deficiency.
Albinism: 1. Albinism is a congenital disorder characterized in humans by

the complete or partial absence of pigment in the skin, hair and eyes. 2. It is a
defect in one of several genes that produce or distribute melanine. 3. Due to
absence of tyrosinase (Cu containing) enzyme in the melanocyte cells. It is
also known as achromia.
38
Alkeptonuria: Alkaptonuria is a rare inherited disorder. It occurs when your body can't produce enough of an enzyme
called homogentisic dioxygenase (HGD). The gene defect makes the body unable to properly break down certain amino
acids (tyrosine and phenylalanine). As a result, a substance called homogentisic acid builds up in the skin and other body
tissues. Affected individuals may have dark urine or urine that turns black when exposed to air.
Tyrosinemia: Tyrosinemia is a genetic metabolic disorder that causes the body's inability to effectively break down the
amino acid tyrosine. The inability to breakdown the amino acid is caused by the deficiency of the fumarylacetoacetate
hydrolase (FAH) enzyme (Type I), tyrosine aminotransferase enzyme (Type II) and 4-hydroxyphenyl-pyruvate
dioxigenase enzyme (Type III) which required for the
metabolism of tyrosine. It leads to accumulation of toxic
materials in various tissues and finally kidney and liver are
destroyed.
Biosynthesis and significance of 5-HT:
1. Serotonin (5-HT) is an important chemical and

neurotransmitter in the human body.
2. It is produced in brain.
3. It is believed to help regulate mood and social behavior,

appetite and digestion, sleep and memory and function such as
vasoconstrictor (smooth construction of muscles).
Biosynthesis and significance of melatonin:
1. In humans, melatonin plays an

important role in the regulation
of sleep cycles (i.e., circadian
rhythm).
2. Melatonin is released by the

pineal gland in the brain during
the nighttime hours,
3. It induces physiological
changes that promote sleep, such
as decreased body temperature
and respiration rate.
39
Biosynthesis and significance of Dopamine:
1. Dopamine belongs to
catecholamines.
2. Epinephrine and
norepinephrine are
synthesized from
dopamine.
3. It plays significance
role in learning,goal
directed behavior,
regulation of hormones,
motor control etc.
4. It control flow of
information from other
areas of the brain
5. It plays role in
movement.
Biosynthesis and
significance of
noradrenaline,
adrenaline: 1.
Adrenaline
(epinephrine)
produced in adrenal
gland whereas
noradrenaline
(norepinephrine) is
secreted from certain
neurons of brain as well as adrenal gland.
2. Both are the example of catecholamines.
3. Noradrenaline is the main neurotransmitter of the sympathetic nerves in
the cardiovascular system.
4. Adrenaline is the main hormones secreted by the adrenal medulla.
5. Noradrenaline is used to increase and maintain blood pressure in acute
situations like cardic arrest etc.
6. Adrenaline is used to treat low blood pressure associated with septic
shock, allergic reaction etc.
Catabolism of heme (or Haem): 1. It consist of an iron ion co-ordinated
to a porphyrin of hemoglobin and acting as a ligand.
40
2. Heme break down takes place in macrophages of reticuloendothelial system of spleen and liver.
3. The catabolism of heme is shown in below flow charts.
Hyperbilirubinemia and jaundice: 1. Hyperbilirubinemia is a condition in which there is too much bilirubin (a
yellow coloured pigment ) in the blood. When red blood cells break down, a substance called bilirubin is formed. Babies
are not easily able to get rid of the bilirubin and it can build up in the blood and other tissues and fluids of the baby's
body.
2. It causes yellowing of the skin, eyes and other tissues. This condition is known as jaundice (bilirubin > 2 mg/100ml).
3. Types of jaundice: a) Hemolytic jaundice: a condition due to excessive hemolysis of blood.
b) Parenchymatous jaundice: a condition due to liver cell damage.
c) Obstructive jaundice: a condition due to presence of tumors in biliary tract
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Unit IV [YouTube lecture link: https://www.youtube.com/watch?v=fDS_qJBMPVM&list=PLVLZCIcT1Dow4XtHW

https://www.youtube.com/watch?v=fDS_qJBMPVM&list=PLVLZCIcT1Dow4XtHW-wLdOdKfMvUjZTRb ]
Nucleic acid metabolism transfer Biosynthesis of pur

