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Transcript
From food webs to the life of a cell energy energy energy AP Biology Enzyme catalyze reactions dehydration synthesis (synthesis) + enzyme H2O hydrolysis (digestion) enzyme H2O AP Biology + Examples dehydration synthesis (synthesis) enzyme hydrolysis (digestion) enzyme AP Biology How does ATP transfer energy? ADP + O– –O P O ATP O– –O–P O– –O–P O O– O– –O P O ATP ADP O– + O Pi releases energy ∆G = -7.3 kcal/mole Fuels other reactions Phosphorylation released Pi can transfer to other molecules destabilizing the other molecules AP Biology enzyme that phosphorylates = “kinase” 7.3 energy ATP + H2O → ADP + Pi ATP Hydrolysis AP Biology Explain. An example of Phosphorylation… Building polymers from monomers need to destabilize the monomers phosphorylate! H C OH + H C HO synthesis +4.2 kcal/mol “kinase” H C OH + H C AP Biology ATP enzyme -7.3 kcal/mol H + P C HO H H C C OHHO enzyme H H + C C O H2O H + C ADP P H H -3.1 kcal/mol C C O + Pi AP Biology METABOLISM Chapter 8 An Introduction to Metabolism Metabolism = total of an organism’s chemical reactions AP Biology Glycan Metabolism Lipid Metabolism AP Biology Nucleotide Metabolism Carbohydrate Metabolism Amino Acid Metabolism Cofactors & Vitamins Metabolism AP Biology ATP - ADP cycle Can’t store ATP good energy donor, not good energy storage cellular respiration ATP 7.3 kcal/mole too reactive transfers Pi too easily only short term energy + Pi ADP storage carbohydrates & fats are long term energy storage A working muscle recycles over 10 million ATPs per second I need some glucose (and O2)! AP Biology What drives reactions? If reactions are “downhill”, why don’t they just happen spontaneously? because covalent bonds are stable bonds starch AP Biology Why don’t stable polymers spontaneously digest into their monomers? Activation energy Breaking down large molecules requires an initial input of energy activation energy large biomolecules are stable must absorb energy to break bonds cellulose AP Biology energy CO2 + H2O + heat Too much activation energy for life Activation energy amount of energy needed to destabilize the bonds of a molecule moves the reaction over an “energy hill” glucose AP Biology Not a match! That’s too much energy to expose living cells to! Uphill is hard How can it be made easier? Lower the hill! AP Biology Catalysts So what’s a cell got to do to reduce activation energy? get help! … chemical help… ENZYMES Call in the ENZYMES! G AP Biology Reducing Activation energy Catalysts reducing the amount of energy to start a reaction uncatalyzed reaction catalyzed reaction NEW activation energy reactant product AP Biology That takes a lot less energy! Describe each type of reaction. Label the energy diagrams. ______gonic Reaction ______gonic Reaction Free Energy _________ __________ Products ___G ______gonic Reactants Reaction progress AP Biology Reactants Products + Energy Free Energy Energy + Reactants Products _________ __________ Reactants ___G _______gonic Products Reaction Progress Know the difference. Be able to label. Endergonic Reaction Exergonic Reaction Activation Energy Products +G Endergonic Reactants Reaction progress AP Biology Reactants Products + Energy Free Energy Free Energy Energy + Reactants Products Activation Energy Reactants -G Exergonic Products Reaction Progress Effect of Catalyst on Reaction Rate Describe what a catalyst does.. Indicate the activation energy for the uncatalyzed reaction and for the catalyzed reaction. ___________________ Energy ___________________ reactants products AP Biology Reaction Progress Effect of Catalyst on Reaction Rate Catalyst lowers the activation energy for the reaction. No catalyst Energy activation energy for catalyzed reaction reactants products AP Biology Reaction Progress Enzymes Biological catalysts (Ribozymes – proteins (& RNA) RNA can have catalytic properties) facilitate chemical reactions increase rate of reaction without being consumed reduce activation energy don’t change free energy (G) released or required required for most biological reactions highly specific thousands of different enzymes in cells control reactions of life AP Biology http://highered.mcgrawhill.com/sites/0072495855/student_view0/chapter2/animation__how_en zymes_work.html Enzymes vocabulary http://www.kscience.co.uk/animations/anim_2.htm substrate reactant which binds to enzyme enzyme-substrate complex: temporary association product end result of reaction active site enzyme’s catalytic site; substrate fits into active site active site substrate enzyme AP Biology enzymesubstrate complex products Properties of enzymes Reaction specific each enzyme works with a specific substrate chemical fit between active site & substrate H bonds & ionic bonds Not consumed in reaction single enzyme molecule can catalyze thousands or more reactions per second enzymes unaffected by the reaction Affected by cellular conditions any condition that affects protein structure temperature, pH, salinity 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) AP Biology http://highered.mcgrawhill.com/sites/0072495855/student_view0/chapter2/anim ation__how_enzymes_work.html Lock and Key model Simplistic model of enzyme action substrate fits into 3-D structure of enzyme active site H bonds, ionic bonds between substrate & enzyme like “key fits into lock” specificity AP Biology In biology… Shape matters! http://www.indiana.edu/~oso/animations/hexokinase.html 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 AP Biology http://web.chem.ucsb.edu/~molvisual/ABLE/induced_fit/ Models of enzyme activity AP Biology Enzymes are proteins Enzymes interact with substrate