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Chapter 5.

Microbial
Metabolism
Catabolism and anabolism

• Catabolism: breakdown of complex organic compounds (e.g., carbohydrates,


proteins, fats, and nucleic acids) into simpler ones; energy-releasing
• Anabolism: building of complex organic compounds from simpler ones; energy-
requiring. Examples: biosynthesis of carbohydrates (e.g., peptidoglycan in the cell
wall) from simple sugars, proteins (e.g., enzymes) from amino acids, lipids (e.g.,
lipid bilayer of the cell membrane) from fatty acids and glycerol, and DNA from
nucleotides.
• Uses of cellular energy: ATP (adenosine triphosphate) stores energy in a "high-
energy" bond & plays the role of linking the anabolic and catabolic reactions.
Examples of energy use include biosynthesis (anabolism), active membrane
transport, cell motility, and bioluminescence.

Metabolic diversity of microorganisms

Source of Carbon
Source of Inorganic compounds (CO2) Organic compounds
Energy
Light photoautotrophs photoheterotrophs

• Organisms: Plants, algae, • Organisms: Non-


cyanobacteria, green/purple sulfur sulfur green and
bacteria purple bacteria
• Green/purple sulfur bacteria: Split H2S
instead of water during photosynthesis,
no oxygen release, strictly anaerobes,
evolved first

• Cyanobacteria: Split water during


photosynthesis; release oxygen;
evolved later and responsible for the
oxygenization of Earth atmosphere
Chemicals chemoautotrophs chemoheterotrophs

• Uses inorganic chemical as energy • Organic compounds as


source energy source and
• Also called chemolithotrophs carbon source
• Example: Nitrifying bacteria uses • Organisms: most
ammonia to produce nitrates, thus bacteria, fungi, animal
recycles nitrogen source in soil

Enzymes

• Enzymes are biological catalysts made of protein; having high substrate


specificity and high efficiency
• Naming: most end with "-ase" (e.g., lipase, sucrase, DNA polymerase used in
PCR)
• Components: Some consist of protein (apoenzyme) and non-protein parts.
Inorganic factors (e.g., zinc) are called cofactors; and organic cofactors are called
coenzymes (many vitamins are coenzymes)
• Factors influencing enzyme activity: temperature, pH, substrate concentration,
inhibitors
o Competitive inhibitors: competitive binding of active sites with substrates;
effect reversible; sulfa drugs are competitive inhibitor of PABA, the
substrate for folic acid (essential for bacteria growth) synthesis, thus stops
bacteria growth
o Non-competitive inhibitors: binding to non-active sites; effect non-
reversible; example is the denaturation of enzymes by heavy metals.
• Protein denaturation: Active proteins form specific 3-D shapes to perform its
function. Breakage of the non-covalent bonds that hold the active protein shapes
renders protein inactive. The loss of protein 3-D structure and function due to
heat or chemical treatment is called denaturation.

Overview of carbohydrate catabolism

• Glycolysis: Oxidation of glucose to pyruvic acid; occurs in both aerobes and


anaerobes; uses NAD and produces 2 ATPs; some bacteria process glucose
differently (e.g. into pentose).
• Anaerobic metabolism (Fermentation): Conversion of pyruvic acid into alcohol,
lactic acid, and other organic compounds; produces NAD for re-use in glycolysis,
no net gain of ATP except for 2 ATPs produced during glycolysis; important for
food production, industrial production of organic compounds, and diagnostic tests
of pathogenic bacteria
• Aerobic respiration: Complete breakdown of pyruvic acid into CO2 and water.
Oxygen as the final electron acceptor. Uses Krebs (TCA) Cycle. Occurs in
cytoplasm (bacteria) or mitochondria of the eukaryotes. Produces 38 ATPs
through electron transport chain (a cascade of redox reactions that generate most
of ATP) and chemiosmosis (ATP synthase driven by proton gradient)

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