Chapter 8 Metabolism & Enzymes

Chapter 8 Metabolism & Enzymes

From food webs to the life of a cell
energy energy energy

Flow of energy through life
Life is built on chemical reactions transforming energy from one form to another organic molecules  ATP & organic molecules sun organic molecules  ATP & organic molecules solar energy  ATP & organic molecules

Concept 8.1: An organism’s metabolism transforms matter and energy, subject to the laws of thermodynamics Metabolism is the totality of an organism’s chemical reactions Metabolism is an emergent property of life that arises from interactions between molecules within the cell

Enzyme 1 Enzyme 2 Enzyme 3 A B C D Reaction 1 Reaction 2 Reaction 3 Starting molecule Product

That’s why they’re called anabolic steroids!
Metabolism Chemical reactions of life forming bonds between molecules dehydration synthesis synthesis anabolic reactions breaking bonds between molecules hydrolysis digestion catabolic reactions That’s why they’re called anabolic steroids!

Examples dehydration synthesis (synthesis) hydrolysis (digestion)
enzyme + H2O hydrolysis (digestion) enzyme + H2O

Examples dehydration synthesis (synthesis) hydrolysis (digestion)
enzyme hydrolysis (digestion) enzyme

Forms of Energy Energy is the capacity to cause change
Energy exists in various forms, some of which can perform work Kinetic energy is energy associated with motion Heat (thermal energy) is kinetic energy associated with random movement of atoms or molecules Potential energy is energy that matter possesses because of its location or structure Chemical energy is potential energy available for release in a chemical reaction Energy can be converted from one form to another

On the platform, the diver has more potential energy. Diving converts potential energy to kinetic energy. Climbing up converts kinetic energy of muscle movement to potential energy. In the water, the diver has less potential energy.

The Laws of Energy Transformation
Thermodynamics is the study of energy transformations A closed system, such as that approximated by liquid in a thermos, is isolated from its surroundings In an open system, energy and matter can be transferred between the system and its surroundings Organisms are open systems

The First Law of Thermodynamics
According to the first law of thermodynamics, the energy of the universe is constant Energy can be transferred and transformed Energy cannot be created or destroyed The first law is also called the principle of conservation of energy

The Second Law of Thermodynamics
During every energy transfer or transformation, some energy is unusable, often lost as heat According to the second law of thermodynamics, every energy transfer or transformation increases the entropy (disorder) of the universe

First law of thermodynamics Second law of thermodynamics
LE 8-3 CO2 Chemical energy Heat H2O First law of thermodynamics Second law of thermodynamics

Living cells unavoidably convert organized forms of energy to heat
Spontaneous processes occur without energy input; they can happen quickly or slowly For a process to occur without energy input, it must increase the entropy of the universe

Biological Order and Disorder
Cells create ordered structures from less ordered materials Organisms also replace ordered forms of matter and energy with less ordered forms The evolution of more complex organisms does not violate the second law of thermodynamics Entropy (disorder) may decrease in an organism, but the universe’s total entropy increases

Concept 8.2: The free-energy change of a reaction tells us whether the reaction occurs spontaneously
Biologists want to know which reactions occur spontaneously and which require input of energy To do so, they need to determine energy changes that occur in chemical reactions

Free-Energy Change, G A living system’s free energy is energy that can do work when temperature and pressure are uniform, as in a living cell

The change in free energy (∆G) during a process is related to the change in enthalpy, or change in total energy (∆H), and change in entropy (T∆S): ∆G = ∆H - T∆S Only processes with a negative ∆G are spontaneous Spontaneous processes can be harnessed to perform work

Free Energy, Stability, and Equilibrium
Free energy is a measure of a system’s instability, its tendency to change to a more stable state During a spontaneous change, free energy decreases and the stability of a system increases Equilibrium is a state of maximum stability A process is spontaneous and can perform work only when it is moving toward equilibrium

LE 8-5 Gravitational motion Diffusion Chemical reaction

Free Energy and Metabolism
The concept of free energy can be applied to the chemistry of life’s processes

Chemical reactions & energy
Some chemical reactions release energy exergonic digesting polymers hydrolysis = catabolism Some chemical reactions require input of energy endergonic building polymers dehydration synthesis = anabolism digesting molecules= less organization= lower energy state building molecules= more organization= higher energy state

Endergonic vs. exergonic reactions
- energy released - digestion energy invested synthesis +G -G G = change in free energy = ability to do work

Energy & life Organisms require energy to live
where does that energy come from? coupling exergonic reactions (releasing energy) with endergonic reactions (needing energy) energy + + energy + +

