Enzymes (C1.1) + Respiration (C1.2) + Photosynthesis (C1.3) Flashcards
Define an enzyme (3)
biological catalysts
speed up chemical reactions + increase rate of occurrence
globular proteins
Define metabolism
complex network of interacting chemical reactions in living organisms
Properties of enzymes
specific - catalyses specific reaction
Significance of enzyme shape to being complementary to subtrate (2)
interactions of amino acids determine active site shape
active site created from folding of polypeptide chain
How enzymes catalyse reactions (6)
substrate moves randomly until close enough to active site
chemical properties of enzyme surface attract substrate to active site
induced fit-binding : interactions between substrate + AS change 3D shape of both
if 2nd substrate, it will bind to another part of AS
changed substrate molecules weaken bonds + allow new bonds to form to make products
products detach from A.S + enzyme activity site returns to original shape
Molecular motion in forming enzyme substrate complexes (3)
enzyme substrate complex only form when both are close to each other
random movement causes occasional successful collision
increasing substrate/enzyme amount + temperature increases chances of collision
Variation of molecular motion between enzymes and substrates (3)
most cases substrate smaller than enzymes = substrate moves more
some substrates large + dont move much = enzyme has to move in relation to substrate
some enzymes embedded in membranes = substrate does all movement
Relationship between pH and enzyme activity (2)
ph increases = rate of reaction increases up till optimum ph
beyond optimum pH = denaturation + alter shape of active site
Why pH affects enzyme activity (2)
prescence/abscence of hydrogen ions affects ionic bonds between amino acids
changes AS shape
Enzymes role in energy (2)
reduce activation energy required for a reaction - increases rate of reaction
bonds in substrate weaken during enzyme-substrate complex = less energy needed to break
Enzyme anabolic reactions (4)
synthesis of complex molecules from simpler molecules
by reducing repulsion between substrates, allowing them to bond more easily
requires energy
e.g protein/DNA synthesis
Enzyme catabolic reactions (4)
breaks complex molecules into simpler molecules
puts strain on the bonds, making them easier to break
releases energy
e.g digestion, respiration
Define extracellular enzymes (2)
enzymes released from cell + work outside it
synthesized by ribosomes attached to endoplasmic reticulum
Define intracellular enzymes (2)
enzymes used within cells
synthesized by ribosomes in cytoplasm
Factors which affect enzyme activity (4)
substrate concentration
enzyme concentration
temperature
pH
Define the saturation point for an enzyme
point at which every active site is filled
Rate of reaction formula
(product formed/reactant used up)/ time
Define an allosteric site
second active site for a different substance to bind/unbind to
Features of non-competitive inhibitors (4)
bind to allosteric site - change shape of enzyme
enzyme rate of reaction decreases
changing enzyme shape = A.S no longer complementary to substrate
hence fewer complementary enzymes
Features of competitive enzyme inhibitors (4)
bind to active site of enzyme = substrate cannot bind to A.S
chemically similar to substrate
inhibitor competes with substrate for A.S
faster rate of reaction than non-competitive inhibitor
Features of end-product inhibition (2)
enzymes allosterically inhibited by end-product of pathway
prevents over-production of certain substance
Features of mechanism-based inhibition (3)
irreversible binding of inhibitor to A.S through covalent bond
enzyme permanently loses catalytic ability
harmful to organisms
Penicillin as mechanism-based inhibition (3)
bacterial cell wall protects + prevents bacteria from bursting
transpeptidase - enzyme which maintains cell wall structure by forming cross-links with polysaccharide chains
penicillin binds to transpeptidase irreversibly - inhibits its function + cell wall weakens
Define ATP (2)
consist of adenine, ribose sugar, 3 phosphate groups
used for temp. storage of energy + energy transfer
Properties of ATP (5)
soluble in water - can move freely through cytoplasm
stable at pH levels close to neutral
cannot pass freely through phospholipid bilayer
3rd ATP phosphate group easily removed + attached through hydrolysis + condensation reaction
hydrolysing ATP to ADP + phosphate releases energy
Uses of ATP (3)
synthesizing DNA + Protein
active transport of molecules + ions across membraines
move things around cells (e.g chromosomes + muscle fibers)
How ATP works (4)
ATP has 3 phosphates linked through high energy bonds
breaking of phosphate group (hydrolysis) releases energy
ATP –> ADP + one phosphate group
ADP converted back into ATP through respiration
Define phosphorylation (2)
process of adding a phosphate to a molecule
makes many molecules more unstable + more reactive
Define respiration
complex metabolic process to break down carbon compounds + create energy
Define respiratory substrate (3)
organic nutrient oxidised in respiration
e.g glucose, fats, proteins
Define aerobic respiration (4)
complete breakdown of glucose to generate a net gain of 36 molecules of ATP in presence of oxygen
takes place in cytoplasm + mitochondria
can use glucose, fats and proteins as respiratory substrates
produces water + carbon dioxide as waste products
Define anaerobic respiration (4)
partial breakdown of glucose to produce net 2 ATP in absence of oxygen
takes place in cytoplasm
only carbohydrates as respiratory substrates
produces lactic acid/lactate as a waste product
Factors which affect respiration rate (4)
Temperature
pH
concentration of respiratory substrates
oxygen concentration
Function of respirometer (2)
simple devices
measure rate of respiration in organism that respire aerobically