2.1 - 2.5 Molecules + enzyme Flashcards
Anabolism vs catabolism
Ana: synthesis of complex molecules from simpler molecules, use of energy
Energonic
Cat: breakdown of complex into simpler, release energy
Exergonic
Draw: a/b glucose, ribose + formula
Glu” c6h12o6
ribose: c5h10o5
Role of urea
Excretion of nitrogen: access amino acids > urea at liver > excreted in kidney
Urea is fertilizer
Properties of water (6) and significance
- Polar and hydrogen bonding:
O more electronegative than H
Partial positive/negative, net dipole
H bond: H is attracted to O on neighbouring atom - High shc
Insulator, thermally stable and constant environment for biochemical reactions to occur. - High lhv
Evaporative coolant - remove heat: sweating - High lhf
Cells unlikely to freeze - Cohesion/adhesion/surface tension
Cohesion: attraction between water molecules
Adhesion: attraction between water molecules and other polar molecules of different substances
Capillary action
Surface tension: how difficult it is to break surface of a liquid - small insects move on surface of water - Universal solvent
Dissolve polar substances
Ions and polar groups surrounded by water molecules, form hydration shells
Ions separated from each other
Transport medium
Water v methane
Boiling point: due to imf of attraction
Polar/nonpolar
Can/cannot form hydrogen bonds
Condensation v hydrolysis
condensation: 2 molecules combine to form larger molecule, production of water as byproduct
hydrolysis: large molecule reacts with molecule of water, split into 2 smaller molecules.
Functions of carbohydrates (7)
- Energy
- Cellulose
- Nucleic acid
- Nectar
- Lubricant
- Glycoprotein
- Used to produce AA/fats
Amylose v amylopectin v glycogen
All a-glucose
Amylose: 1-4, helical coiling into complex shape
Amylopectin: 1-4, 1-6, branching with long side chains (20-25 monomers)
Glycogen: 1-4. 1-6, branching with short side chains, more compact than amylopectin.
Advantages of glycogen structure
Branching provides site for enzymes to cleave off glucose molecules, allows for rapid hydrolysis, produce high levels of glucose more quickly, higher resp
Cellulose structure
b-glucose molecules
1-4, every alternate molecule inverted
long, straight, unbranched
chains run parallel to each other
hydroxyl groups project outwards enable hydrogen bonding between neighboring chains
rigid cross linking
Cis vs trans, significance of boiling point
Cis - pronounced kink, H at same side of double bond chain extends in diff direction, prevents tight packing, lower mp, do not solidify as readily.
Trans - less pronounced kink, H at diff side of double bond, chain extends in same direction, can be packed closely with each other, higher mp.
Example of simple, compound, derived lipids
Triglyceride, phospholipid, cholesterol
Lipid functions (6)
Long term energy storage
Structure - phospholipid
Signaling - steroid hormones
Insulation - subcutaneous tissue
Protection - adipose tissue surround and cushion internal organs
Buoyancy - less dense than water, animals float
Lipids v carbohydrates
Lipids higher energy per gram
Solubility in water
Long term energy storage
Aerobic vs ana/aerboic resp
Types of protein structures (4) and explain
Primary - linear sequence of aa in specific order, held together by peptide bonds
Secondary - regular folding, twisting, coiling of primary structure to form a helix or b pleated sheet
Tertiary - folding of secondary structures to form 3D conformation
Quaternary - Comprised of more than one polypeptide chain to form functional protein.
Proteome vs genome’
Why proteome is larger?
Proteome - set of proteins produced by cell/organism at given time and defined conditions
Genome - set of genes in cell/organism
Proteome is larger - alternative splicing and modification of proteins.
Functions of proteins (9) but prob 7 is enough
- Hemoglobin
- Actin and myosin
- Tubulin
- Membrane proteins (adhesion)
- glycoproteins
- digestive enzymes
- fibrinogen
- collagen
- Histones
Collagen - function and structure
insoluble, fibrous protein
Structural support, elasticity to connective tissue, along with elastin
Found in extracellular matrix
Zwitter ions?
Ionized carboxyl and amino groups.
Fibrous protein v globular protein
insoluble v soluble
long and narrow v rounded
Structural/support, functional/metabolic
Collagen v hemoglobin
More sensitive to changes in pH/temp, less sensitive
Enzyme - definition
Globular protein
Biological catalyst
Speed up rate of organic rxn
lower activation energy
Not consumed by rxn
Lock and key vs induced fit
L/K:
Enzyme active site is specific to shape of substrate
Active site is rigid, inflexible
Only substrates with exact, complementary shape can bind.
Could not explain why some active sites can bind to multiple substrates
I/F:
- Active site is flexible and not necessarily complementary
- Binding induces change in conformation, better fit substrate
- Change in shape reduces Ea, facilitates bond breaking
Effect of temp on enzyme activity
Increase to optimum
- increase in ke
- increase in frequency of collisions, effective collisions
- increase rate of es complex formation
- increase rate of rxn
Optimum - highest rate of rxn
Past optimum
- Thermal agitation of enzymes
- H bond, ionic interaction, weak hydrophobic interactions which give 3d shape disrupted.
- 3D conformation enzyme and active site disrupted
- Enzyme denatured
Effect of pH on enzyme activity
Low/high ph:
Ionic charges of acidic and basic groups on side chains of amino acid residue are altered, resulting in the disruption of ionic and hydrogen bonds which allow for 3d shape of enzyme. 3d conformation of active site is lost, enzyme denatured.