Stable polymers don’t spontaneously digest into their monomers
What drives reactions? If reactions are “downhill”, why don’t they just happen spontaneously? because covalent bonds are stable bonds Stable polymers don’t 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 Need a spark to start a fire energy cellulose CO2 + H2O + heat

Too much activation energy for life
The amount of energy needed to destabilize the bonds of a molecule moves the reaction over an “energy hill” Not a match! That’s too much energy to expose living cells to! 2nd Law of thermodynamics Universe tends to disorder so why don’t proteins, carbohydrates & other biomolecules breakdown? at temperatures typical of the cell, molecules don’t make it over the hump of activation energy but, a cell must be metabolically active heat would speed reactions, but… would denature proteins & kill cells

Reducing Activation energy
Catalysts reducing the amount of energy to start a reaction Pheeew… that takes a lot less energy!

Equilibrium and Metabolism
Reactions in a closed system eventually reach equilibrium and then do no work Cells are not in equilibrium; they are open systems experiencing a constant flow of materials A catabolic pathway in a cell releases free energy in a series of reactions Closed and open hydroelectric systems can serve as analogies

Concept 8.3: ATP powers cellular work by coupling exergonic reactions to endergonic reactions
A cell does three main kinds of work: Mechanical Transport Chemical To do work, cells manage energy resources by energy coupling, the use of an exergonic process to drive an endergonic one

The Structure and Hydrolysis of ATP
ATP (adenosine triphosphate) is the cell’s energy shuttle ATP provides energy for cellular functions

LE 8-8 Adenine Phosphate groups Ribose

The bonds between the phosphate groups of ATP’s tail can be broken by hydrolysis
Energy is released from ATP when the terminal phosphate bond is broken This release of energy comes from the chemical change to a state of lower free energy, not from the phosphate bonds themselves

Adenosine triphosphate (ATP)
LE 8-9 P P P Adenosine triphosphate (ATP) H2O P + P P + Energy i Inorganic phosphate Adenosine diphosphate (ADP)

In the cell, the energy from the exergonic reaction of ATP hydrolysis can be used to drive an endergonic reaction Overall, the coupled reactions are exergonic

Glutamic acid Ammonia Glutamine ATP H2O ADP
LE 8-10 Endergonic reaction: DG is positive, reaction is not spontaneous NH2 + NH3 DG = +3.4 kcal/mol Glu Glu Glutamic acid Ammonia Glutamine Exergonic reaction: DG is negative, reaction is spontaneous ATP + H2O ADP P + DG = –7.3 kcal/mol i Coupled reactions: Overall DG is negative; together, reactions are spontaneous DG = –3.9 kcal/mol

How ATP Performs Work ATP drives endergonic reactions by phosphorylation, transferring a phosphate group to some other molecule, such as a reactant The recipient molecule is now phosphorylated The three types of cellular work (mechanical, transport, and chemical) are powered by the hydrolysis of ATP

Reactants: Glutamic acid
LE 8-11 P i P Motor protein Protein moved Mechanical work: ATP phosphorylates motor proteins Membrane protein ADP ATP + P i P P i Solute Solute transported Transport work: ATP phosphorylates transport proteins P NH2 + NH3 Glu + P i Glu Reactants: Glutamic acid and ammonia Product (glutamine) made Chemical work: ATP phosphorylates key reactants

The Regeneration of ATP
ATP is a renewable resource that is regenerated by addition of a phosphate group to ADP The energy to phosphorylate ADP comes from catabolic reactions in the cell The chemical potential energy temporarily stored in ATP drives most cellular work

Energy for cellular work (endergonic, energy- consuming processes)
LE 8-12 ATP Energy for cellular work (endergonic, energy- consuming processes) Energy from catabolism (energonic, energy- yielding processes) ADP P + i

Concept 8.4: Enzymes speed up metabolic reactions by lowering energy barriers
A catalyst is a chemical agent that speeds up a reaction without being consumed by the reaction An enzyme is a catalytic protein Hydrolysis of sucrose by the enzyme sucrase is an example of an enzyme-catalyzed reaction

LE 8-13 Sucrose C12H22O11 Glucose C6H12O6 Fructose C6H12O6

The Activation Energy Barrier
Every chemical reaction between molecules involves bond breaking and bond forming The initial energy needed to start a chemical reaction is called the free energy of activation, or activation energy (EA) Activation energy is often supplied in the form of heat from the surroundings

Progress of the reaction
LE 8-14 A B C D Transition state A B EA Free energy C D Reactants A B DG < O C D Products Progress of the reaction

