UNIT 2> CHEMICAL REACTIONS AND ENZYMES

what are chemical reactions

-changes in chemical bonds

products vs rectants

-recants = compounds that engage in reaction -products = compounds created as a result

chemical reactions that absorb vs release energy

-release energy -> occur on their own -absorb energy -> need extra energy source

what do enzymes do?

-speed up chemical reactions in living things ^w/o being used up -usus ends in 'ase/ are proteins -biological catalysts -specific shape due to teritary structure -> when unable to unfold cant have specific shape -combines with a substrate ^area able to bind to substrate = active site

-w/o enzyme ^energy -w/enzyme decerease enzyme

working of an enzymes

-enzyme ^area able to bind to substrate = active site -substrate (thing that react w/enzyme) recatants

-subtsrate +enzyme (when binded w/bonds formed) = enzyme subsrate complex -> subtrates turned into products -> released results in formed bonds or broken bonds

ph impact on enzyme

-optimal ph = ph that it works best at -graph, expoentail graph basically but decreases, needs to be good or wont work on either far end of spectrum

-> to far out of ph range -> disrupt bonds (e.x hydrogen) -> removes unique shape/destorys teritary structure -> changes active site -> substrate cant bind to enzyme ^^^ DESATURATION - can be reversiable, but sometimes perm

ph

pH = −log ([H+]) ^ potential of hydrogen, unit of measurement for hydrogen ions = how basic/acidic something is -log= change of 1PH unit (10x change in hydro ions) H+=hydrogen ion concreation

7 (acidic) 7= netural 7< alkanie/basic

temperate and enzymes

-diff optiaml temps -> similar w/ph, oncee out of optimal range it increases reaction less and less until denatured and enzyme just doesnt work

-^ kinetic energy = moles move faster -> more collisons -> more sucessful reaction -same as ph graph goes up peaks then down and dies out ^ALSO to hot =breaks bonds just like ph

inhibitors

compettive: -molecules that take place of active site -> no speeding up reaction -more substartes = effect of comp inhibitors

non-competive -molecule that binds to alllosteric site of enzyme (just another bidning site) -causes active site to change shape -> cant speedup/catatalsye -more substrates = no effect because arent fighting for same spot

enzyme concentration

-goes up and peaks then stops increasing (plateaus) -> adding more = more likely to collide w/ -> endlessly adding enzymes when all the subtrates are used doesnt rlly do anything, cant add anything more

substrate concentration

-goes up then peaks -> adding more=more likely to collide w/ -> endlessly adding substrates when all enzymes are used doesnt do anything

cofactors and coenzymes

-same enzymes need cofactors make substrate bind/ make the enzyme work -cofactor= usu inoragnic ions (calcium, magneisum)

-> attach temp to enzyme depending on bond and help substrate bond

-coenzymes = type of cofactors that are organic = carbon based, get from vitamins