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LS Enzymes

The document provides an overview of enzymes as biological catalysts, detailing their functions, mechanisms of action, and the models that explain enzyme activity, such as the 'Lock and Key' and 'Induced Fit' hypotheses. It also discusses the types of enzymes, their role in metabolism, and factors affecting enzyme activity, including substrate concentration. Additionally, it includes starter questions and answers related to biochemistry concepts relevant to enzymes.

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6 views17 pages

LS Enzymes

The document provides an overview of enzymes as biological catalysts, detailing their functions, mechanisms of action, and the models that explain enzyme activity, such as the 'Lock and Key' and 'Induced Fit' hypotheses. It also discusses the types of enzymes, their role in metabolism, and factors affecting enzyme activity, including substrate concentration. Additionally, it includes starter questions and answers related to biochemistry concepts relevant to enzymes.

Uploaded by

portosachantelle
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PDF, TXT or read online on Scribd
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Date: 9 October, 2024

Title: Enzymes

Objectives:
▪ Describe enzymes as biological catalysts
▪ Explain how enzymes work in cells to increase the rate of
reaction
▪ Use ‘Lock and key’ and Induced fit’ models to explain
enzyme action
Starter questions:

1. What two monosaccharides are produced when lactose is


hydrolysed?
2. What is the difference between α and β glucose?
3. How is a triglyceride structure different from a phospholipid
structure?
4. What makes the 20 amino acids different?
5. What bonding is responsible for the tertiary structure in
proteins?
6. What is responsible for the surface tension between water and
air?
Starter answers:

1. Glucose and galactose


2. The OH (hydroxyl) group on carbon at position 1 is
above the ring in β glucose, below the ring in α glucose
(orientation of the OH on carbon 1)
3. A triglyceride has three fatty acids attached to the
glycerol molecule. A phospholipid has two fatty acids
and a ‘phosphate-containing’ group attached to the
glycerol
4. The nature of the R-group
5. Hydrogen bonding, ionic interaction, covalent bonding
in disulphide bridge (-S-S-) and
hydrophilic/hydrophobic interactions
6. Hydrogen bonding between water molecules
Key words and terms
• Enzyme • Induced fit hypothesis
• Substrate • Enzyme-product
• Biological catalyst complex
• Enzyme-substrate • Activation energy
complex • Metabolic
• Active site • Competition
• Specificity • Inhibitor
• Lock-and-key • Cofactor
hypothesis • Coenzyme
Enzymes
• Globular proteins
• Biological catalysts
• Small region on surface – active site
• Specific – only catalyse certain reactions
• Sensitive to temperature, pH, ion
concentration
Lock-and-key hypothesis
• Molecule/molecules with complementary
shape bind to the active site
• Temporary bonds formed with amino acids of
the active site forming and enzyme-substrate
complex
• Enzyme holds the substrate such that a
reaction takes place more easily than without
• Products are released, enzyme unchanged
Lock-and-key...
Induced fit hypothesis
• Similar to lock-and-key
• Substrate binds and enzyme molecule changes
shape to fit more closely around the substrate
Induced fit
Catalysts
• Lower the activation energy of a chemical
reaction
• Reactions can happen at lower temperatures
than without a catalyst
• Many reactions can happen at body
temperature which would otherwise occur
very slowly
Activation energy
Metabolism
• Sum of enzyme-controlled chemical reactions
in an organism
• Catabolism – breaking-down reactions
(hydrolysis)
• Anabolism – building-up reactions
(condensation)
• Some are intracellular, some are extracellular
Types of enzyme
• Hydrolase – hydrolyse molecules
• Synthetase – synthesise molecules
• Hydrase – hydrate molecules
• Isomerase – change the arrangement
• Carboxylase – add CO2
• Decarboxylase – remove CO2
• Polymerase – join things together
• Hydrogenase – add hydrogen
• Dehydrogenase – remove hydrogen
Rates of enzyme-controlled reactions
• Found by determining the quantity of substrate
used or the product produced with time
• Initial rate is given by the gradient of the line at
the start of the reaction, e.g. volume of gas
produced against time (initial rate)
• Use the following results to plot a graph and find
the initial rate of the reaction
• Label and annotate the graph to show where
substrate is limiting, and where enzyme is limiting
Time (s) Volume O2 (cm3)

0 0.0

30 2.8

60 4.6

90 5.4

120 6.1

150 6.3

180 6.5

210 6.7

240 6.7
Effect of substrate concentration
• With an unlimited supply of enzyme, rate
increases with increase in substrate
concentration
• With a limited supply of enzyme, rate
increases and then ‘levels off’ as the enzymes
molecules are all being used – active sites are
all occupied, and no further reaction can
happen until an active site becomes available
Objective questions:

1. What is an enzyme?
2. Which part of the enzyme molecule is involved in the
catalysis of biochemical reactions?
3. What is meant by the ‘induced fit hypothesis’ of enzyme
action?

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