Chapter 8- An Introduction to Metabolism
metabolism- includes all the chemical reactions in an organism
these chemical reactions are ordered into metabolic pathways
sequence of steps, each controlled by an enzyme
products of one step become the reactants of the next step
enzymes help regulate the rate (or speed) of metabolic pathways
two types of metabolic pathways
catabolic
breakdown pathways
complex molecule to simpler compound
spontaneous
exergonic
release energy (kinetic)
downhill reactions
examples:
cellular respiration and hydrolysis of starch into glucose
anabolic
synthesis pathways
simple compound to complex molecule
non-spontaneous
endergonic
consume (absorb) energy (potential)
uphill reaction
examples
photosynthesis and synthesis of protein from amino acids
the energy released from catabolic pathways drives the anabolic pathways in a cell
laws of thermodynamics (energy transformations)
an organisms metabolism transforms matter and energy
subject to the laws of thermodynamics
in an open system, energy and matter may be exchanged between the system and its surroundings (organism and environment)
1st law of thermodynamics
principle of conservation of energy
energy can be neither created or destroyed
total energy of the universe is constant
2nd law of thermodynamics
entropy (disorder)
every energy transformation or transfer results in increasing entropy (disorder)
as energy is transferred or transformed more energy is wasted (unavailable for work)
some energy converted to heat in all chemical reactions
free energy and metabolism
free energy (G)- the portion of a systems energy available to perform work when the systems temperature and pressure are uniform
free energy equation- see in powerpoint notes
exergonic reactions (energy outward)
spontaneous reaction in which there is a net release of free energy
see powerpoint/BILL for graphic
endergonic reactions (energy inward)
non spontaneous reactions in which free energy is absorbed from the surroundings
see powerpoint/BILL for graphic
equilibrium and metabolism
reactions in an isolated system will naturally move toward equilibrium
not the same as homeostasis
cells are never at equilibrium because of the constant flow of materials in and out of the cell
steady supply of reactants
constant flow of energy
living organisms do not work in isolation
living organisms are open systems
a cell at equilibrium is a dead cell
hydrolysis of ATP to ADP
ATP is the energy source used to drive most types of cellular work
chemical, transport, and mechanical
the bond between the final two phosphate groups is broken by hydrolysis
the breaking of the final phosphate bond produces ADP, inorganic phosphate, and energy
because hydrolysis of ATP to ADP releases energy considered exergonic
regeneration of ATP from ADP and Pi
cells regenerates ATP very quickly through the process of cellular respiration
human muscle cell @ 10 million molecules per second per cell
enzymes that are biological catalysts
catalyst- a substance that can change the rate of a reaction without being altered in the process
enzyme- a protein catalyst that changes the rate of a reactions without being consumed
speeds up rate of metabolic reactions but are unchanged by the actions
activation energy
in chemical reactions- bonds are broken and bonds are formed
AB+CD to AC+BD
reactants must absorb energy from their surroundings for their bonds to break and energy is released when new bonds are formed to make products
activation energy (EA)- energy needed initially to reach transition state, in which bonds can be broken and from which the reaction can proceed
activation energy is often supplied in the form of heat (in chemistry)
(in biology) high temps denature proteins and kill cells
heat would speed up all reactions not just those that are needed
instead of heat organisms use enzymes to catalyze metabolic reactions
how do enzymes speed up a reactions?
enzymes lower the activation energy
allow reaction to begin sooner
allow reaction to proceed more quickly
enzymes do not change the G for a reactions
enzymes only change the rate at which a reaction occurs
enzymes are not consumed in a reactions (enzymes are reused)
enzyme structure and specificity
protein enzymes are macromolecules with characteristic three dimensional shapes
result in their being very specific- each enzymes works on one specific reaction
substrate- the reactant that an enzyme acts on
active site- region on an enzyme where the substrate binds
pocket or groove found on surface of enzyme that has a shape compatible to that of the substrate
forms enzyme-substrate complex
the enzyme works by binding itself to the substrate
biochemists have discovered and named more than 4000 different enzymes in various species
enzyme reaction rates
one enzyme can act on 1000 substrate molecules per second
rate at which an enzyme works depends on initial concentration of substrate
the more substrate molecules there are, the more frequently they will bind to the active site of available enzyme (higher rate of reaction)
when the concentration of substrate is high enough that all of the enzymes active sites are engaged the enzyme is said to be saturated
when enzymes are saturated the only way to increase the reaction rate would be to add more enzyme
effects of local conditions on enzyme activity
temperature- each enzyme has an optimal termperature at which its reaction rate is the fastest
what happens to the enzyme as the temperature moves beyond the optimal temperature?
