ch 8 an introduction to metabolism n.
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Ch. 8 An Introduction to Metabolism. A organism’s metabolism is subject to thermodynamic laws. The totality of an organism’s chemical reactions is called metabolism .

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a organism s metabolism is subject to thermodynamic laws
A organism’s metabolism is subject to thermodynamic laws
  • The totality of an organism’s chemical reactions is called metabolism.
  • We can picture a cell’s metabolism as an elaborate road map of the thousands of chemical reactions that occur in a cell, arranged as intersecting metabolic pathways
metabolic pathways
Metabolic pathways
  • A metabolic pathway begins with a specific molecule, which is then altered in a series of defined steps, resulting in a certain product.
  • Each step of a pathway is catalyzed by a specific enzyme
metabolic pathways2
Metabolic pathways
  • Enzymes catalyze reactions in intersecting metabolic pathways, which may be catabolic (breaking down molecules, releasing energy) or anabolic (building molecules, consuming energy).
bioenergetics
Bioenergetics
  • Energy is the capacity to cause change; some forms of energy do work by moving matter.
  • Kinetic energy is associated with motion and includes thermal energy (heat) associated with random motions of atoms or molecules.
  • Potential energy is related to the location or structure of matter and includes chemical energy possessed by a molecule due to its structure
thermodynamics
Thermodynamics
  • The first law of thermodynamics, conservation of energy, states that energy cannot be created or destroyed, only transferred or transformed
  • The second law of thermodynamics states that spontaneous processes, those requiring no outside input of energy, increase the entropy (disorder) of the universe
free energy
Free energy
  • A living system’s free energy is energy that can do work under cellular conditions.
  • The change in free energy (∆G) during a biological process is related directly to enthalpy change (∆H) and to the change in entropy (∆S): ∆G=∆H - T∆S.
  • Organisms live at the expense of free energy
free energy1
Free energy
  • During a spontaneous change, free energy decreases and that stability of a system increases.
  • At maximum stability, the system is at equilibrium and can do no work.
spontaneous reaction
Spontaneous reaction
  • In an exergonic (spontaneous) chemical reaction, the products have less free energy than the reactants (-∆G)
endergonic reactions
Endergonic reactions
  • Endergonic (nonspontaneous) reactions require an input of energy (+∆G).
  • The addition of starting materials and the removal of end products prevent metabolism from reaching equilibrium
coupling and atp
Coupling and ATP
  • ATP is the cell’s energy shuttle. Hydrolysis of its terminal phosphate yields ADP and Pᵢ and releases free energy.
coupling and atp2
Coupling and ATP
  • Through energy coupling, the exergonic process of ATP hydrolysis drives endergonic reactions by transfer of a phosphate group to specific reactants, forming a phosphorylated intermediate that is more reactive
coupling and atp4
Coupling and ATP
  • ATP hydrolysis (sometimes with protein phosphorylation) also causes changes in the shape and binding affinities of transport and motor proteins
coupling and atp6
Coupling and ATP
  • Catabolic pathways drive regeneration of ATP from ADP and Pᵢ.
enzymes speed up metabolic reactions
Enzymes speed up metabolic reactions
  • In a chemical reaction, the energy necessary to break the bonds of the reactants is the activation energy, Eᴀ.
  • Enzymes lower the Eᴀ barrier
enzyme action
Enzyme action
  • Each type of enzyme has a unique active site that combines specifically with its substrate(s), the reactant molecule(s) on which it acts.
  • The enzyme changes shape slightly when it binds the substrate(s) (induced fit).
enzyme action2
Enzyme action
  • The active site can lower the Eᴀ barrier by orienting substrates correctly, straining their bonds, providing a favorable microenvironment, or even covalently bonding with the substrate
  • Each enzyme has optimal temperature and pH. Inhibitors reduce enzyme function. A competitive inhibitor binds to the acive site, whereas a noncompetitive inhibitor binds to a different site on the enzyme
enzyme action3
Enzyme action
  • Natural selection, acting on organisms with mutant genes encoding altered enzymes, is a major evolutionary force responsible for the diverse array of enzymes found in organisms
enzyme regulation
Enzyme regulation
  • Many enzymes are subject to allosteric regulation: regulatory molecules, either activators or inhibitors, bind to specific regulatory sites, affecting the shape and function of the enzyme
allosteric regulation1
Allosteric regulation
  • In cooperativity, binding of one substrate molecule can stimulate binding or activity at other active sites.
  • In feedback inhibition, the end product of a metabolic pathway allosterically inhibits the enzyme for a previous step in the pathway
enzyme regulation1
Enzyme regulation
  • Some enzymes are grouped into complexes, some are incorporated into membranes, and some are contained inside organelles, increasing efficiency of metabolic processes