Thermoregulation

Processes that may move heat into and out of an organism

- Convection : the upward flow of warm air or the downward flow of cold air past he body
- Radiation : from a body to a colder object not in contact; the heat is transferred by
infra-red waves
- Conduction : from the hotter to the colder of the two surfaces in contact
- Evaporation : the change of liquid to vapour, due to the presence of latent heat, has a
marked cooling effect

Structure of human skin :

CAPILLARY MUSCLES
In warm conditions : vasodilation of skin arteriole (refers to arteriole NEAR THE SKIN)
- By-pass arteriole constricts, the skin arteriole dilates, more blood flows to the skin
surface when the body needs to lose heat.
In cold conditions : vasoconstriction of skin arteriole
- By-pass arterioles dilate, skin arteriole constricts, less blood flows to skin surface when
body needs to retain heat

HAIR ERECTOR MUSCLES

In warm conditions : hair erector muscles relax when heat loss must be increased, allows a
current of air to flow over skin, increasing heat loss

In cold conditions : Hair erector muscles contract to trap a layer of ​STILL​ air above skin in order
to limit heat loss
SWEAT GLANDS
Sweat gland produces sweat when the body needs to lose heat, but does not when the body
needs to retain heat. The evaporation of sweat results in heat loss through the latent heat of
vaporization. (Heat that is lost through a change in state of the swear, but does not change skin
temp.)

SHIVERING
Produces heat in the human body
1. Body experiences a sudden loss of heat
2. Shivering occurs, defined as the non-coordinated contraction of skeletal muscles
3. Raising muscle heat production about five times above basal rate
The Nervous System

Neurons are specialised nerve cells organised into central nervous system (brain + spinal cord)
and peripheral nerves linking to sense organs, muscles and glands with the brain or spinal cord
Input (stimuli) → receptor (detected by) → Control Centre → Effector (initiates response) →
Output (may lead to negative feedback loop)

IN THE BRAIN
internal/external stimuli → receptors (sense organs) → impulses transmitted by the neurons of
the nervous system/coordination of responses by the brain → effector neurons (e.g. muscles,
glands) → responses (leads to feedback information and subsequent internal stimuli)
Neurons :
1) Motor neuron
a) Function : to transmit impulses from central nervous system to effector organs
such as muscles or glands
2) Relay neuron
a) Function : to relay impulses from sensory neurons to motor neurons
b) Dendron and axon cannot be distinguished for this neuron
3) Sensory neuron
a) Function : to transmit impulses from receptors to spinal cord or brain (central
nervous system)
b) Dendrites → one side connects to sensory receptors (e.g. thermoreceptor) and
the other end connects to central nervous system
Neuron parts
- Cell body + nucleus (Soma)
- Dendrites
- Branched projections on neurons that receive electrical messages
- Axon (long rod-like projections of cell)
- Carries nerve impulse ​away​ from cell body
- Dendron (long rod-like projections of cell)
- Carries nerve impulse ​towards​ the cell body
- Node of Ranvier
- A gap in the myelin sheath of a nerve
 - Allows electrical impulses to move more quickly down the axon → allow for ions
to diffuse in and out of neuron, propagating the electrical signal down the axon
- Myelin sheath
- Insulation layer of protein and fatty substances to allow electrical impulses to
transmit quickly and efficiently
Synapses​ - the junction between neurons
Transmission occurs by particular chemicals, known as transmitter substance. These
substances are all relatively small, diffusible molecules. They are produced by the Golgi
apparatus and held in tiny vesicles before use.
Reflex arcs
Stimulus (e.g. mechanical pressure) → receptor (e.g. sensory organs) → sensory neuron →
relay neuron → motor neuron → effector (e.g. muscle)
How does reflex arc work?
- The action begins when the receptors on a sense organ detect a stimulus (an increases/
decrease in temperature)
- Becomes a nerve impulse transmitted by a sensory neuron to the spinal cord
- In the spinal cord, the nerve impulse is transmitted to the relay neuron, and then to the
motor neuron
- The motor neuron transmits the impulses from the spinal cord to the effector
- When it arrives at the effector, the impulse causes a response - for example. It may
cause a hair erector muscle to contract for a sweat gland to secrete sweat