etabolism and genetic information transfer: purine and pyrimidine
nucleotides. Catabolism of purine nucleotides
nucleotides and Hyperuricemia and Gout disease. Organization of
mammalian genome. Structure of DNA and RNA and their functions DNA replicati replication (semi conservative
model) Transcription or RNA synthesis. Genetic code, Translation or Protein synthesis and inhibitors.
Nucleic acid:
1. Nucleic acids are large biomolecules and biopolymers which are essential for henetic information
2. Nucleic acids are

re mainly of two types: DNA and RNA.
3. Genes are the segment of DNA that carries the genetic information as a genetic code.
4. Various components of DNA (nucleic acid) are as shown in flow chart.
5. Nucleotide:: Phosphate + pentose sugar (ribose) + nitrogenous

nit base
6. Nucleoside: pentose sugar (ribose) + nitrogenous base
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7. Type of sugar: a) Ribose, b) Deoxyribose
8. Type of nitrogenous base: a) Purines

ines (Adenine, Guanine);
Guanine) b) Pyrimidines (Cytosine,
Cytosine, Thymine, Uracil)
Biosynthesis of purine nucleotides: 1. It is the de novo synthesis by which a new purine ring is synthesized
along with the nucleotide that attaches to the ribose sugar generated by HMP pathway.
2. D-ribose-5-phosphate
phosphate serves as the starting material for stepwise synthesis of the purine ring.
3. The first biosynthesized purine product after 11 step is Inosine-5’-monophosphate
Inosine (See figure on next page).
IMP worked as precursor for various purine base. 4. It occurs in the liver. 5. In this whole reaction 6 ATP is
utilized.
43
44
Biosynthesis of Pyrimidine nucleotides:
45
1. Pyrimidine nucleotide biosynthesis takes place with six membered pyrimidine ring synthesis followed by
attachement to ribose phosphate in 8 step.
2. The synthesis begins with combined CO2 and NH3 and Pyrimidine ring is formed first.
3. Formation of cytosolic carbamoyl phosphate is a regulatory step.
4. This biosynthesis occurs in cytoplasm.
5. Carbamoyl phosphate is used in urea synthesis which is made in the mitochondrion.
Catabolism of purine nucleotides: It is an important pathway of the nucleic acid metabolism. Nucleic acids
are degraded in the digestive tract to nucleotides by various enzyme.
46
Hyperuricemia: 1. Hyperuricemia is an excess of uric acid in the blood. Uric acid passes through the liver, and enters
your bloodstream. Most of it is excreted (removed from your body) in your urine, or passes through your intestines to
regulate "normal" levels.
2. Normal uric acid level: 2.4-6.0 mg/dl (Female) and 3.4-7.0 mg/dl (male).
3. Causes: alcohol consumption, high levels of meat ingestion or high levels of seafood ingestion.
4. Risk factor: Hypertension, Kidney diseases, gouty arthritis.
5. Treatment: uricosuric drug (e.g. probenecid, allopurinol) and NSAID drugs.
Gout: 1. A form of arthritis characterised by severe pain, redness and tenderness in joints.
2. Pain and inflammation occur when too much uric acid crystallises and deposits in the joints.
3. Type: a) acute gout which is also known as gout attack. b) Chronic gout attacks are caused by the deposition of urate
in various joints in body.
3. Symptoms of gout include severe pain, redness and swelling in joints, often the big toe. Attacks can come suddenly,
often at night.
4. Treatment: During an acute attack, anti-inflammatory medication (NSAIDs) can help to relieve pain and shorten the
duration of the attack. Patients with chronic gout can use behavioural modification such as diet, exercise and decreased
intake of alcohol to help minimise the frequency of attacks. Additionally, patients with chronic gout are often put on
medication to reduce uric acid levels.
Organization of mammalian genome:

1. The genome of an organism is the whole of its
hereditary information encoded in its DNA (or,
for some viruses, RNA). This includes both the
genes and the non-coding sequences of the DNA.
2. The human genome is stored on
23 chromosome pairs in the cell nucleus and in
the small mitochondrial DNA. Chromosomes are
storage unit of genes.
3. The human genome contains just over
20,000 protein-coding genes, that code proteins
and many more that are non-coding.
4. Genes are the basic unit of genetic information
forms of DNA. DNA is
a collection of chemical information that carries
the instructions for making the proteins a cell will
need. Each gene contains a single set of
instructions.
Structure of DNA:
1. DNA (Deoxyribonucleic acid) is a molecule composed of two chains that coil around each other to form a double helix
carrying genetic instructions for the development.
47
2. DNA is made up of molecules called nucleotides. Each nucleotide contains a phosphate group, a sugar group and a
nitrogen base. The four types of nitrogen bases are adenine (A), thymine (T), guanine (G) and cytosine (C). The order of
these bases is determines DNA's instructions, or genetic code.
Function of DNA:
48
Structure of RNA:
1. RNAs (ribonucleic acids) are
single stranded. RNA consists of
ribose nucleotides (nitrogenous
bases appended to a ribose sugar)
attached by phosphodiester bonds,
forming strands of varying lengths.
The nitrogenous bases in RNA are
adenine, guanine, cytosine, and
uracil, which replace thymine in
DNA.
2. Function and Type of RNA:
There are main function of RNA is
the transfer of genetic information
from the nucleus to the cells. They
make up ribosome and help to assemble proteins. There are 3 main types of RNA, each encoded by its own type of
gene:
 mRNA - Messenger RNA: Encodes amino acid sequence of a polypeptide.
 tRNA - Transfer RNA: Brings amino acids to ribosomes during translation.
 rRNA - Ribosomal RNA: With ribosomal proteins, makes up the ribosomes, the organelles that translate the
mRNA.
DNA Replication (Semi-conservative

model):
1. Semi-conservative replication was
discovered by Watson and Crick. Semi-
conservative replication means that
during DNA replication, the two strands of
nucleotides separate. Both strands then form
the template for free nucleotides to bind to
create the two identical daughter strands.
Hence each daughter strand has half of
the DNA from the original strand and half
newly-formed DNA.
2. The step are as follow:
a) Replication fork formation: Double
helix of DNA unzipped in single stand in the
presence of enzyme DNA helicase.
b) Primer Binding: A primer (RNA piece)
binds in the presence of enzyme DNA
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primase.
c) Elongation: Enzyme DNA polymerases are responsible for creating the new strand by elongation process.
d) Termination:: An Enzyme exonuclease removes all RNA primers from the original strands when the continuous and
discontinuous
nuous strands are formed and there after primers are replaced
repl with appropriate bases.
e) Telomerase enzyme catalyzes the synthesis of telomere sequences at the end of the DNA
f) Finally two DNA molecules formed by replication half part of parent and half part as new stand.
Transcription or RNA synthesis:

1.Transcription is the first step in gene expression,
expression
in which information from a gene is used to
construct a functional product such as a protein.
2. The goal of transcription is to make a RNA copy
of a gene's DNA sequence.
3. For a protein-codingcoding gene, the RNA copy,
or transcript,, carries the information needed to build
a polypeptide (protein or protein subunit).
4. Eukaryotic transcripts need to go through some
processing steps before translation into
nto proteins.
5. RNA polymerase is the main transcription
enzyme. Using a DNA template, RNA polymerase
builds a new RNA molecule through base pairing. For instance, if
there is a G in the DNA template, RNA polymerase will add a C to
the new, growing RNA strand.
6. Steps:
a) Transcription initiation: To begin transcribing a gene, RNA
polymerase binds to the DNA of the gene at a region called
the promoter.. Basically, the promoter tells the polymerase where to "sit down" on the DNA and begin transcribing.
b) Elongation: Once RNA polymerase is in position at the promoter, the next step of transcription
transcription—elongation—can
begin. Basically, elongation
ation is the stage when the RNA strand gets longer.
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c) Transcription termination: RNA polymerase

will keep transcribing
ibing until it gets signals to stop. The
process of ending transcription is called termination.
termination
There are two major termination strategies found
in bacteria: Rho-dependent and Rho-independent.
independent.
In Rho-dependent termination,, the RNA
contains a binding site foror a protein called Rho
factor. Rho factor binds to this sequence and starts
"climbing" up the transcript towards RNA
polymerase.
Rho-independent termination depends on
specific sequences in the DNA template strand.
51
Genetic Code:
1. The genetic code is the set of rules by which information encoded in genetic material (DNA or RNA sequences) is
translated into proteins (amino acid sequences) by living cells.
2. The genetic code consists of 64 triplets of nucleotides.
3. Each of these triplets is defined as codones. Eg. AAA, AUG etc
4. Each unit of triplets represents a nucleotide (A, G, C, T, U) such as A stand for adenosine nucleotide.
4. There are two specific types of genetic codes called as RNA codons (read on MRNA) and DNA codons (read on
DNA).
5. The codones are of two types, viz:
a) Sense codons: They code for amino acids. There are 61 sense codones in the genetic code which code for 20 amino
acids e.g. AAA etc
b) Signal codons: They code for signals during protein synthesis. There are four codons namely AUG, UAA, UAG, and
UGA.
6. Properties: a) triplet, b) Universal, c) Coma-less, d) Non-overlapping, e) polar in nature, f) Non-ambiguous, g)
Redundant.
7. Application: 1) ATG is used as start codon, 2) TAG, TGA, and TAA are used as stop codon, 3) Start codon inform to
ribosome to start translation., 4) Stop codon stops translation of specific amino acid chain.
Translation or Protein synthesis

