BIOCHEMISTRY REVIEW NOTES

What Is Biochemistry?
Biochemistry is the study of the chemistry of living things. This includes organic molecules and their chemical
reactions. Most people consider biochemistry to be synonymous with molecular biology.

The principal types of biological molecules or biomolecules are:

• carbohydrates
• lipids
• proteins
• nucleic acids
Many of these molecules are complex molecules called polymers, which are made up of monomer subunits.
Biochemical molecules are based on carbon.

What Is Biochemistry Used For?

• Biochemistry is used to learn about the biological processes which take place in cells and organisms.
• Biochemistry may be used to study the properties of biological molecules, for a variety of purposes. For
example, a biochemist may study the characteristics of the keratin in hair so that shampoo may be developed
that enhances curliness or softness.
• Biochemists find uses for biomolecules. For example, a biochemist may use a certain lipid as a food additive.
• Alternatively, a biochemist might find a substitute for a usual biomolecule. For example, biochemists help to
develop artificial sweeteners.
• Biochemists can help cells to produce new products. Gene therapy is within the realm of biochemistry. The
development of biological machinery falls within the realm of biochemistry.
Amino Acids and Primary Structure of Proteins
Functions of proteins:
1- catalysts - enzymes for metabolic pathways
2- storage and transport - e.g. myoglobin and hemoglobin3- structural - e.g. actin,
myosin
4- mechanical work - movement of flagella and cilia, microtubule movement during mitosis, muscle
contraction
5- decoding information - translation and gene expression6- hormones and hormone
receptors
7- specialized functions - e.g. antibodiesStructure of amino acids
There are 20 common amino acids called a-amino acids because they all have an amino (NH3+)group and a carboxyl
group (COOH) attached to C-2 carbon (a carbon).
At pH of 7, amino group is protonated (-NH3+) and carboxyl group is ionized (COO-). Theamino acid is called a
zwitterion.
pKa of a carboxyl group = 1.8 - 2.5pKa of a amino group = 8.7 -
10.7

The a carbon is chiral or asymmetric ( 4 different groups are attached to the carbon; exception is glycine.)

Amino acids exist as stereoisomers (same molecular formula, but differ in arrangement of groups).
Designated D(right) or L(left).
Amino acids used in nature are of L configuration.

carboxylate group at top --> points awayside chain at bottom a amino group orientation determines
NH3+ on left = L
NH3+ on right = D
Can also use RS system of nomenclature.

Structures of 20 common amino acids:

Amino acids are grouped based upon the properties and structures of side chains.

1) aliphatic (R groups consist of carbons and hydrogens)glycine - R=H smallest

a.a. with no chiral centeralanine - R=CH3 methyl group
valine R = branched; hydrophobic; important in protein foldingleucine R= 4 carbon branched
side chain
isoleucine R = 2 chiral centers
proline R = ring; puts bends or kinks in proteins; contains a secondary amino group

2) aromatic (R groups have phenyl ring) phenylalanine - very

hydrophobic
tyrosine - hydrophobic, but not as much because of polar groups tryptophan - “

Absorb UV light at 280 nm --> used to estimate [protein]

3) sulfur-containing R groups
methionine - sulfur is internal (hydrophobic)
cysteine - sulfur is terminal --> highly reactive; can form disulfide bonds
4) side chains with alcohols
serine - b-hydroxyl groups --> hydrophilicthreonine - “

5) basic R groups
histidine - hydrophilic side chains - + charged at neutral pHlysine - “
arginine - strong base

6) acidic R groups and amide derivatives

aspartate - b carboxyl group - confer - charges on proteinsglutamate - g carboxyl group

asparagine - amide of aspartate - side groups uncharged --> polarglutamine - amide of glutamat- “
Amide groups can form H bonds with atoms of other polar amino acids.
 Ionization of Amino Acids
All amino acids are have a neutral net charge at physiological pH (7.4).