the heat breaks bonds in the enzyme, denaturing it and causing it to be inactive
pH- enzymes have a specific pH in which they are most active
the optimal pH for most enzymes is between 6 and 8
what happens to the enzyme when the pH drops below or goes above the optimal pH?
the enzyme is denatured
cofactors and coenzymes
many enzymes are not able to work unless they have the help of another molecule
cofactors- any non-protein molecule that is required for the proper functioning of an enzyme
example: minerals such as iron or zinc
if a cofactor is an organic molecule, it is more specifically called a coenzyme
example: vitamins
regulation of enzyme activity
the cells metabolic pathways cannot all operate simultaneously (overload)
to regulate metabolic pathways the cell
switches on and off the genes that encode the specific enzymes (genetics) or
regulates the activity of enzymes once they are made
enzyme inhibitors
competitive inhibitors- molecules that resemble the normal substrate and compete to bind to the active site
resembles/mimics normal substrate
competitive inhibitors bind directly to the active site
overcome by increasing concentration of substrate
noncompetitive inhibitors- inhibitors that bind to the other part of the enzyme causing it to change shape so the substrate can’t bind the the active site
active site becomes non-functional
also called allosteric inhibitors
inhibitor binds to allosteric site
feedback inhibition
another way in which metabolic pathways are regulated
end product shuts down pathways by binding to allosteric site
prevents wasting of chemical resources
increases efficiency of cell
ATP can act as a feedback inhibitor
metabolism- includes all the chemical reactions in an organism
these chemical reactions are ordered into metabolic pathways
sequence of steps, each controlled by an enzyme
products of one step become the reactants of the next step
enzymes help regulate the rate (or speed) of metabolic pathways
two types of metabolic pathways
catabolic
breakdown pathways
complex molecule to simpler compound
spontaneous
exergonic
release energy (kinetic)
downhill reactions
examples:
cellular respiration and hydrolysis of starch into glucose
anabolic
synthesis pathways
simple compound to complex molecule
non-spontaneous
endergonic
consume (absorb) energy (potential)
uphill reaction
examples
photosynthesis and synthesis of protein from amino acids
the energy released from catabolic pathways drives the anabolic pathways in a cell
laws of thermodynamics (energy transformations)
an organisms metabolism transforms matter and energy
subject to the laws of thermodynamics
in an open system, energy and matter may be exchanged between the system and its surroundings (organism and environment)
1st law of thermodynamics
principle of conservation of energy
energy can be neither created or destroyed
total energy of the universe is constant
2nd law of thermodynamics
entropy (disorder)
every energy transformation or transfer results in increasing entropy (disorder)
as energy is transferred or transformed more energy is wasted (unavailable for work)
some energy converted to heat in all chemical reactions
free energy and metabolism
free energy (G)- the portion of a systems energy available to perform work when the systems temperature and pressure are uniform
free energy equation- see in powerpoint notes
exergonic reactions (energy outward)
spontaneous reaction in which there is a net release of free energy
see powerpoint/BILL for graphic
endergonic reactions (energy inward)
non spontaneous reactions in which free energy is absorbed from the surroundings
see powerpoint/BILL for graphic
equilibrium and metabolism
reactions in an isolated system will naturally move toward equilibrium
not the same as homeostasis
cells are never at equilibrium because of the constant flow of materials in and out of the cell
steady supply of reactants
constant flow of energy
living organisms do not work in isolation
living organisms are open systems
a cell at equilibrium is a dead cell
hydrolysis of ATP to ADP
ATP is the energy source used to drive most types of cellular work
chemical, transport, and mechanical
the bond between the final two phosphate groups is broken by hydrolysis
the breaking of the final phosphate bond produces ADP, inorganic phosphate, and energy
because hydrolysis of ATP to ADP releases energy considered exergonic