1. Protein synthesis is accomplished through a process
called translation.
2. After DNA is transcribed into a messenger RNA
(mRNA) molecule during transcription, the mRNA
must be translated to produce a protein.
3. In translation, mRNA along with transfer RNA
(tRNA) and ribosomes work together to
produce proteins.
4. There are three important steps namely initiation,
elongation, and termination.
a) During initiation the mRNA, The tRNA and the first
amino acid inter in ribosome.
b) In second step addition of amino acids one by one
occurs by the formation of peptide bonds.
c) In third step, termination occurs when a ribosome hits
with stop codon.
Inhibitors of Translation or Protein synthesis
1. Protein synthesis inhibitors is a substance that stops
or slows the growth of prokaryotic and eukaryotic cells
at ribosomal level.
2. Inhibitors of both prokaryotic and eukaryotic protein synthesis: Edeine, Fusidic acid, Tetracycline
3. Inhibitors specific for prokaryotes (only in bacterial cell): Chloramphenicol, Colicin E3, Erythromycin, Streptomycin.
4. Inhibitors specific for eukaryotes: anisomysin, Pactamicin,
-------------------------------------------------------------------------------------------------------------------------------------------------
52
Unit V [YouTube lecture link: https://www.youtube.com/watch?v=fDS_qJBMPVM&list=PLVLZCIcT1Dow4XtHW-wLdOdKfMvUjZTRb ]

Enzymes Introduction, properties, nomenclature and IUB classification of enzymes. Enzyme kinetics
(Michaelis plot, LineWeaver Burke plot) Enzyme inhibitors with examples. Regulation of enzymes: enzyme
induction and repression, allosteric enzymes regulation. Therapeutic and diagnostic applications of enzymes
and isoenzymes. Coenzymes –Structure and biochemical functions.
Enzymes Introduction: enzymes
1. Enzymes are a substance produced by a living organism which acts as a catalyst to bring about a specific
biochemical reaction.
2. Enzymes are biological molecules (typically proteins) that significantly speed up the rate of virtually all of the
chemical reactions that take place within cells. They are vital for life and serve a wide range of important functions
in the body, such as aiding in digestion and metabolism
3. Enzymes are made from amino acids, and they are proteins. When an enzyme is formed, it is made by stringing
together between 100 and 1,000 amino acids in a very specific and unique order. The chain of amino acids then folds
into a unique shape.
Properties of Enzymes:
1. Enzymes are protein macromolecule.
2. They are organic biocatalyst (simple or conjugated)
3. They require small quantity for the biological
action.
4. Their activity depends on the temperature
(optimized temp. 35oC-40oC) and changes in
hydrogen ion concentration (pH).
5. They are specific for bonds or linkage like ester,
peptide or glycoside e.g. Estrase act on ester bond
6. They act on only one type of specific substrate e.g.
urease decompose urea).
7. They always produce the same end products.
8. They are reusable.
9. Proenzymes are inactive before the start of
reaction.
10. Some enzymes requires as cofactor for proper functioning. Cofactors are non-protein part derived from
niacin, riboflavin etc. which is bound within the enzyme molecules.
11. They lower the activation of energy so reactions occur at mild temperature in all leaving cells.
12. Many enzymes are stereospecific e.g. L amino acid oxidase act only on the L. amino acid not on D-
amino acid.
Nomenclature of Enzymes:
1. The nomenclature of first discovered enzymes was named according to their sources by adding suffix -
in like pepsin, trypsin etc.
2. Enzymes were named according to their substrate by adding suffix –ase. E.g. Lactase acts on lactose
(substrate).
3. Enzymes are classified as per their functions like oxidases catalyze oxidation reaction.
Classification of enzymes based on the reactions: Enzymes are classified into 6 groups.
a) Addition or removal of water: Hydrolases (e.g. esterases) Hydrases (e.g. fumarase)
53
b) Transfer of electrons: Oxidases, Dehydrogenases