The a carboxyl and a amino groups and any other ionizable groups determine charge.

Each amino acid has 2 or 3 pKa values (7 amino acids have side chains that are ionizable) (see Table 3.2). This
complicates the basic titration curve, so that there are 3 inflectionpoints rather than 2.

At a given pH, amino acids have different net charges.

Can use titration curves for amino acids to show ionizable groups.
The isoelectric point (pI) is the pH at which the amino acid has no net charge = zwitterion.
If pH > pI, amino acid would be negatively charged.If pH < pI, amino acid would be
positively charged.If pH = pI, amino acid would have no charge.

Classification of amino acids on the basis of R-group

1.Nonpolar, Aliphatic amino acids: The R groups in this class of amino acids are nonpolar and hydrophobic.
Glycine, Alanine, Valine, leucine, Isoleucine, Methionine, Proline.
2.Aromatic amino acids: Phenylalanine, tyrosine, and tryptophan, with their aromatic side chains, are relatively
nonpolar (hydrophobic). All can participate in hydrophobic interactions.
3.Polar, Uncharged amino acids: The R groups of these amino acids are more soluble in water, or more
hydrophilic, than those of the nonpolar amino acids, because they contain functional groups that form hydrogen
bonds with water. This class of amino acids includes serine, threonine, cysteine, asparagine, and glutamine.
4.Acidic amino acids: Amino acids in which R-group is acidic or negatively charged. Glutamic acid and Aspartic acid
5.Basic amino acids: Amino acids in which R-group is basic or positively charged. Lysine, Arginine, Histidine
Classification of amino acids on the basis of nutrition
• Essential amino acids (Nine)
Nine amino acids cannot be synthesized in the body and, therefore, must be present in the diet in order for protein
synthesis to occur.
These essential amino acids are histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine,
tryptophan, and valine.
• Non-essential amino acids (Eleven)
These amino acids can be synthesized in the body itself and hence do not necessarily need to be acquired
through diet.
These non-essential amino acids are Arginine, glutamine, tyrosine, cysteine, glycine, proline, serine, ornithine,
alanine, asparagine, and aspartate.
Classification of amino acids on the basis of the metabolic fate
1.Glucogenic amino acids: These amino acids serve as precursors of gluconeogenesis for glucose formation.
Glycine, alanine, serine, aspartic acid, asparagine, glutamic acid, glutamine, proline, valine, methionine, cysteine,
histidine, and arginine.
2.Ketogenic amino acids: These amino acids break down to form ketone bodies. Leucine and Lysine.
3.Both glucogenic and ketogenic amino acids: These amino acids break down to form precursors for both ketone
bodies and glucose. Isoleucine, Phenylalanine, Tryptophan, and tyrosine
Enzymes
Enzymes Definition
An enzyme is a protein biomolecule that acts as a biocatalyst by regulating the rate of various metabolic reactions
without itself being altered in the process.
• The name ‘enzyme’ literally means ‘in yeast’, and this
was referred to denote one of the most important
reactions involved in the production of ethyl alcohol
and carbon dioxide through the agency of an
enzyme zymase, present in yeast.
• Enzymes are biological catalysts that catalyze more
than 5000 different biochemical reactions taking
place in all living organisms.
• However, these are different from other catalysts
which are chemical and can last indefinitely.
Enzymes are proteins that are prone to damage and inactivation.
• Enzymes are also highly specific and usually act on a specific substrate of specific reactions.

