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AP Biology 2007-2008 Enzymes
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AP Biology 2007-2008 Enzymes AP Biology Exothermic vs. endothermic reactions exothermicendothermic - energy released - digestion - energy invested -

Dec 21, 2015

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  • Slide 1
  • Slide 2
  • AP Biology 2007-2008 Enzymes
  • Slide 3
  • AP Biology Exothermic vs. endothermic reactions exothermicendothermic - energy released - digestion - energy invested - synthesis -G-G G = change in free energy = ability to do work +G+G All chemical reactions require energy
  • Slide 4
  • AP Biology Activation energy Breaking down large molecules requires an initial input of energy activation energy large biomolecules are stable must absorb energy to break bonds energy cellulose CO 2 + H 2 O + heat
  • Slide 5
  • AP Biology Too much activation energy for life Activation energy moves the reaction over an energy hill Why is activation energy important?? glucose
  • Slide 6
  • AP Biology Reducing Activation energy Catalysts reducing the amount of energy to start a reaction Pheeew that takes a lot less energy! reactant product uncatalyzed reaction catalyzed reaction NEW activation energy
  • Slide 7
  • AP Biology Catalysts So whats a cell got to do to reduce activation energy? get help! chemical help ENZYMES GG Call in the ENZYMES! The ENZYMES are here
  • Slide 8
  • AP Biology Enzymes Biological catalysts Proteins facilitate chemical reactions increase rate of reaction without being consumed reduce activation energy dont change free energy ( G) released or required required for most biological reactions highly specific thousands of different enzymes in cells control reactions of life
  • Slide 9
  • AP Biology Enzymes vocabulary substrate reactant which binds to enzyme enzyme-substrate complex: temporary association product end result of reaction active site enzymes catalytic site; substrate fits into active site substrate enzyme products active site
  • Slide 10
  • AP Biology Lock and Key model Simplistic model of enzyme action substrate fits into 3-D structure of enzyme active site H bonds between substrate & enzyme like key fits into lock In biology Size doesnt matter Shape matters!
  • Slide 11
  • AP Biology Induced fit model More accurate model of enzyme action 3-D structure of enzyme fits substrate substrate binding cause enzyme to change shape leading to a tighter fit conformational change bring chemical groups in position to catalyze reaction
  • Slide 12
  • AP Biology Properties of enzymes Reaction specific each enzyme works with a specific substrate H bonds & ionic bonds between active site and substrate Not consumed in reaction single enzyme molecule can catalyze thousands or more reactions per second Affected by cellular conditions any condition that affects protein structure temperature, pH, salinity - Denaturation
  • Slide 13
  • AP Biology Naming conventions Enzymes named for reaction they catalyze sucrase breaks down sucrose proteases break down proteins lipases break down lipids DNA polymerase builds DNA adds nucleotides to DNA strand pepsin breaks down proteins (polypeptides)
  • Slide 14
  • AP Biology 2007-2008 Got any Questions?!
  • Slide 15
  • AP Biology 2007-2008 Factors that Affect Enzymes
  • Slide 16
  • AP Biology Enzyme concentration enzyme concentration reaction rate Whats happening here?! as enzyme = reaction rate
  • Slide 17
  • AP Biology Substrate concentration substrate concentration reaction rate Whats happening here?! as substrate = reaction rate
  • Slide 18
  • AP Biology 37 Temperature temperature reaction rate Whats happening here?! Optimal T o Slow molecules Denaturation Optimum T greatest number of molecular collisions
  • Slide 19
  • AP Biology Enzymes and temperature Different enzymes function in different organisms in different environments 37C temperature reaction rate 70C human enzyme hot spring bacteria enzyme (158F)
  • Slide 20
  • AP Biology 7 pH reaction rate 20134568910 pepsintrypsin Whats happening here?! 11121314 pepsin trypsin
  • Slide 21
  • AP Biology Salinity salt concentration reaction rate Whats happening here?! Salinity is salt concentration
  • Slide 22
  • AP Biology Compounds which help enzymes cofactors non-protein small inorganic compounds & ions bound within enzyme molecule Examples: Mg, K, Ca, Zn, Fe, Cu IMPORTANT!!!!! So sit up! coenzymes non-protein organic molecules bind temporarily or permanently to enzyme near active site Examples: many vitamins NAD (niacin; B3) FAD (riboflavin; B2) Coenzyme A
  • Slide 23
  • AP Biology Show me some coenzymes homeskillet! Mg in chlorophyll Fe in hemoglobin
  • Slide 24
  • AP Biology Compounds which regulate enzymes Inhibitors molecules that reduce enzyme activity competitive inhibition noncompetitive inhibition feedback inhibition
  • Slide 25
  • AP Biology Competitive Inhibitor Inhibitor & substrate compete for active site disulfiram (Antabuse) treats chronic alcoholism blocks enzyme that breaks down alcohol severe hangover & vomiting 5-10 minutes after drinking How can I beat a competitive inhibitor?
  • Slide 26
  • AP Biology Non-Competitive Inhibitor Inhibitor binds to site other than active site allosteric inhibitor binds to allosteric site causes enzyme to change shape conformational change active site is no longer functional binding site keeps enzyme inactive
  • Slide 27
  • AP Biology Metabolic pathways A B C D E F GA B C D E F G enzyme 1 enzyme 2 enzyme 3 enzyme 4 enzyme 5 enzyme 6 Many enzymes are used in chemical reactions efficiency control = regulation A B C D E F GA B C D E F G enzyme When might Inhibitors be helpful?
  • Slide 28
  • AP Biology allosteric inhibitor of enzyme 1 Feedback Inhibition Regulation & coordination of production product is used by next step in pathway final product is inhibitor of earlier step allosteric inhibitor of earlier enzyme feedback inhibition no unnecessary accumulation of product A B C D E F GA B C D E F G enzyme 1 enzyme 2 enzyme 3 enzyme 4 enzyme 5 enzyme 6 X
  • Slide 29
  • AP Biology Feedback inhibition Example synthesis of amino acid, isoleucine from amino acid, threonine isoleucine becomes the allosteric inhibitor of the first step in the pathway as product accumulates it collides with enzyme more often than substrate does threonine isoleucin e
  • Slide 30
  • AP Biology 2007-2008 Dont be inhibited! Ask Questions!
  • Slide 31
  • AP Biology Extra Info
  • Slide 32
  • AP Biology Factors affecting enzyme function pH changes in pH adds or remove H + disrupts bonds, disrupts 3D shape disrupts attractions between charged amino acids affect 2 & 3 structure denatures protein optimal pH? most human enzymes = pH 6-8 depends on localized conditions pepsin (stomach) = pH 2-3 trypsin (small intestines) = pH 8 72013456891011
  • Slide 33
  • AP Biology Factors affecting enzyme function Salt concentration changes in salinity adds or removes cations (+) & anions () disrupts bonds, disrupts 3D shape disrupts attractions between charged amino acids affect 2 & 3 structure denatures protein enzymes intolerant of extreme salinity Dead Sea is called dead for a reason!