Christi Barr – Clicker 2 7 October 2009

Block 4
Enzymes (Chapter 6) Notes
http://bio1152.nicerweb.com/Locked/media/doc/Art/

• Metabolism – the total of the chemical reactions in an organism

• Catabolism – breaking down
o Cellular respirations
• Anabolism – building up
o Photosynthesis
• Metabolism = catabolism + anabolism
• Laws of Thermodynamics
o 1st Law – energy can be transferred but neither created nor destroyed
o 2nd Law – transfers of energy increase entropy (disorder)
• Free energy
o Like potential energy
o Symbolized by letter G
o Is energy available to do work
o Changes that occur in a reaction are
delta G
o Spontaneous
 System becomes more stable
 Delta G is less than zero
 The released free energy can
be harnessed to do work
• Delta G = Gfinal – Gstarting
o Spontaneous – delta G = - (energy never released)
o Non-spontaneous – delta G = + (energy must be added)
• Reactions are either:
o Exergonic – release energy, spontaneous, loss of free energy, - delta G
(think respiration)
o Endergonic – absorbs energy non-spontaneous, gain of free energy,
+deltaG (think photosynthesis)
• http://www.columbia.edu/cu/biology/courses/c2005/purves6/figure06-05.jpg
• delta G of zero
o found in systems at equilibrium
o can do no work
o Cells at metabolic equilibrium is dead
o Disequilibrium is maintained because living things are open systems
o Fuel sources in (high in free energy) and waste is out (low in free energy)
• Energy Coupling
o Living things tie the release of free energy by some molecules (like
glucose) to the gain of free energy of other molecules
o ATP couples exergonic and endergonic reactions
• Cellular Work
o Mechanical

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o Transport
o Chemical
• ATP – adenosine triphosphate (picture)
• Purina double dog chow; Pure as gold (purine: adenine, guanine)
• ATP Hydrolysis
o Non spontaneous (picture)
• If ATP were directly hydrolyzed in the cell, it would just release heat
• If, however, the hydrolysis is coupled with a transfer of a phosphate froup to
another molecule, more of the energy can be used
• The molecule is said to be phosphorylated
• ATP Cycle

o
o Energy used to phosphorylate ADP is released in catabolic reactions
o ATP couples the cell’s energy – yielding processed to energy-consuming
processes
• Reaction Profile

o
o 1. Need a collision of sufficient impact and correct orientation
“productive collision”
o 2. Bonds distort
o 3. New products are more stable – lower free energy
o 4. Before they can react they much climb the activation energy hill
• Enzyme Action

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o Enzymes don’t change deltaG, they lower the activation energy needed

o
• Enzymes and Catalysts
o Biochemical reactions require enzymes to speed up and control reaction
rates
o Catalyst – chemical agent that accelerates a reaction without being
permanently changed in the process so it can be reused
o Enzyme – proteins which are biological catalysts
• Enzyme Characteristics
o Most enzymes are proteins
o They lower activation energy
o Do NOT change deltaG
o Act on a substrate (thing getting broken apart)
o Are selective and specific
o Commonly named with –ase ending
o Work because of their shape, destroy shape, destroy enzyme function
o Have an active site where substrate fits
o Can be controlled
• Enzyme Induced Fit

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• Catalytic Cycle

o
o Substrate binds to active site
o Forms enzyme-substrate complex due to chemical interactions
o Induced fit – side chains of a few amino acids catalyze the reaction
o Product departs – enzyme resumes original shape
• Enzyme Rap
o Enzyme Structure’s one of a kind
o 3-D shape will let it bind
o Enzyme-structure is not snug
o Induced fit provides a hug
o Most are protein don’t you know
o Amino acid “r” groups show
o Specific is the site that active
o Only one thing is reactive
o A groove we see as the active site
o Substrates come and fit here tight
o Catalytic cycle is the enzyme way
o Fit, fill, hug, release all day
• SIP SAC
o Structure
o Induced fit
o Protein
o Specific
o Active site
o Catalytic cycle
• Enzyme Regulation
o Is affected by many different things
 Environmental conditions (pH, temperature, ionic concentration)

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 Cofactors
• Non-protein helpers needed for catalysis by many enzymes
• May be permanently bound to the active site
• May bind at the same time as the substrate
• Some cofactors are inorganic like metal
• Organic cofactors are called coenzymes and are often
vitamins or derived from vitamins
 Enzyme Inhibitors
• Competitive
• Non-competitive
 Allosteric site interactions
• Activators
• Inhibitors

o GRAPHS ON TEST!!!!
• Enzyme Inhibition
o If the enzyme attaches covalently it is usually irreversible, weak bonds are
usually reversible

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o Competitive
 Compete for the active site
 Similar to normal substrate
 Reduces productivity – active sites are “busy”
 If reversible increasing substrate concentration will overcome
inhibitor
o Non-competitive
 Bind to a part of the enzyme away from the active site
 Causes shape change which inactivates or reduces activity
• Allosteric Regulation
o Inhibition and Activation are important in enzyme control
o Most regulating molecules bind to an Allosteric site, a receptor site
different from the active site

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o
o Allosteric inhibitors are a type of non-competitive inhibitor
o Inhibitors and activators are attached by weak bonds and are affected by
concentration
o The activator and the inhibitor may be similar enough in shape to compete
for the Allosteric site making concentration the driving factor for whether
or not a reaction proceeds
o Most enzymes with allosteric sites are made of two or more polypeptide
chains. The allosteric site is usually found where the subunits join
• Enzyme Cooperativity
o Seen when an enzyme has two or more subunits
o Amplifies the response of enzymes to the substrate
o One substrate molecule stabilizes the enzyme to accept additional
substrate
• Feedback Inhibition

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Block 4

o
o Common way metabolism is controlled
o Metabolic pathway is turned off by its end product
o The end product inhibits an enzyme in the pathway
• One Practical Use of Enzymes
o Use of lactase in production of lactose-free milk
 1. Most humans born with the enzyme lactase that digest lactose
 2. Production of lactase is gradually lost as people age (in many
people)
 3. When milk products are consumed, bacteria feast on the lactose
leading to cramping, gas and diarrhea
 4. Lactase can be added to milk products to pre-digest the lactose

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