 MICROBIAL METABOLISM

 METABOLISM
 sum of all chemical reactions within a living organism.
 Chemical reactions either release or require energy
 Can be viewed as an energy-balancing act.
 Metabolism is divided into 2 classes of chemical reactions- release energy and those that
require energy.
 CATABOLISM
 Enzyme-regulated chemical reactions that release energy
 Breakdown of complex organic compounds into simpler ones- Degradative reactions
 Hydrolytic reactions- reactions which use water and in which chemical bonds are broken
 Exergonic- produce more energy than consumed
 Ex: sugars are broken into carbon dioxide and water
 ANABOLISM
 energy-requiring reactions
 building of complex organic molecules from simpler ones- Biosynthetic reactions
 Dehydration synthesis reactions- reactions that release water
 Endergonic- consume more energy than they produce
 Ex: Production of proteins from amino acids, polysaccharides from simple sugars

 Catabolic reactions provide building blocks for anabolic reactions

 Coupling of energy-requiring and energy-releasing reactions is made possible through ATP
 ATP
 Consists of an adenine, a ribose, and three phosphate groups.
 Stores energy from catabolic reactions and releases it later for anabolic reactions and perform
other cellular work
 Anabolic reactions are coupled to ATP breakdown
 Terminal phosphate group is split from ATP, adenosine diphosphate
(ADP) is formed, and energy is released to drive anabolic reactions
 Catabolic reactions are coupled to ATP synthesis
 Energy from catabolic reactions is used to combine ADP and a phosphate
to resynthesize ATP

 ENZYMES AND CHEMICAL REACTIONS

 Catalysts- substances that speed up reactions without being permanently changed
 Acts on a specific substance (substrate)
 Ex: sucrose (table sugar) is the substrate of the enzyme sucrase, which catalyzes the
hydrolysis of sucrose to glucose and fructose
 Active site- region which interacts with the specific substrate
 ENZYMES AND CHEMICAL REACTIONS
 Enzyme-substrate complex- formed by the temporary binding of enzyme and reactants
 Accelerates reaction without significantly increasing temperature
 Speed up biochemical reactions at a temperature compatible with the normal functioning of
the cell.
 ENZYME COMPONENTS
 Consists entirely of proteins
 Most have a protein component (apoenzyme) and non protein portion (cofactor)
 Cofactor- iron, zinc, magnesium, or calcium
 Coenzyme- cofactor that is an organic molecule
 Apoenzymes must be activated by cofactors (Holoenzyme)

 SOME IMPORTANT COENZYMES

 nicotinamide adenine dinucleotide (NAD+) - catabolic
 nicotinamide adenine dinucleotide phosphate (NADP+) – anabolic
 flavin mononucleotide (FMN)
 flavin adenine dinucleotide (FAD)
 coenzyme A (CoA) – Krebs cycle
 MECHANISM OF ENZYMATIC ACTION
 1. Substrate contacts the active site of enzyme
 2. formation of enzyme-substrate complex
 3. Transformation of substrate (rearrangement of existing atoms, the breakdown of the
substrate molecule, or in combination with another substrate molecule.)
 4. Transformed substrate are released from the enzyme- they no longer fit within the active
site.
 5. Enzyme is now free to react with other molecules

 FACTORS INFLUENCING ENZYMATIC ACTIVITY

 Temperature
 elevation beyond a certain temperature, drastically reduces the rate of reaction
 optimal temperature for most disease-producing bacteria in the human body is between 35°C
and 40°C.
 Beyond the optimal temperature, enzyme undergoes denaturation
 Denaturation alters the active site of enzymes
 FACTORS INFLUENCING ENZYMATIC ACTIVITY
 pH
 Most enzymes have an optimum pH at which their activity is maximal
 Beyond this pH, reaction rate decreases
 Extreme changes in pH can cause denaturation
 Acids and bases alter a protein’s three-dimensional structure

 FACTORS INFLUENCING ENZYMATIC ACTIVITY

 Substrate Concentration
 Saturation- enzyme is said to be in this condition if there is a high substrate concentration
 Active site is always occupied by substrate or product molecules
 Further increase in substrate concentration will not affect the reaction rate because all active
sites are already in use
 FACTORS INFLUENCING ENZYMATIC ACTIVITY
 Inhibitors
 classified as either competitive or noncompetitive inhibitors
 Competitive inhibitors- compete with the normal substrate for the active site.
 Competitive inhibitor- has the same structure and chemical composition as the substrate.
 Reversible/ irreversible
 Ex: sulfanilamide competes with para-amino benzoic acid (essential nutrient of bacteria for
the synthesis of folic acid)
 FACTORS INFLUENCING ENZYMATIC ACTIVITY
 Inhibitors
 Non-competitive inhibitors- do not compete with the normal substrate for the active site.
Bind with the allosteric site, changing the configuration of active site making it nonfunctional
 either reversible or irreversible, depending on whether the active site can return to its original
shape