How Enzymes Lower the EA Barrier
Enzymes catalyze reactions by lowering the EA barrier Enzymes do not affect the change in free-energy (∆G); instead, they hasten reactions that would occur eventually Animation: How Enzymes Work

Progress of the reaction
LE 8-15 Course of reaction without enzyme EA without enzyme EA with enzyme is lower Reactants Free energy Course of reaction with enzyme DG is unaffected by enzyme Products Progress of the reaction

Substrate Specificity of Enzymes
The reactant that an enzyme acts on is called the enzyme’s substrate The enzyme binds to its substrate, forming an enzyme-substrate complex The active site is the region on the enzyme where the substrate binds Induced fit of a substrate brings chemical groups of the active site into positions that enhance their ability to catalyze the reaction

LE 8-16 Substrate Active site Enzyme Enzyme-substrate complex

Catalysis in the Enzyme’s Active Site
In an enzymatic reaction, the substrate binds to the active site The active site can lower an EA barrier by Orienting substrates correctly Straining substrate bonds Providing a favorable microenvironment Covalently bonding to the substrate

LE 8-17 Substrates enter active site; enzyme changes shape so its active site embraces the substrates (induced fit). Substrates held in active site by weak interactions, such as hydrogen bonds and ionic bonds. Active site (and R groups of its amino acids) can lower EA and speed up a reaction by acting as a template for substrate orientation, stressing the substrates and stabilizing the transition state, providing a favorable microenvironment, participating directly in the catalytic reaction. Substrates Enzyme-substrate complex Active site is available for two new substrate molecules. Enzyme Products are released. Substrates are converted into products. Products

Effects of Local Conditions on Enzyme Activity
An enzyme’s activity can be affected by: General environmental factors, such as temperature and pH Chemicals that specifically influence the enzyme

Effects of Temperature and pH
Each enzyme has an optimal temperature in which it can function Each enzyme has an optimal pH in which it can function

LE 8-18 Optimal temperature for typical human enzyme Optimal temperature for enzyme of thermophilic (heat-tolerant bacteria) Rate of reaction 20 40 60 80 100 Temperature (°C) Optimal temperature for two enzymes Optimal pH for pepsin (stomach enzyme) Optimal pH for trypsin (intestinal enzyme) Rate of reaction 1 2 3 4 5 6 7 8 9 10 pH Optimal pH for two enzymes

Cofactors Cofactors are nonprotein enzyme helpers
Coenzymes are organic cofactors

Enzyme Inhibitors Competitive inhibitors bind to the active site of an enzyme, competing with the substrate Noncompetitive inhibitors bind to another part of an enzyme, causing the enzyme to change shape and making the active site less effective

LE 8-19 A substrate can bind normally to the active site of an enzyme. Substrate Active site Enzyme Normal binding A competitive inhibitor mimics the substrate, competing for the active site. Competitive inhibitor Competitive inhibition A noncompetitive inhibitor binds to the enzyme away from the active site, altering the conformation of the enzyme so that its active site no longer functions. Noncompetitive inhibitor Noncompetitive inhibition

Concept 8.5: Regulation of enzyme activity helps control metabolism
Chemical chaos would result if a cell’s metabolic pathways were not tightly regulated To regulate metabolic pathways, the cell switches on or off the genes that encode specific enzymes

Allosteric Regulation of Enzymes
Allosteric regulation is the term used to describe cases where a protein’s function at one site is affected by binding of a regulatory molecule at another site Allosteric regulation may either inhibit or stimulate an enzyme’s activity

Allosteric Activation and Inhibition
Most allosterically regulated enzymes are made from polypeptide subunits Each enzyme has active and inactive forms The binding of an activator stabilizes the active form of the enzyme The binding of an inhibitor stabilizes the inactive form of the enzyme

Active site (one of four)
LE 8-20a Allosteric activator stabilizes active form. Allosteric enzyme with four subunits Active site (one of four) Regulatory site (one of four) Activator Active form Stabilized active form Oscillation Allosteric inhibitor stabilizes inactive form. Non- functional active site Inhibitor Inactive form Stabilized inactive form Allosteric activators and inhibitors

Cooperativity is a form of allosteric regulation that can amplify enzyme activity
In cooperativity, binding by a substrate to one active site stabilizes favorable conformational changes at all other subunits

Binding of one substrate molecule to
LE 8-20b Binding of one substrate molecule to active site of one subunit locks all subunits in active conformation. Substrate Inactive form Stabilized active form Cooperativity another type of allosteric activation

Feedback Inhibition In feedback inhibition, the end product of a metabolic pathway shuts down the pathway Feedback inhibition prevents a cell from wasting chemical resources by synthesizing more product than is needed

