enzymes currenttheorystructureinduced fit modelsuggests that substratea 30protein does not fit intoactivesite like a lock in akeychemicalreactionsallowbindingsubstrate can moldactivesite's R groups top a tertiarystructurespeedup chemical reactionschange in structure denaturedmGPsubstratephysical chemicalproperties ofsubstrate must be compatible withenzyme is not changed from reaction instead reusedsubstrates requirespecific enzymes to facilitatereactiondenaturing factorsoptimumtemp optimum pHTtemp fKMTY small ideal pitrangeM toohightemp denature tpit hpit denaturedwtemp slow run rate distrupt it bonds in activetemperature t KMT not denatured ph levelsitesubstrate enzyme concentrationone variablemomd defficiency only I constantly if both variableconcentrations increasehighprobability of binding activation energy Eatransitionalstatea catalysts decrease the amount ofa free energy needed for reactantsto reach the transitional stateto make it work when neededIs something to an enzymesangtwo types of activatorscofactorsGenzymecannoweg nemecoenzymesfriend organic functioncofactor egthiamine vitaminshow can you slow down an enzyme example competitive alcohol1 competitive inhibitionO left substrateusing an inhibitor tobondintoactivesiteinstead of substrate ea'gppedistiteinhibitorcompetitive inhibitorsmimics substrate'sshape notfunction2 allosteric noncomeditiveinhibitions examplenoncompetitive heavymetalsinibitorbondstoallostericsite whichwillinitigmpeditive O Eistratechange activationsiteshape to stopallostericsitesubstrate fromfitting Etive