Transcript enzymes

3.2: Carbon Compounds
• All of the many compounds can be classified in TWO
broad categories:
ORGANIC COMPOUNDS AND
INORGANIC COMPOUNDS.
• ORGANIC CHEMISTRY =
• The Chemistry of Carbon =
• Chemistry of Life
ORGANIC
• Made up of mostly what element?
• CARBON
• -C-C-C-C-C-C-C-C
II. Carbon’s Bonding Behavior
A. Outer shell of carbon
has ____ electrons;
but can hold ____
B. Each carbon atom
can form __________
bonds with up to
_________ atoms
4 covalent bonds
C. Carbon atoms can
form
_______________ or
______________
• D. Carbon atoms
covalently bonded
form the
________________
of organic
compounds
• E. ______________
can project from the
carbon backbone
F. Carbon’s tendency to _______________
results in an enormous variety of ORGANIC
COMPOUNDS
Carbon can share two or even three pair of
electrons with another atom
a) SINGLE BOND - A bond formed when
two atoms share ONE pair of electrons.
b) DOUBLE BOND - Atoms share TWO
pairs of electrons.
c) TRIPLE BOND - Atoms Sharing THREE
pairs of electrons.
Covalent Bonds – single, double, triple
III. Functional Groups
A. Atoms or clusters of atoms that are
covalently bonded to a
_____________________________
B. Gives organic compounds their different
properties
ex: HYDROXYL GROUP -OH attached
makes an ALCOHOL
Examples of Functional Groups
Hydroxyl group
- OH
Amino group
- NH3+
Carboxyl group
- COOH
Phosphate group
- PO3-
Methyl group
- CH3
R – Is a repeating unit
IV. LARGE CARBON MOLECULES
A. Large Carbon Compounds are built up from
smaller simpler molecules called
_______________ (building blocks)
(MONO = ONE)
B. Monomers can bind to one another to form
complex molecules known as
_________________
(POLY = MANY)
C. A Polymer consist of repeated, linked units,
forming large polymers called
______________________
(MACRO = LARGE)
V. Types of Reactions
1. Condensation-Dehydration Synthesis
2. Hydrolysis
1) Condensation Reactions (Dehydration
Synthesis)
a) Monomers link to form ______________
b) Monomers are CONDENSED and water
(H2O) is squeezed out (DEHYDRATE)
-H2O is a by-product of the reaction
c) Enzymes remove
from one molecule,
from another
 bond formed between two molecules
CONDENSATION (dehydration synthesis)
enzyme action at functional groups
Fig. 3.4a, p. 37
2) Hydrolysis
a) The _________________ of complex
molecules, such as polymers
b) SPLITTING of a WATER molecule to
ADD -OH group and an H
 bonds break that hold polymers together
HYDROLYSIS
enzyme action at functional groups
Fig. 3.4b, p. 37
3.3 MOLECULES OF LIFE
Four organic compounds:
•
•
•
•
Carbohydrates
Proteins
Lipids
Nucleic Acids
Plants: mostly carbs
Animal: mostly protein
What is the difference between structural
formula and molecular formula?
• Molecular Formula:
H2O
– The way it is written
• Structural Formula: H – O – H
– The way it looks (arrangement)
Human Body
Oxygen
65%
Carbon
18%
Hydrogen
10%
Nitrogen
3%
Calcium
2%
Phosphorus 1.1%
Sulfur
0.25%
Sodium
0.15%
Chlorine
0.15%
Magnesium
0.05
Iron
0.004%
1. Carbohydrates: sugars and starches
contain C, H, and O in the ratio of CH2O
-carbo (C) hydrate (H2O)
a) monomers of sugars (simple sugars) -
1)eg: Glucose (manufactured by plants)
Fructose (found in fruits)
2) ____________: has the same molecular
formula but a different structural formula
3) Used for _______________________
Isomers: same molecular formula, but
different structural formula
glucose
fructose
galactose
b) Disaccharides – double sugar
C6H12O6 + C6H12O6 = C12H22O11 + H2O
What type of reaction??
dehydration synthesis – combining of 2
monomers (monosaccharides) by squeezing out a
H20
1) EXAMPLES:
sucrose (glucose + fructose = table sugar)
maltose (2 glucose)
2) bond between two monosaccharides is called
a ___________________ bond
3) a disaccharide contains __________energy
than the two units it is composed of (bc of bond)
Disaccharides
• Made up of?
glucose
fructose
– Two monosaccharides
• What type of bond?
– Covalent
o
– “Glyc
sidic”
• What type of reaction?