LE 8-21 Initial substrate (threonine) Active site available Threonine
in active site Enzyme 1 (threonine deaminase) Isoleucine used up by cell Intermediate A Feedback inhibition Enzyme 2 Active site of enzyme 1 can’t bind theonine pathway off Intermediate B Enzyme 3 Intermediate C Isoleucine binds to allosteric site Enzyme 4 Intermediate D Enzyme 5 End product (isoleucine)

Specific Localization of Enzymes Within the Cell
Structures within the cell help bring order to metabolic pathways Some enzymes act as structural components of membranes Some enzymes reside in specific organelles, such as enzymes for cellular respiration being located in mitochondria

sites of cellular respiration
LE 8-22 Mitochondria, sites of cellular respiration 1 µm

Catalysts So what’s a cell got to do to reduce activation energy?
get help! … chemical help… ENZYMES Call in the ENZYMES! G

Enzymes Biological catalysts proteins (& RNA)
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

Enzymes vocabulary substrate product active site active site products
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 products substrate enzyme

Properties of enzymes Reaction specific Not consumed in reaction
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

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)

Size doesn’t matter… Shape matters!
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” Size doesn’t matter… Shape matters!

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

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 diegstion active site binds substrate & puts stress on bonds that must be broken, making it easier to separate molecules

Got any Questions?!

Factors that Affect Enzymes

Factors Affecting Enzyme Function
Enzyme concentration Substrate concentration Temperature pH Salinity Activators Inhibitors Living with oxygen is dangerous. We rely on oxygen to power our cells, but oxygen is a reactive molecule that can cause serious problems if not carefully controlled. One of the dangers of oxygen is that it is easily converted into other reactive compounds. Inside our cells, electrons are continually shuttled from site to site by carrier molecules, such as carriers derived from riboflavin and niacin. If oxygen runs into one of these carrier molecules, the electron may be accidentally transferred to it. This converts oxygen into dangerous compounds such as superoxide radicals and hydrogen peroxide, which can attack the delicate sulfur atoms and metal ions in proteins. To make things even worse, free iron ions in the cell occasionally convert hydrogen peroxide into hydroxyl radicals. These deadly molecules attack and mutate DNA. Fortunately, cells make a variety of antioxidant enzymes to fight the dangerous side-effects of life with oxygen. Two important players are superoxide dismutase, which converts superoxide radicals into hydrogen peroxide, and catalase, which converts hydrogen peroxide into water and oxygen gas. The importance of these enzymes is demonstrated by their prevalence, ranging from about 0.1% of the protein in an E. coli cell to upwards of a quarter of the protein in susceptible cell types. These many catalase molecules patrol the cell, counteracting the steady production of hydrogen peroxide and keeping it at a safe level. Catalases are some of the most efficient enzymes found in cells. Each catalase molecule can decompose millions of hydrogen peroxide molecules every second. The cow catalase shown here and our own catalases use an iron ion to assist in this speedy reaction. The enzyme is composed of four identical subunits, each with its own active site buried deep inside. The iron ion, shown in green, is gripped at the center of a disk-shaped heme group. Catalases, since they must fight against reactive molecules, are also unusually stable enzymes. Notice how the four chains interweave, locking the entire complex into the proper shape. catalase

Enzyme concentration reaction rate enzyme concentration
What’s happening here?! reaction rate enzyme concentration

Factors affecting enzyme function
Enzyme concentration as  enzyme =  reaction rate more enzymes = more frequently collide with substrate reaction rate levels off substrate becomes limiting factor not all enzyme molecules can find substrate Why is it a good adaptation to organize the cell in organelles? Sequester enzymes with their substrates! enzyme concentration reaction rate

Substrate concentration
What’s happening here?! reaction rate substrate concentration

Substrate concentration as  substrate =  reaction rate more substrate = more frequently collide with enzyme reaction rate levels off all enzymes have active site engaged enzyme is saturated maximum rate of reaction Why is it a good adaptation to organize the cell in organelles? Sequester enzymes with their substrates! substrate concentration reaction rate

Temperature What’s happening here?! 37° reaction rate temperature

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

Enzymes and temperature
Different enzymes function in different organisms in different environments hot spring bacteria enzyme human enzyme 37°C 70°C reaction rate temperature (158°F)

How do ectotherms do it? Enzymes work within narrow temperature ranges. Ectotherms, like snakes, do not use their metabolism extensively to regulate body temperature. Their body temperature is significantly influenced by environmental temperature. Desert reptiles can experience body temperature fluctuations of ~40°C (that’s a ~100°F span!). What mechanism has evolved to allow their metabolic pathways to continue to function across that wide temperature span?

pH pepsin trypsin reaction rate pH 1 2 3 4 5 6 7 8 9 10 11 12 13 14
What’s happening here?! pepsin trypsin pepsin reaction rate trypsin 1 2 3 4 5 6 7 8 9 10 11 12 13 14 pH

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 7 2 1 3 4 5 6 8 9 10 11

Salinity What’s happening here?! reaction rate salt concentration

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!

