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Transcript
Metabolism & Enzymes
AP Biology
2007-2008
From food webs to the life of a cell
energy
energy
energy
AP Biology
Flow of energy through life
 Life is built on chemical reactions


Transforming energy from one form to another
Most reactions are spontaneous
organic molecules  ATP
& organic molecules
sun
solar energy 
AP
Biology
ATP
& organic molecules
organic molecules 
ATP & organic molecules
Metabolism
 All the chemical reactions that take
place in a cell
 Enzymes regulate metabolic pathways
 Metabolic Pathway
Set of enzyme-catalyzed reactions that relate
reactants and products (biochemical
pathways)
 Substrate product = substrate  final
pathway’s product
 Final product can fit in to Enzyme 1 – stop
reaction
 What is this called?
AP Biology

Metabolism
 Chemical reactions of life

forming bonds between molecules
 dehydration synthesis
 synthesis
 anabolic - consumption of energy to build
complex molecules from small molecules
 Glucose  starch
CO2 + H2OC6H12O6 + O2
Photosynthesis
AP Biology
That’s why
they’re called
anabolic steroids!
Metabolism

breaking bonds between molecules
 hydrolysis
 digestion
 catabolic reactions - release energy by
breaking down complex molecules into
simpler molecules.
 Ex. Starch glucose (net loss)
AP Biology
That’s why
they’re called
anabolic steroids!
Examples
 dehydration synthesis (synthesis)
+
enzyme
H2O
 hydrolysis (digestion)
enzyme
H2O
AP Biology
+
Examples
 dehydration synthesis (synthesis)
enzyme
 hydrolysis (digestion)
enzyme
AP Biology
Energy
 The ability to do work
 The 1st law of Thermodynamics
Energy cannot be created or destroyed
 It can only be transformed from one
type into another

 Heat is the ultimate form of energy –
last step of transformation
AP Biology
 The 2nd law of thermodynamics
 Every energy transformation increases


the entropy (disorder of the universe)
K
Free Energy – The amount of energy
available to a system (∆G)
AP Biology
Chemical reactions & energy
 Some chemical reactions net release of
free energy
exergonic
 Energy now available from the breakdown
 digesting polymers
 hydrolysis = catabolism
digesting molecules=
 Spontaneous
LESS organization=

-G

AP Biology
lower energy state
Link for you to study at home
exergonic
-
Spontaneous
w/ enzyme
lowers
activation
energy
-G
AP Biology
G = change in free energy = ability to do work
 Some chemical reactions require
net input of energy
endergonic
 building polymers
 Absorbs free energy from surroundings
 Net gain of energy

building molecules=
MORE organization=
higher energy state
AP Biology
Endergonic vs. exergonic reactions
endergonic
Glucose
A.E. from
light
captured
CO2 +H2O
AP Biology
Net energy
captured by
synthesizing
glucose
- energy invested
- synthesis
+G
Energy & life
 Organisms require energy to live

where does that energy come from?
 coupling exergonic reactions (releasing energy)
with endergonic reactions (needing energy)
+
digestion
synthesis
+
AP Biology
+
energy
+
energy
Starch
Glycogen
Glucose
Exergonic reactions drive Endergonic Reactions
(Catabolic)
(anabolic)
ATP Synthase – hydrogen fed into synthase,
energy, happens in mitochondria, ADP ATP
AP Biology
ATP synthase
(extra for now)
 Enzyme channel in
H+
H+
H+
H+
H+
H+
H+
H+
rotor
mitochondrial membrane


permeable to H+
H+ flow down
concentration gradient
rod
 flow like water over
water wheel
 flowing H+ cause
ADP + P
change in shape of
ATP synthase enzyme
 powers bonding of
ATP
Pi to ADP:
ADP + Pi  ATP
APBut…
Biology How
is the proton (H+) gradient formed?
catalytic
head
H+
What drives reactions?
 If reactions are “downhill”, why don’t they
just happen spontaneously?

because covalent bonds are stable bonds
starch
AP Biology
Why don’t
stable polymers
spontaneously
digest into their
monomers?
Adenine Triphosphate (ATP)
 ATP powers cellular work by coupling
exergonic and endergonic reactions
 ATP  changes the shape of a
molecule causes work then molecule
goes back to original shape
 Phosphorylation – the energy from the
hydrolysis of ATP is directly coupled to
endergonic processes by the transfer of
the phosphate group to another molecule
 The recipient molecule is phosphorylated
AP Biology
ATP / ADP cycle
Can’t store ATP
cellular
 good energy donor,
not good energy storage respiration
 too reactive
 transfers Pi too easily
 only short term energy
storage
 carbohydrates & fats are
long term energy storage
Whoa!
Pass me
the glucose
(and O2)!
AP Biology
ATP
7.3
kcal/mole
ADP + Pi
A working muscle recycles over
10 million ATPs per second
1. Reatants
2. Products
3. Activation Energy
4. Transition State
5. Ea w/ enzyme
6. + or -G
AP Biology
Enzymes
 Biological catalysts


proteins (& RNA)
facilitate chemical reactions
 increase rate of reaction without being consumed
 reduce activation energy
 don’t change free energy (G) released or required


required for most biological reactions
highly specific
 thousands of different enzymes in cells

