GENERAL BIOLOGY 1

Quarter 1 – Module 7: Enzymes

Lesson
Enzymes 
1

In the precious lesson you have learned about the structures and functions of biological molecules (i.e.,
carbohydrates, lipids, nucleic acids, and proteins). These carbon-containing molecules are collectively referred to as
organic molecules, so named because they were first discovered in all forms of life. In all living organisms, sophisticated
biochemical phenomena occur. You have encountered that proteins functions as storage, defense and transport. In this
lesson you will learn that proteins too are involve in chemical processes (enzymatic proteins). Many chemical reactions
happen within our bodies, but these reactions happen too slowly on their own. To help speed up these reactions, our body
uses specific biomolecules called enzymes. 

What’s
In
In the human body, complex metabolic processes break down a variety of food materials to simpler chemicals,
yielding energy and the raw materials to build body constituents, such as muscle, blood, and brain tissue. Also, other
forms of life –plants, animals, fungi, protists, archaebacterial and eubacteria- need enzyme to break down large molecules
or build new ones to carry out their life functions. 

What is
It
Background 
Enzymes are biological catalysts. They are compounds that facilitate chemical reactions. The orderly course of
metabolic processes is only possible because each cell is equipped with its own genetically determined set of enzymes. It
is only this that allows coordinated sequences of reactions (metabolic pathways). Enzymes are also involved in many
regulatory mechanisms that allow the metabolism to adapt to changing conditions. Almost all enzymes are proteins. The
name of the enzyme usually ends in –ase and is derived from the substrate that is affected by it.  For example, enzymes
that break down proteins are called proteases.   
The active site and functional groups of its amino acids may lower activation energy by: acting as a template for
substrate orientation, stressing the substrates and stabilizing the transition state, providing a favorable micro environment,
and participating directly in the catalytic reaction.
Reaction and substrate specificity  
Enzymes are catalysts. Catalysts are compounds that accelerate a reaction without being changed. Enzymes are
not destroyed or changed, but rather reused in the same chemical reaction over and over.  The compounds that enzymes
act upon are known as substrates.  Enzymes bind to an active site in the substrate and lower the energy needed for the
reaction to occur making it faster.  The energy required for a chemical reaction to occur is known as the activation
energy.  The substrates change to form a product. The action of enzymes is usually very specific. This applies not only to
the type of reaction being catalyzed (reaction specificity), but also to the nature of the reactants (substrates) that are
involved (substrate specificity). 

Figure 1. Representation of “lock-key” model for enzyme

An enzyme acts on a specific substrate to form an enzyme–substrate complex because of the fit between their
structures. As a result, something happens to the substrate molecule. For example, it might be split in two at a particular
location. Then the enzyme–substrate complex comes apart, yielding the enzyme and products. The enzyme is not
changed in the reaction and is now free to react again. Note that the arrows in the formula for enzyme reaction point both
ways (Fig. 1). This means that the reaction is reversible. An enzyme–substrate complex can simply go back to the
enzyme and the substrate. The products of an enzymatic reaction can react with the enzyme to form the enzyme–
substrate complex again. It, in turn, may again form the enzyme and the substrate. Therefore, the same enzyme may act
to cause a reaction to go either way. Some enzymes cannot function by themselves. In order to work, they must first be
attached to coenzymes. Coenzymes normally are not protein materials. Some of the vitamins are important coenzymes.
Enzyme classes

Class Description
oxidoreductases catalyze the transfer of reducing equivalents from one redox system to another.
transferases  catalyze the transfer of other groups from one molecule to another. Oxidoreductases and
transferases generally require coenzyme
hydrolases are also involved in group transfer, but the acceptor is always a water molecule
lyases  often also referred to as “synthases”;
catalyze reactions involving either the cleavage or formation of chemical bonds, with double bonds
either arising or disappearing.
isomerases  move groups within a molecule, without changing the gross composition of the substrate.
ligases are energy-dependent and are therefore always coupled to the hydrolysis of nucleoside
triphosphates.

GENERAL BIOLOGY 1
Quarter 1 – Module 8: 
BIOMOLECULES
Monomers & Polymers
• Macromolecules are actually ma
• de up of even smaller subunits. Each subunit of a macromolecule is called a monomer.
• The macromolecules themselves are called polymers, because they are made up of many of these subunits.
I. CARBOHYDRATES
Sources of Carbohydrates
a. Simple Sugars
b. Complex Carbohydrates
c. Dietary Fiber
Digestion and Absorption
Functions
Blood glucose regulation
Dietary sweeteners
Dietary Recommendations

- are an important source of energy.