c) Transfer of radical: Transglycosidases of monosaccharides
d) C-C bond splitting or forming: Desmolases
e) Changing of molecules based on transformation: Isomerases
f) Joining of two molecules either through hydrolysis of pyrophosphate bond in ATP : Ligases
Classification of enzymes: There are various common classification of enzymes
1. Intracellular and extracellular enzymes:
a) Intracellular (endoenzymes) enzymes show their activity within the cells e.g. DNA polymerase
b) Extracellular (exoenzymes) enzymes show their activity outside of the cells e.g. pepsin, trypsin,
amylase etc.
2. Classification of enzymes based on the reactions: Enzymes are classified into 6 groups.
a) Addition or removal of water: Hydrolases (e.g. esterases) Hydrases (e.g. fumarase)
b) Transfer of electrons: Oxidases, Dehydrogenases
c) Transfer of radical: Transglycosidases of monosaccharides
d) C-C bond splitting or forming: Desmolases
e) Changing of molecules based on transformation: Isomerases
f) Joining of two molecules either through hydrolysis of pyrophosphate bond in ATP : Ligases
3. IUB Classification:
a) Due to various classifications and large no of enzymes, International union of chemistry (IUB)
specified standard nomenclature and classification of enzyme.
b) Based on their action they are divided into 6 major classes. Each enzyme is assigned a 4 Digit code number.
54
Enzyme kinetics: Enzyme kinetics is the study of the chemical reactions that are catalysed by enzymes. In
enzyme kinetics, the reaction rate is measured and the effects of varying the conditions of the reaction are
investigated. The two common kinetic processes are Michaelis plot and Line weaver Burke plot.
Michaelis plot:
1. In biochemistry, Michaelis–Menten kinetics is one of the best-known models of enzyme kinetics. It is named
after German biochemist Leonor Michaelis and Canadian physician Maud Menten.
2. In 1913, they proposed a mathematical model of the reaction. It involves an enzyme, E, binding to
a substrate, S, to form a complex, ES, which in turn releases a product, P, regenerating the original enzyme.
This may be represented schematically as
3. The model takes the form of an equation describing the rate of enzymatic reactions, by relating reaction rate
 (rate of formation of product, [P] ) to the concentration of a substrate [S]. Its formula is given by
4.
5. This equation is called the Michaelis–Menten equation. Where
a)  =d[P]/dt = rate of formation of product
b) [P] = Molar concentration of product formed
c) [S]= Molar concentration of substrate (reactant) used.
d) Kcat = catalytic rate constant
55
(BP203T)-2020
e) = maximum rate achieved by the system

sys at high substrate concentration
f) = Michaelis constant which is numerically equal to the substrate concentration at which the reaction
rate is half of .
g) [Eo] = initial concentration of enzyme
6. On the bases of above equation

quation Michaelis Menton graph has been plotted between Substrate concentration
[S] and initial reaction velocity (Vo)
7. The three mean observation of Michaels Menton plot are as shown below
bel
a) Substrate concentration [S] is less then reaction rate (V) is directory propositional to substrate
concentration [S]. It is an example of first order reaction.
b) when [S]>>> Km then V does note depend on [S]. [S]. It is an example of zero order kin
kinetic.
c) when [S]= Km then Intial velocity (Vo) of reaction become half of max velocity (Vmax)
8. Significance
a) The equation explains the velocity of enzyme reaction.
b) Vmax provides the theoretical information about possible maximum rate of reaction and can use as an
indicator to detect catalytic efficiency.
c) Km (Dissociation constant for [ES]) explain binding effect (relative stability);; greater the Km value, lesser
the binding of substrate to the enzyme.
d) If Vmax/Km has high value then A strong affinity
inity between the enzyme and substrate has been possible.
56
Lineweaver-Burk Plot:
1. It is also known as double reciprocal plot.
2. It is the graphical representation of Lineweaver-Burk equation of enzyme kinetics.
3. In M and M equation, When [S] increase , It is not possible to determine Vmax and Km.
4. To solve this problem Lineweaver-Burk, Modify the M & M equation as
Where
Vo =Vi= Initial rate of velocity
Km = The Michaelis constant
Vmax= maximum rate achieved by the system at high
substrate concentration.
[S]= molar concentration of substrate
Above equation can compare with the straight line

