module 2 enzymes Flashcards
enzymes
biological catalysts
globular proteins with substrates
needed for anabolic and catabolic
supplied activation energy
lock and key
area complementary to substrate molecule, substrate binds to active site, enzyme substrate complex formed. r groups make temp bonds.
induced fit hypothsis
active site changes as substrate enters-weak interaction as changes tertiary structure=strength binding, strains on substrate, leading to a weaker bond=less energy, so less activation energy.
starch
broken by amylase to maltose.
salivary glands and pancreas
maltose
broken by maltase to glucose
small intestines.
factors affecting enzymes
temp-denatured if high, as breaks h2 bonding and ionic bonds between r group.
pH=h+ and oh- interferes, so active site changes
q10
rate at temp+10/rate at temp
inhibitors
molecules preventing enzyme carrying normal functiono
competitive inhibitors
molecule similar shape to substrate, and blocks entering, inhibited. most=reversible=statin
not reversib le=asprin
non competitive inhibitors
bind to allosteric site, where teritary structure of enzyme changes.
IREVERSIABLE
end producy inhibition
helps regulate pathway/control amount of products
cofactors
non proetin molecules helping substrate bind to ion.
prothestic groups=permaent
inactive precuraor
produced inactivity
need change in shape-mostly active site.
prevent enzyme damaging cell
coenzyme
non protein molecules, and not permanent.
allow enzyme to function.