Compounds which help enzymes
Activators 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) Coenzyme A Fe in hemoglobin Hemoglobin is aided by Fe Chlorophyll is aided by Mg Mg in chlorophyll

Compounds which regulate enzymes
Inhibitors molecules that reduce enzyme activity competitive inhibition noncompetitive inhibition irreversible inhibition feedback inhibition

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 Ethanol is metabolized in the body by oxidation to acetaldehyde, which is in turn further oxidized to acetic acid by aldehyde oxidase enzymes. Normally, the second reaction is rapid so that acetaldehyde does not accumulate in the body. A drug, disulfiram (Antabuse) inhibits the aldehyde oxidase which causes the accumulation of acetaldehyde with subsequent unpleasant side-effects of nausea and vomiting. This drug is sometimes used to help people overcome the drinking habit. Methanol (wood alcohol) poisoning occurs because methanol is oxidized to formaldehyde and formic acid which attack the optic nerve causing blindness. Ethanol is given as an antidote for methanol poisoning because ethanol competitively inhibits the oxidation of methanol. Ethanol is oxidized in preference to methanol and consequently, the oxidation of methanol is slowed down so that the toxic by-products do not have a chance to accumulate.

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 more cancer cells cyanide poisoning irreversible inhibitor of Cytochrome C, an enzyme in cellular respiration stops production of ATP Basis of most chemotherapytreatments is enzyme inhibition. Many health disorders can be controlled, in principle, by inhibiting selected enzymes. Two examples include methotrexate and FdUMP, common anticancer drugs which inhibit enzymes involved in the synthesis of thymidine and hence DNA. Since many enzymes contain sulfhydral (-SH), alcohol, or acid groups as part of their active sites, any chemical which can react with them acts as a noncompetitive inhibitor. Heavy metals such as silver (Ag+), mercury (Hg2+), lead ( Pb2+) have strong affinities for -SH groups. Cyanide combines with the copper prosthetic groups of the enzyme cytochrome C oxidase, thus inhibiting respiration which causes an organism to run out of ATP (energy) Oxalic and citric acid inhibit blood clotting by forming complexes with calcium ions necessary for the enzyme metal ion activator.

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 doesn’t breakdown the neurotransmitter, acetylcholine Another example of irreversible inhibition is provided by the nerve gas diisopropylfluorophosphate (DFP) designed for use in warfare. It combines with the amino acid serine (contains the –SH group) at the active site of the enzyme acetylcholinesterase. The enzyme deactivates the neurotransmitter acetylcholine. Neurotransmitters are needed to continue the passage of nerve impulses from one neurone to another across the synapse. Once the impulse has been transmitted, acetylcholinesterase functions to deactivate the acetycholine almost immediately by breaking it down. If the enzyme is inhibited, acetylcholine accumulates and nerve impulses cannot be stopped, causing prolonged muscle contration. Paralysis occurs and death may result since the respiratory muscles are affected. Some insecticides currently in use, including those known as organophosphates (e.g. parathion), have a similar effect on insects, and can also cause harm to nervous and muscular system of humans who are overexposed to them.

Allosteric regulation
Conformational changes by regulatory molecules inhibitors keeps enzyme in inactive form activators keeps enzyme in active form Conformational changes Allosteric regulation

Metabolic pathways A  B  C  D  E  F  G A  B  C  D  E  F  G
enzyme 1  enzyme 3  enzyme 2  enzyme  enzyme 4  enzyme 5  enzyme 6  Chemical reactions of life are organized in pathways divide chemical reaction into many small steps artifact of evolution  efficiency intermediate branching points  control = regulation

Whoa! All that going on in those little mitochondria!
Efficiency Organized groups of enzymes enzymes are embedded in membrane and arranged sequentially Link endergonic & exergonic reactions Whoa! All that going on in those little mitochondria!

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  G enzyme 1  enzyme 2  enzyme 3  enzyme 4  enzyme 5  enzyme 6  X allosteric inhibitor of enzyme 1

Feedback inhibition Example
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 isoleucine

Don’t be inhibited! Ask Questions!

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 3 O2 to bind

Chapter 8 Metabolism & Enzymes

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