1) Sensation
a) Receptor (skin) → sensory neuron → relay neuron (spinal cord) → forebrain
2) Voluntary action
a) Forebrain → relay neuron (spinal cord) → motor neuron → effector
3) Involuntary action (reflex action)
a) Receptor → sensory neuron → relay neuron (brain or spinal cord) → motor
neuron → effector
Eyes
PUPIL REFLEX
In bright light :
1) The circular muscles of the iris contract (circular)
2) The radial muscles of the iris relax (straight lines)
3) The pupil becomes smaller or ​constricted​. This reduces the amount of light entering the
eye.
In dim light :
1) The radial muscles of the iris contract
2) The circular muscles of the iris relax
3) The pupil enlarges or dilates. This increases the amount of light entering the eye.

Nervous pathway in pupil reflex :

Stimulus (change in light intensity) → receptor (retina) → sensory neuron in optic nerve → brain
→ motor neuron → effector (iris)

HOW DO WE SEE
1) The light rays are refracted through the cornea and the aqueous humour onto the lens
2) The lens causes further refraction and the rays are brought to a focus on the retina
3) The image on the retina stimulates either the rods or the cones, depending on the
intensity of the light. The image formed on the retina is
i) Upside down (inverted)
ii) Laterally inverted
iii) Diminished (smaller size that the actual object)
Focusing (AKA accommodation)
- Adjustment of the lens of the eye so that clear images of objects at different distances
are formed on the retina
- During focusing, the thickness or curvature of the lens is adjusted to focus light rays on
the retina

Focusing on distant objects (~7m ≥)

1) Ciliary muscles ​relax​, pulling on the suspensory ligaments

2) The suspensory ligaments become ​taut​, pulling on the edge of the lens
3) Lens become ​thinner and less convex​, ​increasing​ ​its focal length​ (focal length -
distance between the middle the lens and the point focus on the retina)
4) Light rays from the distant object are ​sharply focused​ on the retina
5) Photoreceptors​ are stimulated
6) Nerve impulses​ are transmitted by the ​optic nerve to the brain​. The brain interprets
the impulses and the person sees the distant object.
Focusing on near objects
1) Ciliary muscles ​contract​, relaxing their pull on the suspensory ligaments
2) Suspensory ligaments ​slacken​, relaxing their pull on the lens
3) The lens, being ​elastic​, ​becomes thicker and more convex​, ​decreasing its focal
length
4) Light rays from the near object are​ sharply focused​ on the retina
5) Photoreceptors​ are stimulated
6) Nerve impulses are transmitted by the ​optic nerve to the brain​. The brain interprets the
impulses and the person sees the near object.
OTHER INTERNAL STRUCTURES OF EYE
Blind spot
- Small portion of the eye that corresponds to the position of the optic disk, there are no
photoreceptors in the optic disk, resulting in a blind spot
Fovea
- Provides clearest vision in eye
- Cones are concentrated mostly in and near the fovea, however there are no rods
Sclera
- White outer layer of eyeball
Vitreous humour
- The main difference between the vitreous humor and the aqueous humor is that there is
a set amount of the vitreous humor in your eye, and it does not move.
Aqueous humour
- Function :
- Allow the cornea to expand, so it can protect the eye against dust, particles, and
bacteria that can cause harm.
- Preserve ocular pressure.
- Transport nutrients, including vitamin C.
Cones vs rods (photoreceptors)
- Rods are responsible for vision at low light levels (scotopic vision). They do not mediate
color vision, and have a low spatial acuity. Cones are active at higher light levels
(photopic vision), are capable of color vision and are responsible for high spatial acuity.
Biomolecules
ORGANIC COMPOUNDS
- Compounds built from carbon and hydrogen
- In living things, carbon is the third most abundant element by mass, after oxygen
- Then organic compounds to form macromolecules