- Has a monomer monosaccharide
- provide structural support for cells and help with communication between cells.
- Made up of CHO

Types of Carbohydrates
Simple Carbohydrates
– monosaccharides
– disaccharides
Complex Carbohydrates
– oligosaccharides
– polysaccharides
• glycogen
• starches
• fibers
1. Monosaccharides: Single Sugars
Glucose
– carbohydrate form used by the body, referred to as “blood sugar”
– basic sub-unit of other larger carbohydrate molecules
– found in fruits, vegetables, honey
Fructose
– sweetest of the sugars
– occurs naturally in fruits & honey, “fruit sugar”
– combines with glucose to form sucrose
Galactose
– combines with glucose to form lactose, “milk sugar”
2. Disaccharides
Sucrose (“table sugar”)
– glucose + fructose
Lactose (“milk sugar”)
– glucose + galactose
Maltose (“malt sugar”)
– glucose + glucose
Joining and Cleaving Sugar Molecules
 3. Complex Carbohydrates
a. Oligosaccharides
– short carbohydrate chains of 3 - 10 monosaccharides
– found in legumes and human milk
– Examples:
• raffinose
• stachyose
b. Polysaccharides
• long carbohydrate chains of monosaccharides linked by glycosidic bonds
– alpha (a) bonds (starch)
– beta (b) bonds (found in fiber)
b.1 Starch
– plant storage form of carbohydrate
– long branched or unbranched chains of glucose
• amylose
• amylopectin
b.2 Glycogen
– highly branched chains of glucose units
– animal storage form of carbohydrate
• found in LIVER and MUSCLE
• Humans store ~ 100g in liver; ~ 400g in muscle
– negligible source of carbohydrate in the diet (meat)
b.3 Fiber
Dietary Fiber
– non-digestible carbohydrates (chains of monosaccharides) and lignin that are intact and intrinsic in plants
(includes oligosaccharides)
Functional Fiber
– isolated, non-digestible carbohydrates that have beneficial physiological effects in humans
– dietary fiber found in all types of plant foods
– refining removes fiber from whole grains and other foods
– types of non-starch polysaccharides include:
cellulose
hemicelluloses
pectins
gums & mucilages
b-glucans
chitin & chitosan
lignans
 Digestion & Absorption
1. Mouth
• chewing
• salivary amylase
2. Stomach
• fibers remain in the stomach longer, delays gastric emptying
3. Small Intestine
• pancreas secretes enzyme pancreatic amylase
• enzymes located on the cell membranes of the intestinal epithelial cells complete digestion
• only monosaccharides can be absorbed
– glucose & galactose absorbed by ACTIVE TRANSPORT
– fructose absorbed by FACILITATED DIFFUSION
• all three monosaccharides travel in the portal vein to the liver
• three fates of glucose at the liver
– Energy, storage as glycogen, released to blood
4. Large Intestine
• resistant starches and fibers may be digested by bacteria
– produces short chain fatty acids
• absorbed by the intestine and used for energy (dietary fiber yields about 2 kcal/g)
• other health benefits (more later in semester)
Lactose Intolerance
• occurs as a result of insufficient lactase & low lactase activity
• lactose molecules from milk remain in the intestine undigested
• lactose intolerance ¹ milk allergy
• undigested lactose digested by bacteria producing irritating acid and gas
– symptoms include bloating, abdominal discomfort, diarrhea
• individuals who consume little or no milk products may be at risk of developing nutrient deficiencies
• dairy options: yogurt, aged cheddar, small quantities of milk (~ ½ cup), acidophilus milk, cottage cheese
• best to consume with other foods and spread intake throughout day
• gradual increases in milk intake may cause intestinal bacteria to adapt
Alternatives to Milk
1. Calcium
• canned fish with bones, bone soup stock, broccoli, cauliflower, calcium fortified beverages, blackstrap molasses
2. Vitamin D
• 15 minutes exposure to SUNLIGHT several times per week
• fortified margarine, fortified cereals, fatty fish (herring, tuna, salmon, sardines), fortified soy or rice milk
3. Riboflavin
• beef, chicken, liver, clams, mushrooms, broccoli, breads, fortified cereals
Functions of Carbohydrates
1) Energy
• glucose fuels the work of most of the body’s cells