– condensation reaction
(dehydration synthesis)
+ H2O
sucrose
Other sugars:
MONOSACCHARIDES OR DISACCHARIDES?
c) _________________ – 3 or more monosaccharides
complex carbohydrates, starches, cellulose, chitin
1)
most abundant of carbohydrates
2)
thousands of _____________ units bonded
together by dehydration synthesis =
type of: ____________________________
3) energy storage molecules
plants = starch
animals =
“animal starch”
also important as _____________
components of organisms:
eg. -cellulose = 50% of carbon in plants
-chitin = exoskeleton of insects
Glycogen
• Sugar storage form in _____________
• Large storage in _______ and _______ cells
• When blood sugar decreases,
liver cells _____________ glycogen,
releasing _____________
cells store energy as polysaccharides
rather than glucose units because
the
_________________________________
(warehouse of simple sugars)
Cellulose and Starch
Cellulose & Starch
• Differ in bonding patterns between
monomers
• Cellulose - tough, indigestible, structural
material in plants (corn covering )
• Starch - easily digested, storage form in
plants (potato insides)
2 Examples of
MONOSACCHARIDE
• GLUCOSE
• FRUCTOSE
Example of DISACCHARIDE
•SUCROSE
(Glucose + Fructose)
4 examples of
POLYSACCHARIDES
stores energy:
makes up stuff:
• STARCH
• CELLULOSE
• GLYCOGEN
• CHITIN (on
insects)
2. Lipids
A) Composed of C, H, and O
b) Ratio of C to H to O higher than in
carbohydrates
c) Defined based on their solubility:
1) they are insoluble in ___________
2) they are soluble in ____________
d) Primary function –
to store large amounts of energy
(twice as much energy as carbs and proteins
e) Secondary functions of lipids:
1. structural components
eg. phospholipids- major building block
in cell membranes
2. "messengers" (hormones) that play
roles in communications within and
between cells
•
(can’t dissolve in blood plasma 
protects message)
3. insulation and padding
f) Monomers of Lipids are:
3 fatty acids covalently bonded to
a 3-carbon “backbone”- glycerol
The fatty acids are composed of CH2
units
Fatty Acids
building blocks of:
(fats, waxes, phospholipids, but not sterols)
1) Carboxyl group (-COOH) at one end
Methyl (CH3 ) group at the other end
2) Carbon (CH2) backbone (up to 36 C
atoms)
4) Saturated - __________ bonds
between carbons
_________ at room temperature
5) Unsaturated – One ________ bond
________ at room temperature
6) Polyunsaturated – more than one
__________ bond
_________ at room temp.
Three Fatty Acids
7) Glycerol backbone – fatty
acids attach to the glycerol
Dehydration synthesis removes the –H
from the glycerol and -OH from the fatty
acid to form a glycosidic bond.
Triglyceride formed by dehydration synthesis
+ 3H20
three fatty acid tails
glycerol
triglyceride
Fig. 3.8b, p. 40
Unsaturated Fat
Alpha end – from carboxyl
Omega end – from methyl
# - which carbon has double bond
• TRANS
• CIS-UNSATURATED • SATURATED
UNSATURED
FAT
FAT
USUALLY
ARTIFICIAL 
EASIEST TO
BREAKDOWN

9) Phospholipids
• Main components of cell
membranes
• Has a phosphate group and two
fatty acids
Phosphate
group
Phospholipid
Phospholipid Bilayer
Waxes
• Long-chain fatty acids linked to
carbon RINGS
• Feels hard, REPEL water
• Important in water-proofing
Sterols and steroids
• No fatty acids
• Rigid backbone of
four fused-together
carbon rings
• Cholesterol - most
common type in
animals
• Low-density
lipoproteins (barely
moves fats around)
• High-density
lipoproteins (efficiently
moves fats around) 
LE 4-9
Estradiol
Female lion
Testosterone
Male lion
• Transgender -one's gender identity not
matching one’s assigned sex
• Heterosexual – into opposite sex
• Homosexual – into same sex
• Bisexual – into both sexes
• Androgenous – combo of male and female char
• Hermaphrodite – having both sexual organs
• Transvestite - dress or act like opposite sex
3. Nucleic Acids
Include DNA and RNA
DNA strand 
What are the monomers of nucleic
acids?
• DNA 
• Holds genetic info
• RNA 
• Holds instructions to make
proteins
Nucleotide Structure
• Sugar
–Ribose or deoxyribose
• Phosphate group
• Nitrogen Base
Nucleic Acids
Cytosine
Adenine
• Composed of nucleotides
• Single- or double-stranded
• Sugar-phosphate backbone
ATP - A Nucleotide
base
three phosphate groups
sugar
ATP
I.
= ATP
- energy currency of cell
A. Temporarily stores large amounts of
energy in phosphate bonds
B. Regulates many biological pathways
C. is made in a process called
nucleic acids
D. ATP is a monomer of __________
made up of three components
1)
= nitrogen containing base
2)
C5H10O5
= 5 carbon sugar
3) 3 inorganic
(from phosphoric acid)
ATP - A Nucleotide
base
three phosphate groups
sugar
How ATP releases ENERGY
• When break a ______________
group off by _________________
• It becomes  _______ (adenosine
DIphosphate
• And ___________________ energy
II.
= ADP
A. Adenine - ribose- P ~ P
B. When the last phosphate group is
released from ATP, ADP is formed.
ATP ----> ADP + P +
energy
Why would you need ENERGY from ATP
in a cell?
• build larger molecules
• carry substances into the cell
• remove wastes from the cell
• for mechanical work (like muscular
activity).
