Lecture-4-Microbial Metabolism Lecture Part A

1
Microbial Metabolism
Microbial Metabolism 3
 The reactions that are unique to bacteria are fascinating because they
allow microorganisms to do things we cannot do.
 For example, some bacteria can live on cellulose. whereas others can
live on petroleum.
 Through their metabolism, bacteria recycle elements after other

organisms have used them.
 Still other bacteria can live on diets of such inorganic substances as

carbon dioxide, iron, sulfur, hydrogen gas, and ammonia.
Metabolism 4
 The sum of all chemical reactions within a living organism.
 Chemical reactions either release or require energy,

 metabolism can be viewed as an energy-balancing act.
 Accordingly, metabolism can be divided into two classes of chemical

reactions:
 those that release energy
 those that require energy
Catabolism 5
 In living cells, the enzyme-regulated chemical reactions that release

energy are generally the ones involved in catabolism, the breakdown
of complex organic compounds into simpler ones.
 These reactions are called catabolic, or degradative, reactions.
 Catabolic reactions are generally hydrolytic reactions (reactions

which use water and in which chemical bonds are broken), and they
are exergonic (produce more energy than they consume).
 An example of catabolism occurs when cells break down sugars into

carbon dioxide and water.
Anabolism 6
 The enzyme-regulated energy- requiring reactions are mostly involved in anabolism,
the building of complex organic molecules from simpler ones.
 These reactions are called anabolic, or biosynthetic, reactions.
 Anabolic processes often involve dehydration synthesis reactions (reactions that

release water), and they are endergonic (consume more energy than they produce).
 Examples of anabolic processes arc the formation of proteins from amino acids,
nucleic acids from nucleotides, and polysaccharides from simple sugars.
 These biosynthetic reactions generate the materials for cell growth.

Role of ATP
7
Role of ATP
 Catabolic reactions provide building blocks for anabolic

reactions and furnish the energy needed to drive anabolic
reactions.
 This coupling of energy-requiring and energy-releasing

reactions is made possible through the molecule adenosine
triphosphate(ATP).
 ATP stores energy derived from catabolic reactions and

releases it later to drive anabolic reactions and perform
other cellular work.
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9
Enzymes
 A cell 's metabolic pathways (sequences of chemical reactions) are
determined by its enzymes, which are in turn determined by the cell's genetic
makeup.
 Collision Theory: The collision theory explains how chemical reactions

occur and how certain factors affect the rates of those reactions. The basis of
the collision theory is that all atoms, ions, and molecules are continuously
moving and are thus continuously colliding with one another. The energy
transferred by the particles in the collision can disrupt their electron
structures enough to break chemical bonds or form new bonds.
 The collision energy required for a chemical reaction is its activation energy,
which is the amount of energy needed to disrupt the stable electronic
configuration of any specific molecule so that the electrons can be
rearranged.
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 The reaction rate-the frequency of collisions containing sufficient energy to bring
about a reaction- depends on the number of reactant molecules at or above the
activation energy level.
 Substances that can speed up a chemical reaction without being permanently altered
themselves are called catalysts, In living cells, enzymes serve as biological catalysts.
As catalysts, enzymes are specific. 11
 Each acts on a specific substance, called the enzyme's substrate (or substrates, when
there are two or more reactants),and each catalyzes only one reaction.
 For example, sucrose is the substrate of the enzyme sucrase, which catalyzes the
hydrolysis of sucrose to glucose and fructose.
 The enzyme-substrate complex formed by the temporary binding of enzyme and

reactants enables the collisions to be more effective and lowers the activation energy
of the reaction.
 An enzyme's ability to accelerate a reaction without the need for an increase in

temperature is crucial to living systems because a significant temperature increase
would destroy cellular proteins.
 The crucial function of enzymes, therefore, is to speed up biochemical reactions at a

temperature that is compatible with the normal functioning of the cell.
Enzyme Components 12
 Although some enzymes consist entirely of proteins, most consist of both a protein portion,
called an apoenzyme. and a nonprotein component, called a cofactor. Ions of iron, zinc,
magnesium, or calcium are examples of cofactors.
 If the cofactor is an organic molecule, it is called a coenzyme.
 Apoenzymes are inactive by themselves; they must be activated by cofactors.
 Together, the apoenzyme and cofactor form holoenzyme, or whole, active enzyme. If the
cofactor is removed, the apoenzyme will not function.
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Naming Enzymes
 The names of enzymes usually end in -ase.
 All enzymes can be grouped into six classes, according to the type of chemical reaction they
catalyze .
 Enzymes within each of the major classes are named according to the more specific types of
reactions they assist. For example, the class called oxidoreductase is involved with oxidation-
reduction reactions.
 Enzymes in the oxidoreductase class that remove hydrogen from a substrate are called
dehydrogenases; those that add molecular oxygen (O2) are called oxidases.
 Dehydrogenase and oxidase enzymes have even more specific names, such as lactate
dehydrogenase and cytochrome oxidase, depending on the specific substrates on which they act.
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The Mechanism of Enzymatic Action 15
 Enzymes lower the activation energy of chemical reactions.
 The general sequence of events in enzyme action is as follows
1. The surface of the substrate contacts a specific region of the surface of the enzyme molecule, called
the active site.
2. A temporary intermediate compound forms, called an enzyme-substrate complex.
3. The substrate molecule is transformed by the rearrangement of existing atoms, the breakdown of
the substrate molecule, or in combination with another substrate molecule.
4. The transformed substrate molecules- the products of the reaction- are released from the enzyme
molecule because they no longer fit in the active site of the enzyme.
5. The unchanged enzyme is now free to react with other substrate molecules.
 Enzymes have specificity for particular substrates. For example, a specific enzyme may be able
to hydrolyze a peptide bond only between two specific amino acids
16
Factors Influencing Enzymatic Activity 17
---
Dr. Imran Hashmi
THANKS !
Tenured Professor & Associate Dean
Institute of Environmental Sciences and Engineering
(IESE)
School of Civil and Environmental Engineering (SCEE)
National University of Sciences and Technology (NUST)
Sector H-12, Islamabad-44000, Pakistan.
E-mail: [email protected] ;
[email protected]
Phone: + 92 -51-90854200
18

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1

 Through their metabolism, bacteria recycle elements after other

 Still other bacteria can live on diets of such inorganic substances as

 The sum of all chemical reactions within a living organism.

 Chemical reactions either release or require energy,

 Accordingly, metabolism can be divided into two classes of chemical

 In living cells, the enzyme-regulated chemical reactions that release

 These reactions are called catabolic, or degradative, reactions.

 Catabolic reactions are generally hydrolytic reactions (reactions

 An example of catabolism occurs when cells break down sugars into

 These reactions are called anabolic, or biosynthetic, reactions.

 Anabolic processes often involve dehydration synthesis reactions (reactions that

 These biosynthetic reactions generate the materials for cell growth.

 Catabolic reactions provide building blocks for anabolic

 This coupling of energy-requiring and energy-releasing

 ATP stores energy derived from catabolic reactions and

 Collision Theory: The collision theory explains how chemical reactions

 The enzyme-substrate complex formed by the temporary binding of enzyme and

 An enzyme's ability to accelerate a reaction without the need for an increase in

 The crucial function of enzymes, therefore, is to speed up biochemical reactions at a

 If the cofactor is an organic molecule, it is called a coenzyme.

 Apoenzymes are inactive by themselves; they must be activated by cofactors.

 The general sequence of events in enzyme action is as follows

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