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1. Intracellular enzymes
• The enzymes that act within the cells in which they are produced are called intracellular enzymes or endoenzymes.
• As these enzymes catalyze most of the metabolic reactions of the cell, they are also referred to as metabolic
enzymes.
• Most of the enzymes in plants and animals are intracellular enzymes or endoenzymes.
• Intracellular enzymes usually break down large polymers into smaller chains of monomers.
• All intracellular enzymes undergo intracellular digestion during cell death.
2. Extracellular enzymes
• The enzymes which are liberated by living cells and catalyze useful reactions outside the cell but within its
environment are known as extracellular enzymes or exoenzymes.
• Exoenzymes act chiefly as digestive enzymes, catalyzing the breakdown of complex macromolecules to simpler
polymers or monomers, which can then be readily absorbed by the cell.
• These mostly act at the end of polymers to break down their monomers one at a time.
• Exoenzymes are enzymes found in bacteria, fungi, and some insectivores like Drosera and Nepenthes.
• Extracellular enzymes, unlike intracellular enzymes, undergo external digestion during cell death.
Enzymes and activation energy
• According to the transition state theory, for a chemical reaction to occur between two reactant molecules, their free
energy level must be raised above a threshold level to take them to a high-energy transition state.
• The free energy needed to elevate a molecule from its stable, low-energy ground state to a higher energy unstable
state is known as activation energy.
• The rate of a reaction depends on the number of reactant molecules that have enough energy to reach the
transition state of the slowest step (rate-determining step) in the reaction.
• As a rule, very few molecules possess enough energy to reach the transition state.
• Enzymes, however, reduce the value of activation energy for a reaction, thereby phenomenally increasing the rate
of reactions.
• Some enzymes lower the activation energy after the enzyme forms a complex with the substrate which by bending
substrate molecules in a way facilitates bond-breaking.
• Other enzymes speed up the reaction by bringing the two reactants closer in the right orientation.
Structure of Enzymes
All enzymes are proteins composed of amino acid chains linked together by peptide bonds. This is the primary structure of
enzymes. All enzymes have a highly specific binding site or active site to which their substrate binds to produce an enzyme-
substrate complex. The three-dimensional structures of many proteins have been observed by x-ray crystallography. These
structures differ from one enzyme to another, and some of the enzymes and their structure has been described below:
1. Ribonuclease (RNase)
• Ribonuclease is a small globular protein secreted by the pancreas into the small intestine, where it is involved in the
catalysis of the hydrolysis of certain bonds in ribonucleic acids present in ingested food.
• This enzyme protein consists of a single polypeptide chain of 124 amino acid residues with lysine at the N-terminal
and valine at the C-terminal.
• About 25% of the segments are in α-helix structure while the rest are β-sheets.
• Besides, there are eight cysteine residues, thus apparently forming four disulfide linkages that support the tertiary
structure of the protein.
• The active site is present in the depression at the middle of the chain and the residues forming the active site are 6-
8, 11, 12, 41, 42, 46-48, and 117-119.
2. Lysozyme
• Lysozyme is another small globular protein that is present in tears, nasal mucus, gastric secretions, milk, and egg
white.
• The enzyme lysozyme is consists of 129 amino acids linked together to form the primary structure, and the first
amino acid is lysine.
• The enzyme has about 12% β-conformation and 40%-α helical segments.
• Lysozyme has a compactly-folded conformation with most of its hydrophobic R groups inside the globular structure,
away from water, and its hydrophilic R groups outside, facing the aqueous medium.
• The active site has six subsites that bind various substrates or inhibitors, and the amino acid residues located at the
active sites are 35, 52, 59, 62, 63, and 107.
3. Chymotrypsin
• Chymotrypsin is a mammalian digestive enzyme produced in the small intestine that catalyzes the hydrolysis of
proteins.
• Chymotrypsin is highly selective in its action as it catalyzes the hydrolysis of only those peptide bonds that are
present on the carboxyl side of amino acids with aromatic or bulky hydrophobic R groups.
• A molecule of chymotrypsin consists of 3 short polypeptide chains of 13, 131, and 97 amino acid residues
respectively, supported by two interchain disulfide bonds.
• The secondary structure of chymotrypsin consists of several antiparallel β pleated sheet regions and a little α helical
structure.
How do enzymes work?
• The mechanism of action of enzymes in a chemical reaction can occur by several modes; substrate binding,
catalysis, substrate presentation, and allosteric modulation.
• But the most common mode of action of enzymes is by the binding of the substrate.
• An enzyme molecule has a specific active site to which its substrate binds and produces an enzyme-substrate
complex.
• The reaction proceeds at the binding site to produce the products which remain associated briefly with the enzyme.
• The product is then
liberated, and the
enzyme molecule
is freed in an
active state to
initiate another
round of catalysis.
• To describe the
mechanism of
action of enzymes
to different models
have been
proposed;
•
1. Lock and key hypothesis
Lock and key model of Enzymes.
• The lock and key model was proposed by Emil Fischer in 1898 and is also known as the template model.
• According to this model, the binding of the substrate and the enzyme takes place at the active site in a manner
similar to the one where a key fits a lock and results in the formation of an enzyme-substrate complex.
• In fact, the enzyme-substrate binding depends on a reciprocal fit between the molecular structure of the enzyme
and the substrate.
• The enzyme-substrate complex formed is highly unstable and almost immediately decomposes to produce the end
products of the reaction and to regenerate the free enzyme.
• This process results in the release of energy which, in turn, raises the energy level of the substrate molecule, thus
inducing the activated or transition state.
• In this activated state, some bonds of the substrate molecule are made susceptible to cleavage.
• This model, however, has few drawbacks as it cannot explain the stability of the transitional state of the enzyme
and also the concept of the rigidity of the active site.
2. Induced fit hypothesis