equation and draw Lineweaver-Burk plot between ; x (1/[S]) and y (1/ Vi)
y= ax + b
Where y= 1/ Vo (Vi); a = Km/ Vmax ; x= 1/[S] ; b=1/ Vmax
5. This plot shows the reciprocal of the reaction velocity (1/ Vi) as a function of substrate concentration 1/[S]in
the presence or absence of inhibitors.
6. By this plot , we can calculate Km from intercept – 1/ Km and Slope Km/ Vmax
Factors Affecting Enzyme Activity: Enzyme activity depends on various factors like
a) Enzyme Concentration: The correlation between enzyme concentration and velocity of reaction is directly
proportional. On increasing enzyme concentration, velocity of the reaction also increase
b) Substrate Concentration: Rate of velocity of enzyme reaction is also directly proportional with the concentration of
substrate at the limited range.
c) Temperature: With increase temperature, velocity of enzyme reaction increase at certain level (35-40 oC) and above
temperature it decrease.
d) Effect of pH: With increase pH, velocity of enzyme reaction increase at certain level (pH 7.4) and above pH, it
decrease.
e) Effect of activator: Certain ions like Mg+2, Zn+2 etc enhance activity.
Mechanism of Enzyme Action: There are several theories by which mechanism action of an enzyme is explained.
i) Lock and key theory: In this concept, enzymes and substrates are bind together as a lock and key fashion.
57
ii) Induced fit theory:

1. In biology, the active site is the region of an enzyme where substrate molecules bind and undergo a
chemical reaction. The active site consists of amino acid residues that form temporary bonds with the
substrate (binding site) and residues that catalyse a reaction of that substrate (catalytic site).
2. It is base on the active site of an enzyme which binds with suitable substrate and after completing suitable
effect, it breaks again
Enzyme inhibitors:
1. An enzyme inhibitor is a molecule that binds to an enzyme
and decreases its activity. By binding to enzymes' active sites,
inhibitors reduce the compatibility of substrate and enzyme.
2. Enzyme are non specific and specific in their nature
i) Non specific enzyme shows physical effect only.
ii) Specific enzymes have a fix site.
iii) Specific enzyme may be irreversible (show physical
iv) effects) or reversible in nature
3. There are three common types of reversible enzyme
inhibition - competitive, non-competitive and
substrate inhibition.
a) Competitive inhibitors: In competitive inhibition,
an inhibitor that resembles the normal substrate binds to
the enzyme, usually at the active site, and prevents the
substrate from binding. Eg.
antineoplastic drug
methotrexate
b) Non-competitive inhibition
is a type of enzyme
inhibition where the inhibitor
reduces the activity of the
enzyme and binds equally
well to the enzyme whether
or not it has already bound the
substrate. E.g. alanine
noncompetitively inhibits the
enzyme pyruvate kinase
c) Substrate inhibition:
Substrate inhibition means that
the velocity curve of a reaction
rises to a maximum
58
as substrate concentration increases and then decrease either to zero or to a non-zero.

d) Feedback inhibition: It is a cellular control mechanism where the activity is inhibited by the end product of
enzyme This mechanisms allows cells to regulate the production of end product of an enzyme
Regulation of enzyme: Enzymes can be regulated by other

