8.1 Metabolism (HL)

8.
1 - Metabolism (HL)
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abolism_ZP.svg/300px-Insulin_glucose_metabolism_ZP.svg.png
Metabolic pathways consist of chains and cycles of enzyme-
catalysed reactions.
Metabolism
● All the chemical reactions that occur in organisms in order to maintain life (eg.
ATP synthesis during cellular respiration)
● Enzymes catalyse each reaction along each metabolic pathway

○ Some pathways are anabolic, building up
organic molecules
○ other pathways are catabolic, breaking down
large organic molecules into smaller ones
● Some metabolic reactions are cycles

(eg. Krebs Cycle) and some are linear
chains (eg. Glycolysis)
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Enzymes lower the activation energy of the chemical reactions that
they catalyse.
Activation energy
● Energy that must be overcome in order for a chemical reaction to occur
○ the energy needed to weaken and break the chemical bonds of the substrate
● Enzymes work by lowering activation energy needed for the reaction to occur
○ When substrate binds to active site, enzyme changes
conformational shape, altering shape of active site.
○ Changing shape destabilizes the bonds of the bound
substrate.
○ Less energy is required for the reaction to take place.
● More substrates can be converted into more

products & rate of reaction increases dramatically
Enzyme inhibitors can be competitive or non-competitive.
Enzyme inhibition occurs when molecules bind to enzymes and decreases their
activity.
Two types of enzyme inhibition are:

● Competitive
● Non-competitive inhibition.
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Competitive Inhibition
● Occurs when a molecule structurally similar to the substrate competes directly
with substrate for access to the active site
○ inhibitor blocks the substrate from binding to the enzyme
○ decreases the number of times a substrate interacts with an enzyme
○ less enzyme/substrate interactions means reaction rate decreases
● Is usually reversible but can be irreversible
● Can be overcome by increasing the

concentration of substrate and out-competing
the inhibitor
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mb/f/fb/Comp_inhib.svg/350px-Comp_inhib.svg.png
Non-Competitive Inhibition
● Occurs when an inhibitor binds to a separate site (not the active site) on the
enzyme
○ changes the conformational shape of the enzyme (including active site)
○ the substrate can no longer bind to the enzyme for a reaction to occur
● Also called allosteric inhibition; site where inhibitor binds is called the
allosteric site
● Increasing concentration of the substrate will

not speed up the reaction or reduce the
effect of the inhibitor
● Usually reversible
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ric_comp_inhib_1.svg/350px-Allosteric_comp_inhib_1.svg.png
Examples of Competitive Inhibition
1. Introduce ethanol (eg. drinking alcohol) to compete with and inhibit the
oxidation of methanol
○ If someone accidently drinks methanol they can become blind and actually die depending on
the amount.
■ As methanol is oxidized it forms formaldehyde and formic acid that can attack the optic
nerve.
○ Ethanol competes with methanol for the active site on the enzyme alcohol dehydrogenase.
The by-products of ethanol are much less toxic.
More than 60 People Killed by Laced Homemade Alcohol

Many enzyme inhibitors have been used in medicine.
2. Ethanol can be used as a competitive inhibitor for antifreeze
poisoning
○ Inhibit alcohol dehydrogenase from metabolizing ethylene glycol into
glycolic acid & oxalic acid (causes kidney damage)
● The main ingredient in antifreeze is called ethylene glycol

○ Ethylene glycol is a toxic, colourless, odorless liquid with a sweet taste
○ Symptoms include feelings of intoxication and nausea, followed
by vomiting, hyperventilation, acidosis and acute kidney failure.
● Treatment must start as soon as possible to prevent

kidney failure
○ Ethanol outcompetes ethylene glycol for active site (100X) &
ethylene glycol is excreted in urine
Examples of Non-Competitive Inhibition
1. ATP acts as an allosteric inhibitor in the conversion of glycogen to glucose
phosphate in a metabolic pathway
○ ATP binds to the enzyme Glycogen phosphorylase that catalyzes this reaction
○ Prevents the over production of glucose and ATP if it is not needed.
2. Heavy metals such as Ag+, Hg2+ and Pb2+ bind with enzymes
○ Inhibit the enzyme function
3. Fomepizole - used as a non-competitive inhibitor for antifreeze poisoning

○ Approved antidote of the US FDA
○ Binds to the allosteric site of the enzyme & changes the shape
■ ethylene glycol can no longer bind to the active site
○ Since this is non-competitive, dosage adjustments and blood monitoring do not have to be
performed as with ethanol treatment
○ Fomepizole is an expensive alternative to ethanol
Distinguishing different types of inhibition from graphs at specified
substrate concentration.
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Metabolic pathways can be controlled by end-product inhibition.
● Allosteric (non-competitive) inhibition plays an important role in controlling
metabolic pathways
○ Occurs when a metabolic pathway produces a specific product that can also act as an inhibitor
to the metabolic pathway.
● Prevents the cell from over producing products it does not need
○ If a cell makes too much of a product, the product will inhibit the first enzyme in the metabolic
pathway, stopping the metabolic pathway from producing unneeded product
○ Prevents the cell from creating excess waste or using valuable energy resources
● As the end-product is used up, the metabolic pathway starts again as the first
enzyme is reactivated.
○ eg. if too much ATP is produced, ATP acts as an allosteric inhibitor in the conversion of
glycogen to glucose phosphate. ATP binds to the enzyme that catalyzes the reaction
preventing the over production of ATP.
End-product inhibition of the pathway that converts threonine to
isoleucine.
● Isoleucine in an essential amino acid
● High isoleucine concentration inhibits enzyme chain & pathway stops

○ When concentration (and inhibition) drops, production begins again
● Negative Feedback Loop
http://ib.bioninja.com.au/_Media/isoleucine-production_med.jpeg
Use of databases to identify potential new anti-malarial drugs.
● Malaria is caused by the protist Plasmodium falciparum
● Increased resistance of P. falciparum to anti-malarial drugs and global efforts
to eradicate malaria drive the need to produce new anti-malarial drugs
○ P. falciparum strain 3D7 has been sequenced by
scientists and used to test for new possible
medications
○ One study tested over 300,000 chemicals against
chloroquine-sensitive and chloroquine-resistant
strains
○ The results showed that 19 new chemicals inhibited
the enzymes normally targeted by anti-malarial drugs
and 15 chemicals that bound to a total of 61 different
malarial proteins.
○ Competitive & non-competitive inhibition will be
involved in many of these drug interactions
● This research provides starting points to produce possible new anti-malarial drugs
Calculating and plotting rates of reaction from raw experimental
results.
Catalase enzyme found in the cells of many living tissues speeds up the reaction
that breaks down hydrogen peroxide, a toxic chemical, produced in peroxisomes
2H2O2 → 2H2O + O2
If the cells did not break down the hydrogen peroxide, they would be poisoned and
die.
Use the data provided to complete the activity on beef liver degradation by H2O2
Complete
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8.1 Metabolism (HL)

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8.

● Enzymes catalyse each reaction along each metabolic pathway

● Some metabolic reactions are cycles

● More substrates can be converted into more

Two types of enzyme inhibition are:

● Is usually reversible but can be irreversible

● Can be overcome by increasing the

● Increasing concentration of the substrate will

More than 60 People Killed by Laced Homemade Alcohol

● The main ingredient in antifreeze is called ethylene glycol

● Treatment must start as soon as possible to prevent

3. Fomepizole - used as a non-competitive inhibitor for antifreeze poisoning

● High isoleucine concentration inhibits enzyme chain & pathway stops

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