MACROMOLECULES
- Polysaccharides and proteins​ are macromolecules
- Chemically we describe them as ​polymers
- Made by linking together similar building blocks called ​monomers
- Examples :
- Proteins (polymer) are built from amino acids (monomers)
- Polysaccharides (polymer) from monosaccharide sugars (monomers)
Formation
- Monomers are linked together by a reaction in which a water molecule is removed =
condensation reaction
- The bonds between monomers are ​covalent bonds
- The reverse reaction requires water and releases individual monomers again
(​hydrolysis reaction​)

BIOMOLECULES : CARBOHYDRATES
- Largest group of organic compounds (sugars, starch, glycogen, cellulose)
- 3 elements : Carbon, Hydrogen, Oxygen
- General formula : C​x​(H​2​O)​y
- Side Notes
- R = reducing sugar
- NR = non-reducing sugar
- Reducing sugars act as a reducing agent and compounds while non-reducing
sugar cannot reduce compounds
Roles of carbohydrates
= different carbohydrates are needed by living organisms
- Glucose = ​substrate for cellular respiration​ to produce ATP energy
- Cellulose = to form ​supporting structures​ like cell wall in plants
- Glucose = ​can be converted into other organic compounds ​such as amino acids and
fats in humans
- Deoxyribose = for the ​formation of nucleic acids​ in DNA (important component in
nucleotides)

MONOSACCHARIDES
- Smallest building blocks for different carbohydrates (monomers)
- Properties : they taste sweet and are soluble in water, ​all monosaccharides are
reducing sugars
- Examples :
- Glucose (C​6​H​12​O​6​) is
important. Our body
transports glucose in
the blood and all cells
to use for cellular
respiration
- Fructose is also found
in fruits
- Include :
- Glucose (R) = C​6​H​12​O​6
- Galactose (R) =
C​6​H​12​O​6​ (differs from
glucose in one hydroxyl group)
- Fructose (R) = C​6​H​12​O​6
DISACCHARIDES
= carbohydrates made of two monosaccharides combined together
- Properties : soluble in water
- Examples :
- Sucrose = glucose + fructose
- Lactose = glucose + galactose
- Maltose = glucose + glucose
- A molecule of water is removed when two monosaccharides combine, so this reaction is
called a ​condensation reaction
- The bond formed between monosaccharides is a ​glycosidic bond
Sucrose is not a reducing sugar
- An important sugar (table, regular sugar)
- Transported in phloem from leaves to stems/roots/carbohydrate storage sites
- The ‘sugar’ humans prefer to use in foods and drinks, mostly extracted and
purified from sugar cane
Maltose
- Found in germinating barley
- Starch can be reduced to maltose
Lactose
- Found in milk

POLYSACCHARIDES
- Polysaccharides are built from many monosaccharide molecules condensed together
- Properties : insoluble
- Examples : starch, cellulose, glycogen

Starch
 - Made of ​amylose​ chain and ​amylopectin​ chain
- Each chain has thousands of ​glucose molecules
1. Each chain forms a ​helix​ molecule, which makes the molecules ​compact and insoluble
2. Water potential of cell is not changed and can be stored in cells
3. Major storage carbohydrate in most ​storage organs​ of ​plants
4. Can be ​broken down to form glucose readily​ to provide energy

Complex Structure Role Occurrence

carbohydrate

Starch Made up of several Form of storage in plants. Found in ​storage

thousand glucose When needed, can be organs​ of plants
molecules digested to glucose to (potato tubers and
(​amylopectin​ and provide energy tapioca)
amylose​ chains) joined
together

