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Enzymes

activation energy-minimum amount of energy needed for a successful chemical reaction

enzymes-specific tertiary structure, unique 3d shape, active site complimentary to only one substrate, forms enzyme substrate complexes

lock and key-substarte complimentary to active site, binds to active site, products formed no longer fit.

induced fit-substrate binds and changes shape of active site, when it leaves it goes back to original shape

ph-ph changes from optimum, breaks ionic bonds changing shape of active site, substrate can't bind, fewer esc formed, denature, ror decreases.

temperaure- temp rises above optimum, more kinetic energy, more frequent collision, breaks hydrogen and ionic bonds, changes shape of active site, no substrates can bind, fewer esc, denature, ror decreases.

sustrate concentration-as increases substrate concentration is limiting factor as not all active sites are occupied, as increases more collisions so more are occupied so ror increases substrate concentration no longer limiting factor.

optimum temperature-maximum energy suplied to molcecules before hydrogen and ionic bonds start to break

competitive inhibitor-similar structure to substrate, binds to active site so normal substrate can't bind,so few esc formed slows ror not permanent.

non competitive inhibitor-binds to site on enzyme thats not active site, changes shape of active site preventing normal substrate from binding, fewer esc formed, ror decreases, permanent.