GEN BIO MODULE 7  Whey-by-product

 Lactase-enzyme necessary to break down

C, O, N, P, S, H- common set of chemicals in all
lactose
organisms; build larger and more complex molecules
 Lactose intolerant- do not produce enough
Biomolecules-organic molecules/macromolecules lactase to digest lactose
 MALTOSE-MALT or BEER SUGAR); two
-fuel for metabolism; their chemical composition and
glucose; least sweet
quantity are important for cellular activities
 POLYSACCHARIDES- at least three
Carbohydrates- most abundant of all organic monosaccharides; not sweet; don’t form
compounds crystals; used for energy storage
 LINEAR POLYSACCHARIDES- rigid structure;
 -“hydrated carbon”
insoluble
 -include simple and complex SUGARS
 BRANCHED POLYSACCHARIDES-soluble
 -great source of energy; best taken in the
 Starch(energy storage of plants) and
beginning of the day
Glycogen(animals)- composed of chains of
 MONOSACCHARIDES-simple sugar;
glucose molecules
monomers(single structural unit)
 PECTIN-soluble fiber
 -provide immediate energy because they
 CELLULOSE-found in cell wall; most
are smaller than other types of carbs.- can
abundant organic molecule on Earth;
immediately be absorbed through the
cannot be digested(except for cows and
digestive tracts all the way to the
horses)
bloodstream
 CHITIN- in cell walls of fungi; has
 -aldose(presence of aldehyde) or
antibacterial properties
ketose(carbonyl or ketone group located at
the SECOND carbon atom) Lipids-contains hydrocarbons; insoluble in water; long-
 Carbonyl + hydroxyl(aq)= cyclic term energy storage; serve as insulation
compound(hemi-acetal/-ketal)-water-
soluble crystalline solid  TRIGLYCERIDES- FATS; contain a glycerol
attached to three fatty acids
 -classified according to no. of carbon atoms:
 Fatty acid- long chain of carbon atoms
 Dioses- two C atoms
connected to a carboxylic acid(-COOH)
 Pentose(5 C atoms)-includes ribose found in
 SATURATED-single bonds in the fatty acid
RNA
chain; normally sold at room temp.; animals
 Glucose (hexose)-major source of energy
 UNSATURATED- “oils”; one or more double
for all organisms
bonds; normally liquid at room temp.;
 Fructose—found in most plants(sugarcane,
plants
sugar beets, corn); enhance taste
 PHOSPHOLIPIDS- lipids with phosphate group;
 Ascorbic acid- from glucose
hydrophilic head and hydrophobic tail maintains
 Sugary foods, fructose-rich fruits- best
the function of the plasma membrane
sourceof energy for people who are drained
 STEROIDS-four fused carbon rings; regulating
or tired
metabolism, immune response, reproduction
 DISACCHARIDES-two monosaccharides joined
 CHOLESTEROL-sterol (steroid alcohol)
through CONDENSATION
 TESTOSTERONE-male sex hormone;
REACTION(dehydration synthesis takes place-
synthesized from cholesterol in the testes
water is extracted, forms glycosidic bond-links a
 PROGESTERONE and
carbohydrate to another molecule)
ESTROGEN(ESTRADIOL)-female hormone
 -sweet and soluble in water
controlling ovulation cycle; cholesterol in
 SUCROSE-TABLE SUGAR; fructose + glucose
the ovaries
 LACTOSE-MILK SUGAR; glucose + galactose;
dairy products
  ADRENOCORTICOID HORMONES-in the  mRNA- messenger RNA; temporary
adrenal gland; ex: aldosterone- copy of a gene in the DNA that directs
reabsorption of sodium and chloride, the sequence of aminoacids during
cortisol- glucocorticoid regulation of energy protein synthesis
reserves in the body;remove fatty acids  tRNA- transfer RNA; translates the
form the lipid storage sequence of nucleic acids in a gene to
 WAXES-esters; alcohol and fatty acids; create the correct sequence of amino
extremely hydrophobic acids
 CERUMEN- earwax; prevents entry of some  rRNA-ribosomal RNA-forms peptide
materials to the ear canal bonds between amino acids
 ATP-adenosine triphosphate- adenine and three
Protein-most diverse; building blocks of life; composed
phosphate group; highest source of energy in
of chains of amino acid
cells; last two phosphate bonds are unstable
 AMINO ACIDS-Amino(-NH2), acid group(-COOH) and can easily be broken; muscle contraction
and R group; plants are capable of making and nerve impulse
amino acids for themselves
MODULE 8
 ESSENTIAL A.A. – cannot be produced by
our bodies Cellular operations- accomplished through the
 NONESSENTIAL- produced by our bodies biochemical reactions that take place within the cell
 CONDITIONAL- not vital but may become
METABOLISM- series of chemical reactions that
urgent
converts food into energy; helps maintain the
 PEPTIDE BOND-when a carboxyl group
characteristics of life- growth, reproduction, repair and
reacts with an amino group from another
response; connected to nutrition and the availability of
molecule
nutrients
SHAPES
Factors that may influence metabolic process age,
 Primary- simplest; linear sequence of amino gender and weight
acids in a peptide chain
 Secondary- 3D shape created by several
hydrogen bonds; fibrous proteins
 Tertiary- 3D shape of a peptide; can be
fibrous or globular; determined by the
interaction of the side chains of the
different amino acids in the peptide
 Quaternary- proteins havemore than one
polypeptide