Cellulose Made up of many Cellulose cell wall ​protects Present in ​cell

glucose molecules but plant cells from bursting or walls​ of plants
glycosidic bonds damage. It ​cannot be
formed between digested​ in our intestines
glucose units are and serve as ​dietary fibre
different​ from starch that prevents constipation

Glycogen Is a ​highly branched Form of storage in mammals. Stored in the ​liver

molecule made up of When needed, can be and ​muscles​ of
many glucose digested to glucose to mammals
molecules provide energy.
FOOD TESTS
Iodine test
- Test for ​starch
- Add ​Iodine-KI​ reagent to a solution or directly on a potato or other materials such as
bread, crackers, or flour. A ​blue-black​ color results if starch is present. If starch amylose
is not present, then the color will stay ​orange or yellow​.

Biuret test
- Detects ​peptide bonds​ → test for ​protein
- An aqueous sample is treated with an equal volume of 1% strong base (sodium or
potassium hydroxide) followed by a few drops of aqueous copper(II) sulfate. If the
solution turns purple, it contains protein. If not, it will remain blue.

Benedict’s test
- Identifies reducing sugars (simple carbs)
1) Approximately 1 ml of sample is placed into
a clean test tube.
2) 2 ml (10 drops) of Benedict’s reagent
(CuSO4) is placed in the test tube.
3) The solution is then heated in a boiling water
bath for 3-5 minutes.
4) Observe for color change in the solution of
test tubes or precipitate formation.
Ethanol emulsion
- Identifies presence of lipids
- The procedure is for the sample to be suspended in ethanol, allowing lipids present to
dissolve (lipids are soluble in alcohols). The liquid (alcohol with dissolved fat) is then
decanted into water. Since lipids do not dissolve in water, when the ethanol is diluted, it
falls out of the solution to give a cloudy white emulsion.

BIOMOLECULES : LIPIDS

- Elements : contain C, H, O
- Insoluble in water (hydrophobic property)
- Soluble only in organic solvents (alcohol, propanone, ether)
- Animal fats (solid) and plant oils (liquid)
- Phospholipids in cell membranes
- Steroids (growth and sex hormones)
 - Waxes in plants and animals
- Formed by condensation reactions (removal of water molecule) between fatty acids and
glycerol
- 3 fatty acid molecules + 1 glycerol molecule = triglyceride
- Fats and oils are both the same structurally except
- Oils: liquid
- Fats : solid

TRIGLYCERIDES
- Large molecules but smaller than glycogen or starch
- Hydrophobic properties make them clump together → appears as a macromolecule
- Ester bonds​ (a carbon bound to three other atoms) are formed in the production of
triglycerides (formed by ​condensation reaction​)
- Saturated fatty acids : ​no double bonds​ (bad for health)
- Unsaturated fatty acids : ​one or more double bonds​ present (-C=C-)
- Polyunsaturated : when several double bonds are present
- Trans Fat (bad for health)
ROLE OF FATS AND OILS
1) Mass for mass, ​fats and oils release more than twice as much energy​ as
carbohydrates
a) Fats form a ​concentrated, insoluble energy source
2) Concentrated food reserves for long unfavourable seasons
3) Complete oxidation ​produces large amounts of metabolic wate​r (water created inside
organism through metabolic processes)
a) Helps animals to survive when there is little drinking water available
b) Development of embryos of birds and reptiles
4) Buoyancy aid​ (presence of adipose tissue: loose connective tissue, fat) and ​heat
insulation layer
5) Oils act as ​waterproofing​ for hair and feathers
6) Electrical insulation​ (around nerve cells)

