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The Basic Components of Life - Coggle Diagram
The Basic Components of Life
Organic
Enzymes
Types
Apoenzyme
:warning:If the enzyme is made up of only proteins, it isan simple enzyme. Therefore an apoenzyme is a protein. They are the inactive form of enzymes. It also determines the specifity of a enzyme system for a particular substrate. :warning:
Holoenzyme (Complex enzyme)
Composed of
Cofactor (Inorganic)
Zinc, iron, or copper
Coenzyme (Organic)
Mostly vitamins
Models
Key-lock Model
:fire: This model supports enzyme specificity as the enzyme doesn't change its shape during the process. According to enzyme specificity the substrate has a complementary shape to the active site of the enzyme. The enzyme can identify a specific substrate from other substrates. :fire:
Induced Fit Model
:star: According to thismodel, the enzyme changes its shape for the substrate to correctly bind to the enzymesactive site to form an enzyme-substrate complex. As the substrate binds to the enzyme, chemical reaction occurs. After the reaction, the products are released. This model shows that enzymes are flexible and they can go back to their initial shapes to accept new substrates. :star:
Factors Afffecting Enzyme Activity
Temperature
pH
Enzyme concentration
Substrate concentration
Surface area of substrate
Inhibitors
Competitive
:checkered_flag: The inhibitor binds to the active site and prevents subtrates from binding to the active site. A noncompetitive inhibitor on the other binds to somewhere away from active site (allosteric site) to alter the enzyme'sshape in order to prevent other substrates from binding to the active site. :checkered_flag:
Noncompetitive
Activators
:!:They bind to enzymes and speed up the reaction. Examplesare Mg, HCI that activates pepsinogen and vitamin B. When an activator binds to an enzyme, it increases the enzyme's substrate affinity , which leads to more substrates binding to the enzyme and which then finally leads to an increased rate of reaction. :!:
Active
:tada: Some enzymes have 'ase' and some has 'ogen' at the end, showing that the enzyme isn't working. This inactive for of an enzyme is called a zymogen. The pancreas secretes zymogens partly to prevent enzymes from digesting problems. :tada:
Proteins
Monomer
Amino acid
Composed of
Amino group
Variable side chain
Carboxylic acid group
Types
Essential
:check: Histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. These are the essentail amino acids that humans must take from heterotrophic nutrition because their boddy can't synthesize them. :check:
Non-essential
Conditional
Used to
Build muscle/bone
Control rate of reactions
Functions
Transport
Regulatory
Catalytic
Movement
Protection
Structural
Energy
Blood Clotting
Diversity
:pencil2: The unique 3D shape of every protein. It is caused by the number, type and arrangement of amino acids as well asthe structures (primary, secondary etc.) The diversity allows proteins with different types which serve different purposes to be made. :pencil2:
Structures
Primary Structure
Secondary Structure
Tertiary Structure
Quaternary Structure
Found in
Chicken
Fish
Eggs
Deficinency Disorders
Long healing of wounds
Weak immune system
Growth retardation
Edema formation
Example
:smiley: Insulin is a polypeptide consisting of 51 amino acids, 30 in chain B and 21 in chain A. The two chains are linked by disulfide bonds. It regulates metabolism of carbohydrates, lipids and proteins. It is produced in the pancreas. Diabetes is a disease in which absolutely no insulin is produced or there is only a remote amount of insulin produced, depending on the type of diabetes. :smiley:
Denutaration
:pen: It is a process in which the molecular structure of a protein is transformed. After denaturation occurs, the protein loses its initial shape. Denaturation is often irreversible. Renaturation is possible if the denatured object is cooled and denaturing chemicals are removed. Boiling and egg is an example of denaturation. :pen:
Lipids
Carbohydrates
Vitamins
Fat soluble
Vitamin A
Found in
Eggs, liver, fortified milk
Deficiency
Night blindness, less growth in children
Function
Vision, bone growth, reproduction
Vitamin D
Found in
Fatty fish, dairy products
Deficiency
Rickets in children, osteoporosis in old ages
Function
Muscles to move, nerves to carry messages
Vitamin E
Found in
Vegetable oils, nuts, green vegetables
Deficiency
Aging, less muscle development
Function
Protect cells from damage
Vitamin K
Found in
Leafy green vegetables (spinach, turnip greens)
Deficiency
Bruising, bleeding
Function
Clots blood
Water soluble
Vitamin B
Found in
Fish, poultry, eggs, meat
Deficiency
Beri beri, pellegra, anemia
Function
Cell metabolism
Vitamin C
Found in
All vegetables and fruits
Deficiency
Gingivitis, scurvy
Function
Normal growth and development
ATP
Composed of
Adenine nucleotide
Ribose sugar
Three phoshate groups
Energy stored in high energy phoshate bonds
C, H, O, N, P atoms
Synthesized
Respiration
Aerobic
Anaerobic
Dehydration synthesis
Phosphorylation
:explode: It means to add a phosphorlly group to a molecule. It produces the ATP cycle. For example if we add a phosphate to an adenosine diphosphate, it will turn to ATP(adenosine triphosphate). But if we remove one phosphate, it will be adenosine monosphate, whixh is called dephosphorylation, the opposite of phosphorylation. :explode:
Hydrolized
Dephosphorylation
Used for
Endergonic (anabolic) reactions
Synthesis reactions
Active transport across the cell membrane
Movement and contraction of muscles
Nerve impulse transmission
Nucleic acids
Single chain
RNA
Types
mRNA
:fountain_pen: It is synthesized based on a DNA template. Carries the genetic information from DNA to riboomes. They can be used again and again like enzymes. They make 5 percent of all RNa molecules. :fountain_pen:
tRNA
rRNA
Pentose sugar
Ribose
Nitrogenous bases
C
U
G
A
Phospate
Double chain
DNA
Nitrogenous bases
A
G
C
T
Pentose sugar
Deoxyribose
Phosphate
Replication
:recycle: A process in which two identical DNA are produced. Occurs in the cytoplasm of prokaryotes and nucleus of eukaryotes. Once it occurs, a cell identical to the one before can be produced, so it is essential for cell division. It starts with hydrogen bonds between bases being ripped open and corresponding bases for the bases in DNA being supplied from the cytoplasm. False DNA replication can lead to very risky diseases. :recycle:
Shape
Double helix
:black_flag:Two different polynucleotide chains connect together with hydrogen bonds to produce a double helix. Double helix looks like a stair case which moves in a circular direction towards the bottom. In the double helix, adenine connects with thymine ( 2 hydrogen bonds) and cytosine connects with guanin ( 3 hydrogen bonds) :black_flag:
Composed of
Monomers
Nucleotides
Pentose sugar
Phosphate group
Nitrogenous base
Pyrimidine
Cytosine
Thymine
Uracil
Purine
Adenine
Guanine
Inorganic
Acids and Bases
Salts
Minerals
Water