– preferred fuel of NERVOUS TISSUE (the brain, nerves) and RED BLOOD CELLS (RBC)
• excess glucose is stored as GLYCOGEN in liver and muscle tissue
2) Sparing Body Protein
• if diet does not provide enough glucose, then other sources of glucose must be found
• if carbohydrate intake < 50 - 100 g, body protein will be used to make glucose
• an adequate supply of carbohydrate spares body proteins from being broken down to synthesize glucose
 3) Preventing Ketosis (Anti-ketogenic)
• carbohydrates required for the complete metabolism of fat
• incomplete fat metabolism produces KETONES
• an adequate supply of carbohydrate (> 50 – 100 g per day) prevents KETOSIS
Ketosis
• A metabolic state or process in order to keep our body working. When it doesn’t have enough carbohydrates from
food for your cells to burn for energy, it burns fat instead. As part of this process, it makes ketones.
Fiber
• beneficial for weight control by contributing to satiety & delay gastric emptying
• soluble fibers lower blood cholesterol to help reduce risk of cardiovascular disease
• minimizes risk of and helps control Type II Diabetes
• insoluble fibers help promote intestinal health by enlarging stool size and easing passage of stool
Soluble Fiber
• examples include gums, pectins, mucilages, some hemicelluloses
• functions:
– delay gastric emptying
– slow transit through the digestive system
– delay glucose absorption
– bind to bile, help decrease cholesterol
• food sources: fruits
Insoluble Fiber
• examples include cellulose, hemicellulose
• functions:
– speed transit through the digestive tract
– delay glucose absorption
– increase fecal weight and soften stool to ease passage
– reduces risk of hemorrhoids, diverticulitis and appendicitis
• food sources: cereal grains, legumes, vegetables, nuts
Excessive amounts of fiber may lead to:
– displacement of other foods in the diet
– intestinal discomfort
– interference with the absorption of other nutrients
Regulation of Blood Glucose
Optimal functioning of the body is dependant on keeping levels of glucose within certain parameters.
Elevated blood glucose = Hyperglycemia
Low blood glucose = Hypoglycemia
The ENDOCRINE SYSTEM is primarily responsible for regulating blood glucose. The two main hormones are
INSULIN and GLUCAGON.
Diabetes Mellitus
• a disorder of energy metabolism due to failure of insulin to regulate blood glucose
• results in hyperglycemia
• acute symptoms include thirst, increased urine production, hunger
• long term consequences include increased risk of heart disease, kidney disease, blindness, neural damage
• two forms: Type I and Type II
Type I
• accounts for about 10% of cases
• occurs when b cells of the pancreas are destroyed
– insulin cannot be synthesized
• without insulin, blood glucose levels rise because the tissues are unable to access the glucose
• death occurs shortly after onset unless given injections of insulin
Type II
• occurs when cells of body are unable to respond to insulin
• called “insulin insensitivity” or “insulin resistance”
• blood glucose levels rise
• insulin secretion increases in an attempt to compensate
– leads to hyperinsulinemia
Hypoglycemia
• dramatic drop in blood glucose
• symptoms similar to an anxiety attack: rapid weak heart beat, sweating, anxiety, hunger, trembling, weakness
• RARE in healthy people
• may occur as a result of poorly managed Diabetes or other causes:
– reactive hypoglycemia
– fasting hypoglycemia
The Glycemic Index
• a measure of the extent to which a food raises blood glucose concentration & elicits an insulin response
compared to pure glucose
Sugar
Intrinsic sugars
– from intact fruits & vegetables
Added sugars
– saccharides added to foods & beverages by manufacturer, cook, or consumer
Free sugars
– added sugars + concentrated sugars (i.e. from honey, syrups, and juices)
 Why is sugar added to foods?
– flavour enhancement
– provide texture and colour
– permits fermentation
– adds bulk
– acts as a preservative
– balance acidity
Dental Caries
Sugars, whether consumed from the diet or from complex carbohydrates partially digested in the mouth,
contribute to tooth decay.