PHOSPHOLIPIDS
- Similar to triglycerides except ​one of the fatty acids is replaced by phosphate group
- Phosphate group is ​ionised​ and therefore ​water-soluble​ (hydrophilic property)
- 2 fatty acid tails + 1 glycerol molecule + 1 phosphate group = phospholipids
PROPERTIES OF WATER
- Has ​highly specific heat capacity
- Allows for large/bulky organisms to have ​stable​ temperatures
- High ​latent heat of vaporization
- Allows for ​evaporation​ as a mechanism for ​cooling
- Water serves as the ​universal solvent​ in biological systems. Allows for ​chemical
reactions​ to take place. Is a key component of tissues (tissue fluid, digestive juices,
blood) it also helps ​transport dissolved substances
- Highly cohesive​ water molecules. Allows water to be drawn up narrow columns such as
xylem vessels

Property Benefit to life

A liquid at room temperature, water dissolves Liquid medium for living things and for the
more substances than any other common chemistry of life.
liquid.

Much heat energy is needed to raise the Aquatic environments are slow to change
temperature of water. temperature. Bulky organisms have stable
temperatures.

Evaporation requires a great deal of heat. Evaporation causes marked cooling. Much
heat is lost by the evaporation of a small
quantity of water.
 Water molecules adhere to surfaces. Water
column does not break or pull apart under
tension.
Water adheres to the walls of xylem vessels
as it is drawn up the stem to the leaves from
the roots. Water can be lifted by forces
applied to the top, and so can be drawn up
the xylem vessels of a tree trunk by forces
generated in the leaves.

BIOMOLECULES : PROTEINS
TYPES
- Structural proteins → fibrous proteins (e.g. collagen of skin and bone, keratin of hair)
- Enzymes → biological catalysts of organelles and cytosol
- Muscle/movement proteins → e.g. myosin and actin of muscle myofibrils
- Transport proteins → e.g. haemoglobin of red blood cells
- Defense against disease proteins → antibodies (immunoglobulins) secreted by
B-lymphocytes
- Protein of membranes → part structural also as enzymes, pumps and receptors

- Defense
- Transport
- Communication
- Storage
- Enzymes
- Structure

COMPOSITION
- Amino acids contains C, H, O, N and S
- Proteins formed from many ​amino acids​ joined together in a long chain
MONOMER : AMINO ACIDS
- Components
- Carboxyl group (acidic) → O=C-OH
- Amino group (basic) → H​2​N
- Alpha carbon
- Side chain (R-groups)
- Only group that varies and determines protein’s shape and function
- Hydrophobic amino acids → carbon rich side-chains, does not interact well with water
- Hydrophilic amino acids → forms hydrogen bonds, interacts well with water)
- Charged amino acids → react well to oppositely charged amino acids or to other
molecules

POLYPEPTIDES (polymer)
- Peptide bond​ forms when 2 amino acids react together (removal of water molecule) →
condensation reaction ​(between amino and carboxyl groups)
 - Four different levels of structural organisation
- All proteins will have primary, secondary and tertiary structures
- Only some proteins have quaternary structures (those made up of more than one
polypeptides)
- Our focus in on the tertiary structure

PRIMARY STRUCTURE
- Proteins are made up of polypeptide chains,
which are amino acids joined together with
peptide bonds (links amino group to
carboxyl group)
- The unique sequence of amino acids that
make up a polypeptide chain is called the
primary structure

SECONDARY STRUCTURE
- After synthesis, parts of the polypeptide
chains are folded into their secondary
structure
- Two common examples of secondary
structures are ​alpha helices​ (s: helix) and
beta pleated sheets
- Secondary structure is held together by
many ​hydrogen bonds
TERTIARY STRUCTURE
= Proteins with a 3D structure fall into two main types
- Fibrous​ → long fibres and are insoluble in water, they usually have structural roles, such
as:
- collagen in skin, bone and cartilage
- keratin in fingernails and hair
- Globular​ → more spherical structures, they are soluble proteins and usually have
metabolic roles
- Enzymes, haemoglobin and antibodies in mammals
QUATERNARY STRUCTURE
- Quaternary structure is formed when two or more polypeptide chains join together,
sometimes with an inorganic component, to form a protein
- Not all the proteins will have quaternary structures
DENATURATION OF PROTEIN
- Loss of three-dimensional structure of a protein and protein will lose their original
function without the correct 3D structure
- Different bonds that maintain the 3D structure are changed
- Exposure to heat or increase in temperature beyond a certain temperature break the
hydrophobic interactions, hydrogen and ionic bonds between the R-groups of amino acid
residues
- Small changes in pH of the medium alter ionic changes and will break hydrogen and
ionic bonds