Figure: Induced fit model of Enzymes

• The induced fit hypothesis is a modified form of the lock and key hypothesis proposed by Koshland in 1958.
• According to this hypothesis, the enzyme molecule does not retain its original shape and structure.
• Instead, the contact of the substrate induces some configurational or geometrical changes in the active site of the
enzyme molecule.
• As a result, the enzyme molecule is made to fit the configuration and active centers of the substrate completely.
• Meanwhile, other amino acid residues remain buried in the interior of the molecule.
• However, the sequence of events resulting in the conformational change might be different.
• Some enzymes might first undergo a conformational change, then bind the substrate.
• In an alternative pathway, the substrate may first be bound, and then a conformational change may occur in the
active site.
• Thirdly, both the processes may co-occur with further isomerization to the final confirmation.
Properties of enzymes
• Enzyme molecules are large, and because of their large size, the enzyme molecules possess meager rates of
diffusion. As a result, enzymes form colloidal systems in water.
• Enzymes act catalytically and accelerate the rate of chemical reactions occurring in biological systems and
involving biological substrate.
• Most enzymes also do not participate in the reactions they catalyze. Similarly, some enzymes that are involved in
the reaction are recovered without undergoing any qualitative or quantitative change at the end of the reaction.
• Most enzymes are highly specific in their action.
• Being proteinaceous in nature, the enzymes are susceptible to heat. The rate of an enzyme action increases with
the rise in temperature; the rate being frequently increased 2 to 3 times for a rise in temperature of 10ºC.
• The enzymes catalyze the reversion of the reactions they catalyze.
• Enzymes are also pH sensitive as the pH of a medium will affect the efficiency of an enzyme and their activity is
maximum at a specific pH.
Active site of enzymes