PROTEINS
• Structural building blocks of cells in all tissues (not just muscle!)
• Polymers composed of 300 – 100k+ monomers
• Monomers are called amino acid
• There are 20 amino acids, many of which must come from your diet
• 50% dry weight of body
• Mammal cell contains 10,000 proteins
• Made up of CHONPS
• Proteins are found in meat, fish, legumes, nuts, milk, eggs, grains and soy products.
Protein Structure
• Primary structure – the order of amino acids making up the polymer string
• Secondary structure – helixes and sheets of the polymer string folding on itself
• Tertiary structure – globs of sheets and helixes folding around each other
• Quaternary Structure – individual proteins bound to each other to form a multi-protein unit with is own unique
function
Protein classification
A. Protein classification based on chemical composition
1. Simple proteins
• Also known as homoproteins, they are made up of amino acids. Examples are plasma albumin, collagen, and
keratin.
2. Conjugated proteins
• Sometimes also called heteroproteins, they contain in their structure a non-protein portion. Three examples
are glycoproteins, chromoproteins, and phosphoproteins.
B. Protein classification based on shape
1. Fibrous proteins
• They have primarily mechanical and structural functions, providing support to the cells as well as the whole
organism.
2. Globular proteins
• Most of the proteins belong to this class.
They have a compact and more or less spherical structure, more complex than fibrous proteins.
• Unlike fibrous proteins, that have structural and mechanical functions, they act as:
– enzymes;
– hormones;
– membrane transporters and receptors;
– transporters of triglycerides, fatty acids and oxygen in the blood;
– immunoglobulins or antibodies;
– grain and legume storage proteins.
C. Protein classification based on biological functions
• Enzymes (biochemical catalysts).
• Transport proteins
Many small molecules, organic and inorganic, are transported in the bloodstream and extracellular fluids,
across the cell membranes, and inside the cells from one compartment to another, by specific proteins.
• Examples are:
a. hemoglobin, that carries oxygen from the alveolar blood vessels to tissue capillaries;
transferrin, which carries iron in the blood;
membrane carriers;
fatty acid binding proteins (FABP)
• Storage proteins
Examples are:
ferritin, that stores iron intracellularly in a non-toxic form;
milk caseins, that act as a reserve of amino acids for the milk;
egg  yolk phosvitin, that contains high amounts of phosphorus;
prolamins and glutelins, the storage proteins of cereals.
• Mechanical support
Proteins have a pivotal role in the stabilization of many structures. Examples are α-keratins, collagen and
elastin. The same cytoskeletal system, the scaffold of the cell, is made of proteins.
• They generate movement
They are responsible, among others, for:
– the contraction of the muscle fibers (of which myosin is the main component);
the propulsion of spermatozoa and microorganisms with flagella;
the separation of chromosomes during mitosis.
– They are involved in nerve transmission.
An example is the receptor for acetylcholine at synapses.
 – They control development and differentiation.
Some proteins are involved in the regulation of gene expression. An example is the nerve growth factor
(NGF), discovered by Rita Levi-Montalcini, that plays a leading role in the formation of neural networks.
• Hormones
Many hormones are proteins.
They are regulatory molecules involved in the control of many cellular functions, from metabolism to
reproduction. Examples are insulin, glucagon, and thyroid-stimulating hormone (TSH).
Example: Hormone: Insulin
-Frederick Sanger (1940s, 50s), discovered the amino acid sequence of Insulin
-Causes cells to take up more glucose, and liver and muscle cells to create glycogen
-Diabetes is a deficiency of insulin
• Protection against harmful agents.
The antibodies or immunoglobulins are glycoproteins that recognize antigens expressed on the surface of
viruses, bacteria and other infectious agents.
Interferon, fibrinogen, and factors of blood coagulation are other members of this group.
• Storage of energy.
Proteins, and in particular the amino acids that constitute them, act as energy storage, second in size only
to the adipose tissue, that in particular conditions, such as prolonged fasting, may become essential for
survival.