molecules that either increase or reduce their activity.
Molecules that increase the activity of an enzyme are called
activators, while molecules that decrease the activity of
an enzyme are called inhibitors.
1. Enzyme activators are molecules that bind
to enzymes and increase their activity. They are the
opposite of enzyme inhibitors. An example of
an enzyme activator working in this way is fructose
2,6-bisphosphate, which activates
phosphofructokinase 1 and increases the rate of
glycolysis in response to the hormone insulin.
2. Inhibitors: as shown above
3. Enzyme induction: Enzyme induction is a process in which a molecule (e.g. a drug) induces (i.e.
initiates or enhances) the expression of an enzyme. Enzyme inhibition can refer to the inhibition of
the expression of the enzyme by another molecule. Examples of enzyme inducers include
aminoglutethimide, barbiturates, carbamazepine, glutethimide, griseofulvin, phenytoin, primidone,
rifabutin, rifampin, and troglitazone. Some
drugs, such as ritonavir, may act as either
an enzyme inhibitor or an enzyme inducer,
depending on the situation.
4. Enzyme repression: An enzyme repressor is a
substance that negatively regulates the amount
of an enzyme by decreasing the rate of its
biosynthesis. It is the opposite of an enzyme
inducer. For example, if the end product of a
series of enzyme-catalyzed reactions is a
particular amino acid, that amino acid acts as the
repressor molecule to further production.
5. Allosteric enzyme regulation:
Allosteric regulation is the regulation
of an enzyme by binding an effector
molecule at a site other than the
enzyme's active site. The site to
which the effector binds is termed
the allosteric site or regulatory site.
Isocitrate dehydrogenase of the
Krebs tricarboxylic acid cycle is
an example of an allosteric enzyme.
Therapeutic and diagnostic applications of
enzyme:
59
1. Enzymes are used for aiding digestion. Example: Amylases, Proteases, Lipase.
2. They are used as deworming agent E.g.: Papain.
3. They act as anti-clotting agents like fibrinolytic and thrombolytic. Ex. Urokinase.
4. They act to treat atherosclerosis like serratiopeptidase.
5. They are used to treat wounds and swelling. Example: trypsin. Chymotrypisn, serratiopeptidase.
6. They are used to assist metabolism like hyaluronidase.
7. They are used as surface disinfectants. Example: Trypsin
Diagnostic application:
1. They are also used in the diagnosis purpose. Example: Glucose oxidase along with peroxidase to detect the
level of glucose.
2. Liver disease: SGPT (gama-glutamyl transpeptidase)
3. Heart attacks: Asparate aminotransferase (AST)
4. Myocardial infection: Creatine phosphokinase
5. Uric acid: Uricase
Coenzymes-Structure and biochemical functions
1. Coenzymes are small molecules. They cannot by themselves catalyze a reaction but they can help enzymes
to do so. In technical terms, coenzymes are organic nonprotein molecules that bind with the protein molecule
(apoenzyme) to form the active enzyme (holoenzyme).
2. The main coenzyme are NAD/NADP, FMN, FAD, Coenzyme A( CoA), Thiamine pyrophosphate, Pyridoxal
phosphate (PAL).
NAD (Nicotinamide adenine dinucleotide)/NADP (Nicotinamide adenine dinucleotide phosphate):
1. Nicotinamide adenine dinucleotide is a cofactor that is
central to metabolism of redox reactions.
2. Found in all living cells, NAD is called a dinucleotide
because it consists of two nucleotides joined through their
phosphate groups. One nucleotide contains an adenine
nucleobase and the other nicotinamide
3. NAD is a donor of ADP-ribose moieties in ADP-
ribosylation reactions.
4. NAD is a donor of the second messanger molecule cyclic
ADP-ribose.
5. NAD has an important extracellular role as adenine
dinucleotide.
6. Ex. Lactic acid is oxidized to Pyruvic acid with the help of
lactate dehydrogenase enzyme where NAD acts as H-
acceptor.
7. Nicotinamide adenine dinucleotide phosphate, abbreviated NADP+ or, in older notation, TPN
(triphosphopyridine nucleotide), is a cofactor used
in anabolic reactions, such as the Calvin cycle and
lipid and nucleic acid syntheses, which
require NADPH as a reducing agent. NADPH is
the reduced form of NADP+
8. In Kreb cycle, Isocitric acid is converted into
oxalosuccinic acid with the help of isocitrate
60
(BP203T)-2020
dehydrogenase enzyme where NADP acts as H-acceptor.

H
Flavin mononucleotide (FMN) and Flavin adenine dinucleotide (FAD)
1. Flavin adenine dinucleotide (FAD FAD) is a redox-active
active coenzyme associated with various proteins, which is
involved
nvolved with several important enzymatic reactions in metabolism. A flavoprotein is a protein that contains a
flavin group, this may be in the form of FAD or flavin mononucleotide (FMN).
2. Both FAD and FMN act as electron carriers in redox reactions.
3. They are e responsible for energy production
4. FMN and FAD both are cable of reversibly accepting two hydrogen atoms and forms FMNH2 and FADH2
respectively.
5. Ex. In Kreb’s cycle, succinic acid is oxidized to fumaric acid in presence of succinate dehydrogenate where FA
FAD
acts as H-acceptor.
Coenzyme A (CoA):
1. Coenzyme A is a coenzyme containing pantothenic acid, adenosine 3-phosphate 3 phosphate 55-pyrophosphate, and
cysteamine; involved in the transfer of acyl groups, notably in transacetylations.
2. Coenzyme A acts as acyl group carrier rrier because it is chemically thiol

3. It reacts with carboxlic acid to form thioesters
4. It helps in transferring fatty acids from cytoplasm to mitochondria
5. Pantothenic acid is an essential part for coenzyme A
6. It is essential for heme formation in hemoglobin
7. It is essential for the synthesis of acetyl choline which is important for nerve transmission
transmission.
8. It enters into the citric acid cycle and be oxidized to produce energy.
9. It is used as the starting material for the biosynthesis of triglycerides, phospholipids or cholesterol and other
steroids.
Thimine pyrophosphate (TPP): Thiamine pyrophosphate,
or thiamine diphosphate, or cocarboxylase is a thiamine
derivative which is produced by the enzyme thiamine
diphosphokinase. Thiamine pyrophosphate is a cofactor that tha
is present in all living systems, in which it catalyzes several
biochemical reactions such as Pyruvate dehydrogenase
complex, pyruvate decarboxylase in ethanol fermentation,
alpha-ketoglutarate
ketoglutarate dehydrogenase complex etc.
Pyridoxal phosphate (PAL): Pyridoxal