regeneration of ATP from ADP and Pi
cells regenerates ATP very quickly through the process of cellular respiration
human muscle cell @ 10 million molecules per second per cell
enzymes that are biological catalysts
catalyst- a substance that can change the rate of a reaction without being altered in the process
enzyme- a protein catalyst that changes the rate of a reactions without being consumed
speeds up rate of metabolic reactions but are unchanged by the actions
activation energy
in chemical reactions- bonds are broken and bonds are formed
AB+CD to AC+BD
reactants must absorb energy from their surroundings for their bonds to break and energy is released when new bonds are formed to make products
activation energy (EA)- energy needed initially to reach transition state, in which bonds can be broken and from which the reaction can proceed
activation energy is often supplied in the form of heat (in chemistry)
(in biology) high temps denature proteins and kill cells
heat would speed up all reactions not just those that are needed
instead of heat organisms use enzymes to catalyze metabolic reactions
how do enzymes speed up a reactions?
enzymes lower the activation energy
allow reaction to begin sooner
allow reaction to proceed more quickly
enzymes do not change the G for a reactions
enzymes only change the rate at which a reaction occurs
enzymes are not consumed in a reactions (enzymes are reused)
enzyme structure and specificity
protein enzymes are macromolecules with characteristic three dimensional shapes
result in their being very specific- each enzymes works on one specific reaction
substrate- the reactant that an enzyme acts on
active site- region on an enzyme where the substrate binds
pocket or groove found on surface of enzyme that has a shape compatible to that of the substrate
forms enzyme-substrate complex
the enzyme works by binding itself to the substrate
biochemists have discovered and named more than 4000 different enzymes in various species
enzyme reaction rates
one enzyme can act on 1000 substrate molecules per second
rate at which an enzyme works depends on initial concentration of substrate
the more substrate molecules there are, the more frequently they will bind to the active site of available enzyme (higher rate of reaction)
when the concentration of substrate is high enough that all of the enzymes active sites are engaged the enzyme is said to be saturated
when enzymes are saturated the only way to increase the reaction rate would be to add more enzyme
effects of local conditions on enzyme activity
temperature- each enzyme has an optimal termperature at which its reaction rate is the fastest
what happens to the enzyme as the temperature moves beyond the optimal temperature?
the heat breaks bonds in the enzyme, denaturing it and causing it to be inactive
pH- enzymes have a specific pH in which they are most active
the optimal pH for most enzymes is between 6 and 8
what happens to the enzyme when the pH drops below or goes above the optimal pH?
the enzyme is denatured
cofactors and coenzymes
many enzymes are not able to work unless they have the help of another molecule
cofactors- any non-protein molecule that is required for the proper functioning of an enzyme
example: minerals such as iron or zinc
if a cofactor is an organic molecule, it is more specifically called a coenzyme
example: vitamins
regulation of enzyme activity
the cells metabolic pathways cannot all operate simultaneously (overload)
to regulate metabolic pathways the cell
switches on and off the genes that encode the specific enzymes (genetics) or
regulates the activity of enzymes once they are made
enzyme inhibitors
competitive inhibitors- molecules that resemble the normal substrate and compete to bind to the active site
resembles/mimics normal substrate
competitive inhibitors bind directly to the active site
overcome by increasing concentration of substrate
noncompetitive inhibitors- inhibitors that bind to the other part of the enzyme causing it to change shape so the substrate can’t bind the the active site
active site becomes non-functional
also called allosteric inhibitors
inhibitor binds to allosteric site
feedback inhibition
another way in which metabolic pathways are regulated
end product shuts down pathways by binding to allosteric site
prevents wasting of chemical resources
increases efficiency of cell
ATP can act as a feedback inhibitor