Enzymes are much larger than the substrate they act on, and thus there are some
specific regions or sites on the enzyme for binding with the substrate, called active
sites. Even in enzymes that differ widely in their properties, the active site present in
their molecule possesses some common features;
1. The active site of an enzyme is a relatively small portion within an enzyme
molecule.
2. The active site is a 3-dimensional entity made up of groups that come from different parts of the linear amino
acid sequence.
3. The arrangement and orientation of atoms in the active site are well defined and highly specific, which is the
cause of the marked specificity of the enzymes. However, in some cases, the active site changes its
configuration in order to bind a substance.
4. The interactions or forces between the active site and the substrate molecule are relatively weak.
5. The active sites in the enzyme molecules are mostly present in grooves or crevices from where large
quantities of water are excluded.
Enzyme-substrate complex
• The enzyme-substrate complex is a transitional molecule formed after the substrate binds with the enzyme.
• The formation of the enzyme-substrate complex is important for several reasons. The most important and notable
reason is that the substrate binds with the enzyme temporarily and the enzyme is set free once the reaction is
complete.
• This allows a single enzyme molecule to be used millions of times, and thus, only a small amount of enzyme is
required in each cell.
• Another advantage of an enzyme-substrate complex is the reduction in the free energy (activation energy) required
for the substrate to rise into the high-energy transition state.
Enzyme specificity
Most enzymes are highly specific towards the substrate they act on. Enzyme specificity exists in a way that they may act on
one specific type of substrate molecule or on a group of structurally related compounds or on only one of the two optical
isomers of a compound or only one of the two geometrical isomers. Based on this, four patterns of enzyme specificity have
been recognized;
1. Absolute specificity
• Some enzymes are capable of acting on only one substrate, and an example of this is the enzyme urease that acts
only on urea to produce ammonia and carbon dioxide.
2. Group specificity
• Other enzymes catalyze all reactions of a structurally related group of compounds.
• It is observed in lactic dehydrogenase (LDH) that catalyzes the interconversion of pyruvic acid and lactic acid along
with a number of other structurally related compounds.
3. Optical specificity
• Another important form of specificity is seen in some enzymes where a certain enzyme will react with only one of
the two optical isomers of a compound.
• The oxidation of the D-amino acids to the corresponding keto acids by amino acid oxidase is an example of optical
specificity.
• Among the enzymes that exhibit optical specificity, some might interconvert the two optical isomers of a compound.
An example of this is alanine racemase that catalyzes the interconversion between L- and D-alanine.
4. Geometrical specificity
• Geometrical specificity is observed in some enzymes exhibit specificity towards the cis and trans forms.
• An example of this is the enzyme fumarase that catalyzes the interconversion of fumaric and malic acids
Functions/ Biological roles of Enzymes
Enzymes are vital for all biological processes, aiding in digestion, and metabolism. Besides, these are also involved in
several other processes;
1. Enzymes like kinases and phosphatases are important for cell regulation and signal transmission.
 2. Different enzymes are produced throughout the body for the regulation of reactions involved in various
metabolic pathways.
3. The activation and inhibition of enzymes resulting in a negative feedback mechanism adjust the rate of
synthesis of intermediate metabolites according to the demands of the cells.
4. They also catalyze Post-translational modifications involving phosphorylation, glycosylation, and cleavage of
the polypeptide chain.
5. Some enzymes are also involved in the regulation of enzyme levels by changing the rate of
enzyme degradation.
6. Since a tight regulation of enzymes is essential for homeostasis, any changes in the enzyme structure and
production might result in diseases.
7. Enzymes synthesized in various organisms are also utilized in various industries for wine production, cheese
production, bread whitening, and designing fabrics.

Carbohydrates
In biochemical perspective, a carbohydrate is defined as polyhydroxy aldehyde
or ketone.

• The presence of the aldehyde and ketone groups divide carbohydrates

into two major groups namely aldoses and ketoses

Aldehyde: H-C=O
Ketone: O=C-CH2OH

The number of carbons may also be indicated by adding syllables in the carbohydrate’s name:
ALDOHEXOSE- Aldo(aldehyde) HEX (Six) Ose (Carb group)

Glyceraldehyde – aldotriose
Dihydroxyacetone – ketotriose
• Same molecular formula but different functional groups = Tautomers

• Like most organic compounds, carbohydrates have CHIRAL or ASSYMETRIC carbons

For carbohydrates with more than one chiral center, the D or L
designation is determined by the hydroxyl group farthest from the
carbonyl carbon.