LIPIDS
• Include a diverse group of compounds that are nonpolar in nature.
• Fatty compounds made of C H O, don’t interact with water (hydrophobic)
– Cell membranes are composed two lipid layers, which keep water from crossing
• Functions of lipids have include
• insulation of heat,
• storing energy
• protection
• dissolves fat-soluble vitamins
• cellular communication.
CLASSIFICATIONS
FATS AND OILS
WAXES
PHOSPHOLIPIDS
STEROIDS
Fats and Oils
• Fats and Oils Fat- consists of glycerol and fatty acids
• Glycerol- an organic compound (alcohol) with three carbons, five hydrogens, and three hydroxyl (OH) groups.
• Fatty acids have a long chain of hydrocarbons to which a carboxyl group is attached, hence the name fatty acid.
• Fats are also called triacylglycerols or triglycerides
• Examples are:
- Palmitic acid- a saturated fatty acid derived from the palm tree
- Arachidic acid- derived from Arachis hypogea
Classification of Fatty Acids
1. Saturated Fatty Acids- there are only single bonds between neighboring carbons in the hydrocarbon chain
- saturated with hydrogen
- example is stearic acid
- mammals store fats in specialized cells called adipocytes
- plants store fat and oil in their seeds and used as source of energy during seedling development
2. Unsaturated Fatty Acid- the hydrocarbon chain contains double bond
- Usually of plant origin
• Example: Oleic acid
• Liquid at room temperature and are called oils
a. Monounsaturated fat- there is one double bond in the molecule (e.g. olive oil)
b. Polyunsaturated fat- there is more than one double bond (e.g. canola oil)
Trans Fats
• In the food industry, oils are artificially hydrogenated to make them semi-solid and of a consistency
desirable for many processed food products.
• Margarine, some types of peanut butter, and shortening contains artificially hydrogenated trans fats.
• Recent studies have shown that an increase of trans fats may lead to an increase in levels of low-density
lipoproteins (LDL) or bad cholesterol.
• Could cause atherosclerosis
Omega Fatty Acids
• Essential fatty acids that could not be synthesized by the human body
• There are only 2: Omega-3 and Omega-6 Fatty Acids
• Omega-3 fatty acids- are polyunsaturated fatty acids and are called omega-3 because the 3 rd carbon from the end
of the hydrocarbon chain is connected to its neighboring carbon by a double bond.
• Reduce the risk of sudden death from heart attacks and may help reduce the risk of some cancers in animals
Examples of omega-3 fatty acids
• Alpha-linoleic acid (ALA)
• Eicosapentanoic acid (EPA)
• Docosahexanoic acid (DHA)

WAXES
• Made up of long fatty acid chains esterified to long chain alcohols.
 • Examples: feathers of aquatic birds and leaf surfaces of some plants
 
PHOSPHOLIPIDS
• phospholipid is the primary molecule found in the membranes of cells. 
• Lipids in water will arrange themselves to hide their hydrophobic tails
• Amphipathic
• Phosphatidylcholine and phosphatidylserine- phospholipids in our plasma membrane
STEROIDS
• Have fused ring structure
• All have four-linked carbon rings and several of them like cholesterol have a short tail
• Cholesterol- most common steroid
- mainly synthesized in the liver and is the precursor to many steroid hormones such as testosterone and
estradiol, which are secreted by the gonads and endocrine glands.
- also a precursor to Vitamin D and bile salts, which help in the emulsification of fats and their
subsequent absorption by cells.
- component of the plasma membrane
• Anabolic steroids are usually synthetic variants of testosterone
• Use of these substances
can cause serious health
problems

IV. NUCLEIC ACIDS

• The genetic material in any cell
– Deoxyribonucleic acid (DNA) and Ribonucleic acid (RNA)
• The monomers are called nucleotides
• Nucleic acid polymers are millions of monomers long, wound in a double helix
• Helix unwinds during replication (copying)
• Made up of CHONP
• Types of sugar bases:

Clas
sifications
1. DNA is the hereditary material passed on from parents to offspring
-Structure: double-stranded
• -Phosphate group
• -Sugar  deoxyribose
• -Bases 
– Cytosine – Guanine
– Adenine – Thymine
2. RNA
RNA-RiboNucleic Acid
-Structure: single-stranded
Basic units: nucleotides
Phosphate group
Sugar  ribose
Bases 
Cytosine – Guanine
Adenine – Uracil
Three Types of RNA
Messenger RNA (mRNA)
• copies DNA’s code & carries the genetic information to the ribosomes
Transfer RNA (tRNA)
• transfers amino acids to the ribosomes where proteins are synthesized
Ribosomal RNA (rRNA)
• along with protein, makes up the ribosomes

Protein Synthesis
1. Transcription
-the mRNA copies the code from the DNA
Codon- series of 3 consecutive nitrogenous bases of mRNA; codesfor amino acid

2. Translation
- The code copied by the mRNA will be translated by the tRNA in the ribosome
- The tRNA has attached with it the amino acid
- Anticodon- complementary pair of the codon in the tRNA