ENRICHMENT : GLUTEN
- Gluten is a general name for the proteins found in wheat
- Gluten triggers an autoimmune response in some people that attacks the lining of the
small intestine
- The body cannot absorb nutrients into the bloodstream properly, leading to
anemia, delayed growth, and weight loss, among other things

ENRICHMENT : ARTIFICIAL SWEETENERS

- Artificial sweeteners such as aspartame and saccharin, are chemicals that have been
chemically synthesised to replace sugar.
- By offering the taste of sweetness without any calories, artificial sweeteners seem like
they could be one answer to effective weight loss.
- However, there might be unwanted side-effects associated with them.

ENRICHMENT : CARB AND FAT BLOCKERS

- Carbohydrate and fat blockers are substances that prevent the absorption of
carbohydrates and fats
- These nutrients will not be stored in the body as fats, thereby preventing weight gain.

BIOMOLECULES : ENZYMES
= globular proteins that catalyse thousands of metabolic reactions
- Metabolism is the name given to chemical (metabolic) reactions of life. Molecules
involved are called metabolites.
- These reactions can be classified as :
- Anabolic​ reactions = larger molecules are built up from smaller molecules
- Catabolic​ reactions : larger molecules are broken down (e.g. digestion)
- Some enzymes are secreted and worked externally - ​Extracellular​ enzymes (e.g.
digestive enzymes)
- Many enzymes remain ​within​ the cells - ​intracellular​ enzymes. They are found inside
organelles, in the membranes of organelles, in the cytosol and in the cell membrane.

BIOLOGICAL CATALYST
- A catalyst is a molecule that ​speeds up a chemical reaction​ but ​remains unchanged
at the end of a reaction.
- For reactions between two molecules to occur, there must be an ​effective collision
between them. The molecules must collide with each other in the ​right way​ at the r​ ight
speed​.

- Enzymes are biological catalysts made of protein. They speed up the rate of a chemical
reaction.
- Required in small amounts.
- Remain unchanged at the end of the reaction.
- Many enzymes are always present in cells and organisms but some enzymes are
produced only under particular conditions or at certain stages.
- By making some enzymes and not others, cells can control what chemical reactions
happen in the cytoplasm.
 - Many enzymes have a name based on the name of their substrate catalysed. (e.g.
lactase hydrolyses lactose)

CHARACTERISTICS
1. They are biological catalysts - they speed up the rate of a chemical reaction
2. They are required in small amounts.
3. They remain unchanged at the end of the reactions.
4. They are specific in action.
5. They are affected by temperature and pH.

ENZYMES LOWER THE ACTIVATION ENERGY

1) As molecules react, they become unstable, high energy intermediates (momentarily).
a) They are in a ​transition​ state because the products are formed immediately.
2) Products have a lower energy level than the substrate molecules.
3) Energy is needed to raise molecules to a transition state and the minimum amount of
energy needed to do so is activation energy. It is an energy that has to be overcome
before the reaction can happen.
4) Enzymes work by ​lowering the activation energy​ required to activate the reacting
molecules.

ENZYMES ARE HIGHLY SPECIFIC

 - Enzymes are highly specific in their action.
- They catalyse only one type of reaction or only a very small group of very similar
reactions.
- Each chemical reaction inside a cell is catalysed by a unique enzyme.
- Enzyme specificity depends on the active sites.
- This is because the active site where the substrate molecules bind has a precise shape
and distinctive chemical properties. Only substrate molecules complementary to the
shape of the active site can fit.
- Active sites are depressions on the surface of an enzyme that fits the shape of
specific substrate molecules.
- An enzyme is specific due to the unique 3D shape at the active site.