• In nature, the most abundant carbohydrates exist as D

enantiomeric forms while L isomers are rare.

Sugars only differ in only one chiral carbon such as the case of D-mannose and D-glucose at C2.
These are called epimers.

Cyclization (Making into haworth or chair conformation) results to formation of a NEW chiral center in carbon 1, hence
leading to formation of ANOMERS designated as alpha (OH below the ring) or beta (OH above the ring) conformation
which may interconvert through mutarotation

TYPES OF CYCLIC
CARBOHYDRATES
Sugars in ring conformation may adopt a six-membered or a five-membered closed structures which
resembles pyran and furan rings.

CLASSIFICATION OF CARBOHYDRATES
Carbohydrates are classified according to the number of sugar units (Monomers) they contain:
a.Monosaccharides
b.Disaccharides Carbohydrates composed of two sugar units joined by a glycosidic bond
c.Oligosaccharides
d.Polysaccharides
Glycosidic bond-
Can be 1 → 2 bond or 1 → 3 bond or 1 → 4 bond.
Oligosaccharides – are made up of 3-10 monomeric sugar units which are commonly attached to proteins or lipids such as
the ABO antigens.
Polysaccharides – Carbohydrates composed of long chains of sugar molecules, usually more than ten residues.
Polysaccharides play significant roles in organisms as they serve as energy storage (glycogen and starch), provide
structure (cellulose and chitin) as well as protection to host (bacterial cell wall of Gram positive bacteria).

Functions of Carbohydrates:
1.Energy Source
2.Structural Support
3.Cell-mediated recognition

Amylose and Amylopectin of Storage

Carbohydrates
• The principal storage polysaccharides are
amylose and amylopectin. These
polymers are made up of a-D-
glucopyranose which differ in glycosidic
linkage.
• amylose is an unbranched polymer of 100-
1000 D-glucose in an a-(1 --> 4) glycosidic
linkage.
• amylopectin is a branched polymer a-(1-->
6) branches of residues in an a-(1 --> 4)
linkage; overall between 300-6000 glucose
residues, with branches once every25
residues; side chains are 15-25 residues
long

Storage Carbohydrates: Glycogen and Starch

• Starch, the primary carbohydrate storage molecule in plants and Glycogen in animal liver and skeletal muscles both
contain amylose and amylopectin but differ in the frequency of branching points.
•Starch has branch points every 24-30 residues.
•Glycogen has branch points every 8-12 residues

Structural Polysaccharides: Chitin and Cellulose

•Chitin is a polymer made up of N-acetyl-B-D-glucosamine. It is generally found in invertebrates as a major composition of
exoskeletons of arthropods and mollusks.
•Cellulose on the other hand is made up of long chains of B-D-glucose which are held intact by hydrogen bonds giving
plant cell walls stability and high tensile strength.

Glycosaminoglycans
Unbranched polysaccharides that consists of alternating uronic acid and hexosamine residue

Hyaluronic acid – component of connective tissue, synovial fluid, and vitreous humor. Serves as shock absorbers and
lubricants
Heparin – not a constituent of connective tissue; occurs in the intracellular granules of mast cells in arterial walls.
Heparan sulfate – ubiquitous cell surface component; extracellular substance in blood vessels and brain
Plants don’t produce glycosaminoglycans

Glycoproteins
The polypeptide chains of glycoprotein are synthesized under genetic control
Carbohydrate chains are enzymatically added and covalently linked to the polypeptide chain without the guidance of the
nucleic acid template --- microheterogeneity
Types:
◦Proteoglycan
◦Peptidoglycan
◦Glycosylated protein
Proteoglycan
The brushlike structure of proteoglycans, together with the polyanionic character of keratan sulfate and chondroitin
sulfate cause these complexes to be highly hydrated.

