Microbial Metabolism Lecture Part A

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Microbial Metabolism

Microbial Metabolism
 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.

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Metabolism
 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
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Catabolism
 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.
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Anabolism
 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.

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Role of ATP

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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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.

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 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.

 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.
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Enzyme Components
 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.

 As you will see later, 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
 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
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Factors Influencing Enzymatic Activity

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