oxal phosphate, the active form of
vitamin B₆,, is a coenzyme in a variety of enzymatic reactions. PAL is
61
required for transformation reaction, synthesis and catabolism of amino acid, conversion of essential amino acid
trypthophan to niacin vitamin.
Some specific enzyme:

a) Isoenzyme (Isozyme): Isoenzymes are multiple forms of some enzyme that catalyze the same reaction but
have different physic-chemical properties like isoelectric point, electrophoretic mobility modes of regulation
etc. Ex. Lactate dehydrogenase has shown electrophoretic mobility.
b) A ribozyme is a ribonucleic acid (RNA) enzyme that catalyzes a chemical reaction. The ribozyme catalyses
specific reactions in a similar way to that of protein enzymes. Also called catalytic RNA, ribozymes are
found in the ribosome where they join amino acids together to form protein chains.
c) A restriction enzyme is a protein that recognizes a specific, short nucleotide sequence and cuts the DNA
only at that specific site, which is known as restriction site or target sequence. More than 400 restriction
enzymes have been isolated from the bacteria that manufacture them.
AKTU Biochemistry [BP203T] previous year question paper:
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AKTU BIOCHEMISTRY [BP203T] COMPLETE NOTE

[As per AKTU syllabus]

BIOCHEMISTRY (BP 203 T)

Unit I [YouTube lecture link: https://www.youtube.com/watch?v=fDS_qJBMPVM&list=PLVLZCIcT1Dow4XtHW-wLdOdKfMvUjZTRb ]

Classification: A diverse range of bimolecular are exist, In

Biochemical role of carbohydrates:

Chemical nature of carbohydrate:

Carbohydrates are divided into four major groups

 Stereoisomerism: Carbohydrates contain 2n isomers (Where n=asymmetric carbon atoms).

 An oligosaccharide is a saccharide polymer containing a small number of monosaccharides. E. g. maltose,

The fatty acids are broadly classified as follows:

Eg. Palmitic acid: CH3(CH2)14COOH

Biological role of lipids:

Classification of amino acids: Amino acids can be classified in different ways

c) Classification based on the

e, serine, and tyrosine.

3. They provide structural support to cells.

4. Non-covalent bonds break with heat (denaturation).

5. Proteins have molecular weight ranging from 5000 to 3000000.

Bioenergetics: The study of the transformation of energy in living organisms.

Concepts of Free energy: It is defined as “the amount of energy available

Endergonic and exergonic reaction:

Relationship between free energy, enthalpy and

Enthalpy: It is a total heat content of a system.

Entropy:: It is defined as the measure of disorder or

Redox potential: It is also known as oxidation and

as the high energy compound and if the energy of

Biological significances of ATP:

The Adenosine triphosphate (ATP)) molecule is the

Coupling of reaction:: An unfavorable reaction

Biological significances of cyclic AMP:

1) Cyclic adenosine monophosphate (cAMP) is a second

Unit II [YouTube lecture link: https://www.youtube.com/watch?v=fDS_qJBMPVM&list=PLVLZCIcT1Dow4XtHW

Carbohydrate metabolism: It is a biochemical and metabolic process.

Glycolysis- Pathway [ Embden-Meyerhof

2) Glycolysis (Aerobic,, in the presence of oxygen)

b) Energy-releasing phase. In this phase, each three-carbon

Overall, glycolysis converts one six-carbon

Where: NAD= Nicotinamide adenine dinucleotide (coenzyme); NADH= Nicotinamide adenine

Glycolysis- Pathway (Aerobic)

Overall energy of glycolysis:

b) a)Total energetics in anaerobic pathway=

Significance of the glycolysis pathway:

Citric acid cycle [Krebs cycle,, TCA

1. After Glycolysis, Pyruvate inter in mitochondria.

Enzymes in TCA cycle

9. Step VI: Succinate dehydrogenase

14. Hence, 2 Acetyl Co A produce total energy= 12 x 2= 24.

Energetic in complete oxidation of a glucose molecule:

1. Aerobic glycolysis = 8 ATP

2. Oxidation of 2 molecule of Pyruvate = 6 ATP

3. TCA cycle = 24 ATP

NET energetic = 38 ATP