Nucleic acid- largest; composed of nucleotides

(nitrogenous base, fve-carbon sugar, and a phosphate
group; contains gentic information
 -both have 4 nucleotides with a single base
ring(pyrimidine) and double ring( purine)
 DNA- deoxyribonucleic acid; double stranded
helix with base pairing(AGTC); long molecule
that contains coded instructions for cellular
activities; has pentose sugar(deoxyribose)
 RNA-ribonucleic acid; single stranded(AGTU);
for encoding to decoding and regulating of
genes; pentose sugar(ribose)
CATABOLISM- breaking down of molecule to release
energy; energy released is stored in ATP for anabolic
reaction
 Breakdown of polysaccharides to
monosaccharides to generate energy
 Breakdown of nuclei acids to nucleotides for
transmitting genetic information
 Breakdown of proteins into amino acids to
make new ones or to produce glucose
  Breakdown of food in the stomach for the
nutrients to be absorbed into the blood vessels
ANABOLISM- building things; requires and consumes
energy; fueled by catabolism; powered by the use of
ATP molecules
 Building proteins
 Cell reproduction
 Mineralization of bones
 Production of hormones
ENZYMES- organic catalyst; organized mechanisms
regulating and controlling the metabolic pathways;
speed up the processes in chemical reaction
-catalyze SPECIFIC REACTIONS
Typical enzyme- apoenzyme(protein) and
cofactor(nonprotein)
Apoenzyme- can be called proenzyme when it is
inactive(not attached to any substance or the enzyme in
its original form); intra and intermolecular bonds that
are in secondary and tertiary structures
-shape can be disrupted by changes in temp and pH
Cofactor- assist apoenzyme
METAL ION ACTIVATORS- not permanently bound to the
apoenzyme; positive charges to the enzyme through
covalent bonding; Mg, Zn, Mn, Na, Fe, K, Cu
COENZYMES-organic molecules that usually come from
the vitamins; temporarily bind to apoenzymes
PROSTHETIC COFACTORS- either metal ions or organic
molecules; bind to apoenzymes permanently
VITAMINS AS ENZYME COFACTORS
 B1-THIAMINE
 B2-RIBOFLAVIN
 B6-CYANOCOBALAMIN
 B3-NIACIN(NICOTINIC ACID)
 B5-PANTOTHENIC ACID
 BIOTIN
 FOLIC ACID
 VITAMIN C
 VITAMIN E
 VITAMIN K
*NOT ALL ENZYMES ARE PROTEINS
Ribozymes- synthesize the proteins in the ribosomes of
cells; catalytic RNA
ACTIVATION ENERGY-amount of energy required to
stimulate the reaction
-term coined by Svante Arrhenius(1889) to describe the
minimum amount of energy needed to start any
chemical reaction
-essential to control the spontaneous degradation of
molecules within the cell
*enzymes do not affect the amount of energy of the
reaction products or reactants. They only LOWER their
activation energy
Substrates- reactants in an enzymatic reaction
Active sites- cracks or hollows on the surface of the
enzyme due to the manner of the protein folding itself
up to its tertiary structure; LOCK-AND-KEY relationship
Induced fit theory- adjustments are done by the enzyme
to achieve an optimum fit for the substrates
Trypsin- digests proteins by breaking the peptide bond
FACTORS AFFECTING ENZYMATIC SPEED
RATE OF REACTION- amount of product that is
produced per unit of time
Temperature
*As temperature rises, molecules are more inclined to
react because they have more kinetic energy
When temperature is elevated, the enzyme structure
starts to undergo denaturation. The enzymatic activity
declines rapidly because the change in the structure of
an enzyme can no longer accommodate the shape of
the substrate thus binding does not happen.
Endothermic(warm-blooded) animals keep their
internal heat in balance, allowing the enzymes to
perform faster
Substrate Concentration
-amount of substrate molecules available for chemical
reaction

HOLOENZYME- apoenzyme+ cofactor; active and ready

for any catalytic reaction
-substrate concentration increases the enzyme activity
because more collision takes place between the
substrate molecules and enzymes.

*when the active sites are all filled continuously with

the substrate, the rate of reaction no longer increases
(maximum rate is reached)

Optimal pH

-if the pH level continues to increase, the enzymatic

reaction begin to decline

*changing the pH level may affect the ionization of the

side chains(loses structure and becomes inactive) and
disrupt their interactions.

Enzyme cofactor

-some enzymes need the addition of inorganic ions or

coenzymes to help speed up the rate of reaction

-they help bind the substrate to the active site or

participate in the reaction at the active site

Enzyme Inhibitors

-molecule that binds to the enzyme to decrease its

activity; important in controlling enzymatic reactions;
beneficial in conserving raw and energy in the body

-reversible(can still be used because it is not damaged)

or irreversible(inhibitor permanently inactivates or
destroys the enzymes)

-normally used in pharmaceutical industries where

certain chemicals block the activity of the enzyme