AP Biology proper substrate binding causes carboxypeptidase to "twist" a little Carboxypeptidase: Fit, strain, cut proper substrate binding causes carboxypeptidase to "twist" a little twisting enzyme brings 3 "R" groups closer to active site terminal peptide bond of substrate also twisted & strained once bond is strained, easy to break AP Biology How does it work? Variety of mechanisms to: lower activation energy & speed up reaction synthesis active site orients substrates in correct position for reaction enzyme brings substrate closer together digestion active site binds substrate & puts stress on bonds that must be broken, making it easier to separate molecules AP Biology Factors Affecting Enzyme Function Enzyme concentration Substrate concentration Temperature pH Salinity Activators Inhibitors AP Biology catalase Enzyme concentration reaction rate What’s happening here?! enzyme concentration AP Biology Factors affecting enzyme function Enzyme concentration as enzyme = reaction rate more enzymes = more frequently collide with substrate reaction rate levels off reaction rate substrate becomes limiting factor not all enzyme molecules can find substrate AP Biology enzyme concentration Substrate concentration reaction rate What’s happening here?! substrate concentration AP Biology Factors affecting enzyme function Substrate concentration as substrate = reaction rate more substrate = more frequently collide with enzyme reaction rate levels off reaction rate all enzymes have active site engaged enzyme is saturated maximum rate of reaction AP Biology substrate concentration Factors affecting enzyme function Temperature Optimum T° greatest number of molecular collisions human enzymes = 35°- 40°C body temp = 37°C Heat: increase beyond optimum T° increased energy level of molecules disrupts bonds in enzyme & between enzyme & substrate H, ionic = weak bonds denaturation = lose 3D shape (3° structure) Cold: decrease T° molecules move slower decrease collisions between enzyme & substrate AP Biology Temperature reaction rate What’s happening here?! 37° temperature http://www.wiley.com/college/boyer/0470003790/animations/protein_folding/prote AP Biology in_folding.htm Enzymes and temperature Different enzymes function in different organisms in different environments reaction rate human enzyme hot spring bacteria enzyme 37°C AP Biology temperature 70°C (158°F) pH What’s happening here?! trypsin reaction rate pepsin pepsin trypsin 0 AP Biology 1 2 3 4 5 6 pH 7 8 9 10 11 12 13 14 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 AP Biology 0 1 2 3 4 5 6 7 8 9 10 11 Salinity reaction rate What’s happening here?! salt concentration 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! AP Biology Compounds that help enzymes Fe in Activators hemoglobin cofactors non-protein, small inorganic compounds & ions Mg, K, Ca, Zn, Fe, Cu bound within enzyme molecule coenzymes non-protein, organic molecules bind temporarily or permanently to enzyme near active site many vitamins NAD (niacin; B3) FAD (riboflavin; B2) AP Biology Coenzyme A Mg in chlorophyll Compounds that regulate enzymes Inhibitors: molecules that reduce enzyme activity competitive inhibition noncompetitive inhibition irreversible inhibition feedback inhibition Distinguish between the mechanism of competitive and noncompetitive inhibitors. AP Biology Competitive & Noncompetitive Inhibitors Competitive Inhibition Noncompetitive Inhibition AP Biology Competitive Inhibitor Inhibitor & substrate “compete” for active site penicillin blocks enzyme bacteria use to build cell walls disulfiram (Antabuse) treats chronic alcoholism blocks enzyme that breaks down alcohol severe hangover & vomiting 5-10 minutes after drinking Overcome by increasing substrate concentration saturate solution with substrate so it out-competes inhibitor for active site on enzyme 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 some anti-cancer drugs inhibit enzymes involved in DNA synthesis stop DNA production stop division of cancer cells cyanide poisoning irreversible inhibitor of Cytochrome C, an enzyme in cellular respiration stops production of ATP AP Biology Irreversible inhibition Inhibitor permanently binds to enzyme competitor permanently binds to active site allosteric permanently binds to allosteric site permanently changes shape of enzyme nerve gas, sarin, many insecticides (malathion, parathion…) cholinesterase inhibitors AP Biology doesn’t breakdown the neurotransmitter, acetylcholine http://www.kscience.co.uk/animations/model.swf http://usmanscience.com/12bio/enzyme/en zyme_animations.htm Allosteric regulation Conformational changes by regulatory molecules inhibitors keeps enzyme in inactive form activators keeps enzyme in active form AP BiologyConformational changes Allosteric regulation Metabolic pathways 4 5 3 2 G A B C D E F ABCDEFG enzyme enzyme enzyme enzyme enzyme enzyme 1 Chemical reactions of life are organized in pathways divide chemical reaction into many small steps Advantageous evolutionarily efficiency intermediate branching points control = regulation AP Biology 6 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 AP Biology Feedback inhibition threonine 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 AP Biology isoleucine http://www.dnatube.com/video/274/HemoglobinOxygen-Binding Cooperativity Substrate acts as an activator substrate causes conformational change in enzyme induced fit favors binding of substrate at 2nd site makes enzyme more active & effective hemoglobin Hemoglobin 4 polypeptide chains can bind 4 O2; 1st O2 binds now easier for other O2 to bind AP3Biology Don’t be inhibited! Ask Questions! AP Biology 2013-2014