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Metabolism
• Chemical reactions of life
– forming bonds between molecules
•
•
– breaking bonds between molecules
•
•
•
Metabolic pathways
A→ B→ C→ D→ E→ F→ G
→
→
→
enzyme enzyme enzyme enzyme enzyme enzyme
2 3 4 5 6
1
• Series of enzyme-catalyzed
steps from starting molecule to
product
– Anabolic pathways
•
– Catabolic pathways
•
Forms of Energy
• Potential
– Gravity
– Chemical
(bonds)
• Kinetic
– Heat
– Light
1st and 2nd Law of Thermodynamics
• Conservation of Energy
• Every energy transfer increases entropy
(disorder) of the universe – Some energy is
unusable
– Transfers that increase entropy occur
spontaneously
Free Energy Change (ΔG)
Free energy – amount of energy a system has that is available to do work
Chemical Reactions and Energy
• Exergonic reactions
release energy
– digesting polymers
– hydrolysis =
catabolism
• Endergonic reactions
need input of energy
– building polymers
– dehydration synthesis
= anabolism
Organisms are Open
Systems
What drives reactions?
• If reactions are “downhill”, why don’t they just
happen spontaneously?
–
starc
h
Activation energy
• Even exergonic reactions require an initial input of energy
– activation energy
– large biomolecules
are stable
– must absorb energy
to break bonds
Enzymes Lower Activation Energy.
Catalyst: ___________________________________
Enzymes
• Biological catalysts
–
–
• increase rate of reaction without being consumed
• reduce activation energy
• don’t change free energy (∆ G) released or required
– required for most biological reactions
–
• thousands of different enzymes in cells
– control reactions
of life
Enzyme vocabulary
substrate
• reactant which binds to enzyme
• enzyme-substrate complex: temporary association
active site
• enzyme’s catalytic site; substrate fits into active site
product
• end result of reaction
Naming conventions
• Enzyme concentration
• Substrate
concentration
• Temperature
• pH
• Salinity
• Activators
• Inhibitors
Factors affecting enzyme function
• Substrate concentration
– more substrate = more frequently collide with
enzyme = ↑ reaction rate
– reaction rate levels off
• all enzymes have active site engaged
• enzyme is saturated
reaction rate
substrate concentration
Temperature
What’s
happening here?!
reaction rate
37°
temperature
Factors affecting enzyme function
• Temperature
– Optimum T°
• greatest number of _______________
• human enzymes = 35°- 40°C
– body temp = 37°C _____________
– Heat: increase beyond optimum T°
• increased energy of molecules disrupts bonds in enzyme &
between enzyme & substrate
– H, ionic = weak bonds
• denaturation = ___________________________
Compounds that help enzymes
• Activators Fe in
– cofactors hemoglobi
• non-protein, small _______________compounds n
&
ions
– Mg, K, Ca, Zn, Fe, Cu (trace elements, minerals
in nutrition)
– bound to enzyme. Required for proper function
– coenzymes
• non-protein, _________________cofactors
– bind near active site
– Participate in reaction
• many _________________
– NAD (niacin; B3) Mg in
– FAD (riboflavin; B2) chlorophyl
– Coenzyme A l
– Also ATP
Regulation of
Enzyme Activity
• Enzyme Inhibitors
– molecules that reduce
enzyme activity
– competitive inhibition
– noncompetitive
inhibition
– irreversible inhibition
– feedback inhibition
Regulation of Enzyme Activity -
Competitive Inhibitors
• Inhibitor & substrate “compete” for active site
– __________________blocks enzyme bacteria use
to build cell walls
– disulfiram (___________)
treats chronic alcoholism
• blocks enzyme that
breaks down alcohol
• severe hangover & vomiting
5-10 minutes after drinking
• Overcome by increasing substrate
concentration
Regulation of Enzyme Activity -
Non-Competitive Inhibitors
• Inhibitor binds to site other than active site
– __________________ binds to allosteric site
– causes _______________________ in enzyme
• keeps enzyme inactive
– some __________________ drugs
inhibit enzymes involved in DNA synthesis
• stop division of more cancer cells
– ______________________________
irreversible inhibitor of Cytochrome C,
an enzyme in cellular respiration
• stops production of ATP
Regulation of
Enzyme Activity -
Control of Metabolism
____________________
• Conformational changes by
regulatory molecules
– inhibitors
• keeps enzyme in inactive
form
– activators
• keeps enzyme in active
form
Regulation of Enzyme Activity -
Control of Metabolism
Allosteric Regulation – Cooperativity
• Substrate acts as an activator
– substrate causes conformational
change in enzyme
• _________________________
– favors binding of substrate at 2nd site
– makes enzyme more effective
Hemoglobin
4 polypeptide chains
can bind 4 O2;
1st O2 binds
now easier for other
3 O2 to bind
Feedback Inhibition
• Regulation & coordination of production
– product is used by next step in pathway
– final product is inhibitor of earlier step
• allosteric inhibitor of _____________________
– no unnecessary accumulation of product
A →B →C →D →E →F →G
→
→
→
X enzyme
enzyme
2
enzyme enzyme enzyme enzyme
4 5 6
1 3
• Example
– synthesis of amino acid,
isoleucine from threonine
– isoleucine becomes the
allosteric inhibitor of the
first step in the pathway
•
isoleucine
ATP – Cellular Energy
• Organisms/cells are
endergonic systems
• must have energy for
– Mechanical work
– Transport work Ribose, Adenine, 3 phosphates
– Chemical work
ATP – Cellular Energy
• Adenosine tri
phosphate - - -
– 3 phosphate groups
covalently bonded
– Can be removed by
hydrolysis
– High energy bonds
• Negative phosphates
repel one another,
easy to remove
•
digestio
n
+ + energy
synthesi
s
+ + energy
ATP – Energy Coupling
How does ATP transfer energy?
O– O– O– O– 7.3
–
O P –O– P –O– P O– –
O P O– + energy
ATP
ADP O O O O
• ATP → ADP
– releases energy
• ∆G = -7.3 kcal/mole
• Fuel other reactions
• ____________________
– released Pi can transfer to other molecules
• destabilizing the other molecules
– enzyme that phosphorylates = “kinase”
An example of Phosphorylation…
• Building polymers from monomers
H H
– need to destabilize the monomers C C
OHHO
– phosphorylate! enzyme
H H synthesi
H H
s
C + C
+4.2 kcal/mol
C C + H2O
OH HO O
H “kinase” H
+ ADP
enzyme
C
OH
+ ATP -7.3 kcal/mol
C
P
H H H H
C
+ C C C + Pi
P HO -3.1 kcal/mol O
ATP – Drives Cellular Work
• Phosphorylation
– makes
molecule less
stable, more
likely to react
– Conformation
al change
ATP / ADP cycle
Cells can’t store ATP ATP
good energy donor, cellular 7.3
not good energy storage respiration kcal/mole
______________________
______________________
carbohydrates & fats are ADP + Pi
long term energy storage
A working muscle recycles over
10 million ATPs per second