As a result, these complexes have high resilience

Peptidoglycans
Gram positive bacteria have peptidoglycan layers in their surface which contains carbohydrates. Since
carbohydrates have polyhydroxyl groups that form hydrdogen bond with water, Gram positive bacteria can be stained by
dyes dissolved in water

Clinical Disease and Application

Malnutrition
• Kwashiorkor- Nutritional imbalance due to very low protein intake but with adequate or high-calorie intake.
• Marasmus- A state of prolonged negative nitrogen balance due to chronic deficiency of calories but adequate in
protein intake.

Inborn Diseases
• Hartnup’s disease- Inability to absorb neutral amino acids including tryptophan, thus, leading to pellagra-like
condition.
• Albinism- Skin depigmentation due to tyrosinase deficiency.
• Alkaptonuria- Darkening of urine on standing due to oxidation of homogentisic acid into brownish-black pigment
caused by deficiency in homogentisate oxidase.
• Phenylketonuria- Caused by deficiency of phenylalanine hydroxylase.
• Maple syrup disease- Genetic deficiency of branched-chain alpha-ketodehydrogenase
 Creatinine kinase

• Muscle- Creatine Kinase MM

• Brain =Creatine Kinase BB
• Heart- Creatine Kinase MB

Enzymes Diseases

•Troponin I- increased with enzymes suddenly experienced nausea, chest pain that may feel like pressure,
tightness, pain, squeezing or aching, and pain or discomfort that spreads to the shoulder, arm, back, neck, jaw,
teeth or sometimes the upper belly.
• Tarui’s disease- Deficiency in Phosphofructokinase (PFK)
• Her - Deficiency in Liver glycogen phosphorylase
• McArdle’s- Muscle glycogen phosphorylase
WATER SOLUBLE VITAMINS DEFICIENCIES
1. B1 Thiamine: Wernicke-korsakoff, Beri-Beri
2. B2 Ribloflavin - Seborrheic Dermatitis, Glossitis, Cheilosis, Photophobia, Decrease ability of mitochondria to
generate ATP and Growth retardation
3. B3 Niacin - Pellagra: Dermatitis, Dementia, Diarrhea
4. B5 Pantothenic acid: Dermatitis in chicks, Burning foot disease
Folic acid: Spina bifida
5. B6 Pyridoxine- Peripheral neuropathy
6. B7 Biotin, Vitamin H- Dermatitis, Impaired Fat and carbohydrate metabolism
7. B9 Tetrahydrofolate, Folic acid, Pteroylglutamic acid- Megaloblastic anemia, Spina bifida
8. B12 Cyanocolamin, Hydroxocabalamin- Pernicious Anemia and Megablastic Anemia

Vitamin C – Scurvy
FAT SOLUBLE VITAMINS DEFICIENCIES
• Vitamin A - Nyctalopia, Xeropthalmia
• Vitamin D- Rickets, Osteomalacia
• Vitamin E-
• VITAMIN K- Bleeding (Decrease microflora in the intestines)
CARBOHYDRATES DISEASES
• Obesity. Non-insulin dependent diabetes mellitus (NIDDM) Cardiovascular disease.
Galactosemia- usually is caused by a defective component of the second major step in the metabolism of the
sugar galactose.
• Lactose Intolerance- unable to fully digest the sugar (lactose) in milk. As a result, they have diarrhea, gas and
bloating after eating or drinking dairy products.
• Hypoglycemia is a condition in which your blood sugar (glucose) level is lower than the standard range.
• Diabetes- A metabolic disorder in which the body has high sugar levels for prolonged periods of time.
• Type 1 diabetes juvenile diabetes- A chronic condition where the pancreas produces little or no insulin.
Autoimmune disease and insulin dependent.
• Type 2 diabetes mellitus, formerly known as adult-onset diabetes, is a form of diabetes mellitus that is
characterized by high blood sugar, insulin resistance, and relative lack of insulin.
• Gestational diabetes- A condition in which women develop diabetes (high blood sugar) during pregnancy.