4. Proteins
A. Most complex and important substances
in living organisms
B. Composed of C, H, O, N
C. Monomer of a protein is:
D. Types/FUNCTION of Proteins:
1) structural (makes up) – parts of cells,
tissues, collagen and elastin
What is COLLAGEN?
•
•
•
•
1/4 of protein in bodies !
Makes up 75% of our SKIN
Also makes up cartilage, bone..etc.
BOTOX, lip injections…etc 
2) Transport/contractile
–in muscle; myosin and actin
-in cell membrane; calcium pump
3) Communication/hormones
– insulin
-growth factor
4) Storage
-ferritin (stores iron from our food)
5) Defense
– immunoglobin
-antibodies
6) enzymes
– largest group of proteins; regulate
reactions (organic catalyst)
-alpha amylase
E. Amino Acid
Stupid lil H
amino
group
carboxyl
group
R group – 20 different
kinds with distinct properties
1) Properties of Amino Acids
a) Determined by the “R group”
b) there are 20 different Amino Acids
c) Amino acids may be:
tyrosine (tyr)
lysine (lys)
glutamate (glu)
glycine (gly)
valine (val)
phenylalanine (phe)
methionine (met)
proline (pro)
Fig. 3.12, p. 42
2) Protein Synthesis
A Protein is a chain of amino acids
linked by peptide bonds
• Peptide bond:
– Type of covalent bond
– Links amino group of one amino acid with
carboxyl group of next
– Forms through condensation reaction
(dehydration synthesis)
newly
forming
polypeptide
chain
Fig. 3.14, p. 43
If there are only 20 amino acids, how are there
so many types of proteins?
• The sequence (arrangement) of
amino acids
• The kinds of amino acids present
• The number of amino acids in a
protein
Protein Synthesis
• Two linked amino acids = dipeptide
• Three or more amino acids=
polypeptide
• Protein – two or more polypeptide chains
• Backbone of polypeptide has N atoms:
-N-C-C-N-C-C-N-C-C-N-
Protein Shapes
• Fibrous proteins
– Polypeptide chains arranged as strands or sheets
• Globular proteins
– Polypeptide chains folded into compact, rounded
shapes
1-Primary Structure
& Protein Shape
• Long strand of protein
2-Secondary Structure (twisted)
3-Tertiary Structure
heme group
Folding as a
result
of interactions
between R
groups
coiled and twisted polypeptide
chain of one globin molecule
4-Quaternary Structure
Some proteins
are made up of
more than one
polypeptide
chain
Hemoglobin
Denaturation
• Disruption of three-dimensional shape
• Breakage of weak bonds
• Causes of denaturation:
– pH
– Temperature
• Destroying protein shape disrupts function
What’s a REALLY IMPORTANT
protein that speeds up reactions by
either breaking or making things?
Copy into notes p.4 at bottom:
Enzymes LOWER Activation
Energy
activation energy
without enzyme
starting
substance
activation energy
with enzyme
energy
released
by the
reaction
products
Enzymes
• Are Catalysts found in organisms
(biological/organic catalysts)
• Name based on compound being affected.
Most end in “ase”:
- Lipase (works on lipids)
- Maltase (works on maltose)
- Lactase (works on lactose)
- protease (works on proteins)
AMYLASE – breaks down starch
• Where is it found in your body?
Catalase
Catalyzes the formation of oxygen
and water from hydrogen peroxide
2H2O2 ----------> 2H2O + O2
Every enzyme has one or more active sites.
“breaking” reaction
Active Site
Visualize!
Effect of Temperature
• What does cold
temperatures do to
enzymes?
• What does warm
temperature do to
enzymes?
• What do REALLY
high temperatures
do to enzymes?
Effect of pH
LOCK AND KEY MODEL
substrates fits into the active site like a key fits into a lock
INDUCED FIT MODEL
substrates fits into the active site by deforming it somewhat
two
substrate
molecules
substrates
contacting
active site
of enzyme
active sight
TRANSITION
STATE
(tightest
binding but
least stable)
end
product
enzyme
unchanged
by the
reaction
Induced-Fit Model
• “making” reaction
COUPLED REACTION = BIOCHEMICAL PATHWAY
Competitive Inhibitors
In competitive inhibition, an INHIBITOR
can block the active site so the
SUBSTRATE can’t fit there
Non-Competitive Inhibition
• Non-competitive inhibitors do not compete with
active site, but stick to enzyme somewhere else and
changes enzyme’s shape so substrate can’t fit
Where do we get our enzymes
from?
• VITAMINS!
• Vitamin B5 (panthenol) becomes Coenzyme-A and
moves acetyl groups CH3CO- about in respiration.
• Vitamin B2 (riboflavin) becomes flavin
mononucleotide (FADH2) and moves electrons about
in respiration.
• Vitamin B12 (cobalamin) becomes bound moves
methyl CH3- groups about in the C1 metabolism
(important for nucleotide synthesis).
• Vitamin C (ascorbate) moves electrons onto Fe3+ ion
in prolyl hydroxylase, which is needed for collagen
synthesis, hence the symptoms of scurvy (soggy
gums).
Factors Influencing
Enzyme Activity
Temperature
pH
Reusability
Salt concentration