proteins that act as biological catalysts for intracellular and extracellular reactions to determine structure + function - they affect metabolism of cells and the whole organism
specific tertiary structure determines shape of active site
formation of ESC lowers activation energy of metabolic reactions
catalase - intracellular
catalyses decomposition of hydrogen peroxide (which causes oxidative stres) into water and oxygen
h2o2 —> h2o + o2
amylase + trypsin - extracellular
amylase catalyses digestion of starch —> maltose in saliva and small intestine lumen
trypsin catalyses hydrolysis of peptide bonds in small intestine lumen
factors affecting rate of enzyme controlled reactions
enzyme concentration
substrate concentration
concentration of inhibitors
pH
temperature
temperature coefficient
Q10 = (rate of reaction at higher temperature) / (rate of reaction at lower temperature)
describes how much the rate of a reaction changes when the temperature increases by 10°C
competitive inhibitors
bind to active site, since they have similar shape to substrate
prevent ESC from being formed
increasing substrate concentration decreases their effect
non-competitive inhibitors
bind to allosteric binding site
triggers conformational change of the active site
increasing substrate concentration has no impact on their effect
end product inhibitors
one of the products or an enzyme involved in the pathway acts as an inhibitor
prevents further formation of products
anabolic reactions
form biological molecules that make up living tissues, e.g production of collagen
catabolic reactions
break down biological molecules that provide energy, e.g in respiration
activation energy
lowest amount of energy needed for a reaction to occur, enzymes catalyse reactions by lowering the activation energy
how does enzyme specificity arise
active site has a unique shape that only matches certain substrates, so enzymes only catalyse one type of reaction
apoenzyme
inactive enzyme
holoenzyme
active enzyme + cofactor
proenzyme
if a precursor is activated by a change in tertiary structure
irreversible inhibiton
permanently prevents formation of ESC
heavy metal ions eg. mercury cause disulphide bonds in tertiary structure to break
bind to enzymes by strong covalent bonds
metabolicpoison
substance that damages cells by interfering with metabolic reactions
usually an inhibitor
reversible inhibition
can be competitive/non-competitive
temporarily binds to enzymes e.g H-bonds
ESC can form after inhibitor is released
examples of metabolic poisons
cyanide - non-competitive, irreversible, inhibits cytochrome c oxidase