LOCK & KEY HYPOTHESIS

- In a reaction catalysed by an enzyme, the starting substance is called substrate. It is
converted to the product.
- The substrate binds to the enzyme at its active site.
- This concept is referred to as the “lock and key hypothesis”.
- The substrate is the key and the enzyme is the lock.
- As the enzyme and substrate form a complex (E-S), the substrate is raised in energy to
a transition state and then breaks down into products (Pr) plus unchanged enzyme.

KEY STEPS FOR ENZYMATIC REACTION

1) The shape of the active site of the enzyme is ​specific and complementary​ to the shape
of the substrate. Upon ​effective collisions​ between enzyme and substrate, the
enzyme-substrate complex​ is formed.
2) Interactions between ​enzyme and substrate​ molecules​ strain/weaken chemical
bonds within substrates​. Thus, ​lowering activation energy​.
 3) When reactions between substrates finish, products ​no longer fit​ into the active site and
are ​released​. Enzymes are released.

FACTORS AFFECTING ENZYME REACTION

- Temperature
- pH
- Substrate concentration

TEMPERATURE
Observation from graph : For every 10°C rise in temperature, the rate of enzyme reaction is
doubled​ until the ​optimum​ temperature is reached.
- Enzymes are ​inactive​ at low temperatures, due to l​ ow kinetic energy​, the ​frequency
of effective collisions is low​.
- As temperature increases, ​kinetic energy​ of the substrate and enzyme molecule
increases, thereby ​increasing the frequency of effective collisions​ between
substrates and enzyme active sites, which
 - Increases the rate of formation of enzyme-substrate complexes​ and ​increase​ the
rate of reaction/products formed.
Observation from graph : enzyme activity is highest at its optimum temperature of 35-40°C
- Every enzyme has an ​optimum​ temperature at which it is most active.
- Not all enzymes have the same optimum temperature.
Observation from graph : when temperature is increased beyond the optimum temperature of
40°C,
- High temperatures ​break the bonds that keep the enzyme protein in its specific
shape​. (hydrogen, ionic, hydrophobic interactions)
- The active site​ loses its original shape and is no longer complementary​ to the
substrate.
- The enzyme is ​denatured​ and ​loses its catalytic function​.
- The rate of denaturation increases at higher temperatures.
pH
- Each enzyme has an ​optimum​ pH in which it functions most efficiently. Rate of reaction
is at a maximum.
- Enzyme ​maintains its specific 3D conformation​ and so the enzyme active site is
complementary​ to the substrate
- Enzyme binds the substrate to​ form the enzyme-substrate complex​. Substrate is
converted to products​.

Changes in pH can affect enzyme activity.

- Structure of the protein is maintained by various bonds. Changes in pH ​alter the
bonding pattern​ (usually of ionic and hydrogen bonds), thereby ​altering the 3D
conformation/shape of the active site​ of the enzyme.
- Hence, the substrate is ​no longer complementary​ to the active site. ​No
enzyme-substrate can be formed​, no product is formed.
- The enzyme is ​denatured and loses its catalytic function​.
- Effects of pH on active sites are normally reversible (unlike temperature changes),
provided it is not too extreme.

Substrate concentration
- At lower concentrations, the rate increases in direct proportion to the substrate
concentration.
 - All molecules can find an active site without delay. Effectively, there is excess
enzyme present.
- Rate of reaction is set by how much substrate is present. As more substrate is
available, the rate of reaction increases.
- But at higher substrate concentrations, the rate of reaction becomes constant, showing
no increase.
- More substrate molecules than enzyme molecules.
- Substrate molecules have to ​wait​ for access to an active site.
- No increase in the rate of reaction.