AP Biology
control reactions
of life
Enzymes vocabulary
substrate
 reactant which binds to enzyme
 enzyme-substrate complex: temporary association
product
 end result of reaction
active site
 enzyme’s catalytic site; substrate fits into active site
active site
substrate
enzyme
AP Biology
products
Lock and Key model
 Simplistic model of
enzyme action

substrate fits into 3-D
structure of enzyme’
active site
 H bonds between
substrate & enzyme

AP Biology
like “key fits into lock”
In biology…
Size
doesn’t matter…
Shape matters!
Induced fit model
 More accurate model of enzyme action
3-D structure of enzyme fits substrate
 substrate binding cause enzyme to
change shape leading to a tighter fit

 “conformational change”
 bring chemical groups in position to catalyze
reaction
AP Biology
Factors that Affect Enzymes
AP Biology
2007-2008
Factors Affecting Enzyme Function
 Enzyme concentration
 Substrate concentration
 Temperature
 pH
 Salinity
 Activators
 Inhibitors
AP Biology
catalase
Mr Z – Draw Picture of Enzyme on
board
AP Biology
Compounds which help enzymes
Fe in
 Activators
hemoglobin

cofactors
 non-protein, small inorganic
compounds & ions
 Mg, K, Ca, Zn, Fe, Cu
 bound within enzyme molecule

coenzymes
 non-protein, organic molecules
 bind temporarily or permanently to
enzyme near active site
AP Biology
 many vitamins
 NAD (niacin; B3)
 FAD (riboflavin; B2)
 Coenzyme A
Mg in
chlorophyll
Compounds which regulate enzymes
 Inhibitors
molecules that reduce enzyme activity
 competitive inhibition
 noncompetitive inhibition
 irreversible inhibition
 feedback inhibition

AP Biology
Competitive Inhibitor
 Inhibitor & substrate “compete” for active site


penicillin
blocks enzyme bacteria use to build cell walls
disulfiram (Antabuse)
treats chronic alcoholism
 blocks enzyme that
breaks down alcohol
 severe hangover & vomiting
5-10 minutes after drinking
 Overcome by increasing substrate
concentration

AP Biology
saturate solution with substrate
so it out-competes inhibitor
for active site on enzyme
Non-Competitive Inhibitor
 Inhibitor binds to site other than active site


allosteric inhibitor binds to allosteric site
causes enzyme to change shape
 conformational change
 active site is no longer functional binding site
 keeps enzyme inactive

some anti-cancer drugs
inhibit enzymes involved in DNA synthesis
 stop DNA production
 stop division of more cancer cells

cyanide poisoning
irreversible inhibitor of Cytochrome C,
an enzyme in cellular respiration
 stops production of ATP
AP Biology
Irreversible inhibition
 Inhibitor permanently binds to enzyme

competitor
 permanently binds to active site

allosteric
 permanently binds to allosteric site
 permanently changes shape of enzyme
 nerve gas, sarin, many insecticides
(malathion, parathion…)
 cholinesterase inhibitors

AP Biology
doesn’t breakdown the neurotransmitter,
acetylcholine
Allosteric regulation
 Conformational changes by regulatory
molecules

inhibitors
 keeps enzyme in inactive form

activators
 keeps enzyme in active form
AP Biology Conformational
changes
Allosteric regulation
Metabolic pathways







ABCDEFG
5
6
enzyme enzyme enzyme
enzyme enzyme enzyme
enzyme
1
2
3
4
 Chemical reactions of life
are organized in pathways

AP Biology
divide chemical reaction
into many small steps
 artifact of evolution
  efficiency
 intermediate branching points
  control = regulation
Efficiency – This slide is extra
 Organized groups of enzymes

enzymes are embedded in membrane
and arranged sequentially
 Link endergonic & exergonic reactions
Whoa!
All that going on
in those little
mitochondria!
AP Biology
Feedback Inhibition
 Regulation & coordination of production


product is used by next step in pathway
final product is inhibitor of earlier step
 allosteric inhibitor of earlier enzyme
 feedback inhibition

no unnecessary accumulation of product






ABCDEFG
1
2
3
4
5
6
X
enzyme enzyme enzyme enzyme enzyme enzyme
AP Biology
allosteric inhibitor of enzyme 1
threonine
Feedback inhibition
 Example
synthesis of amino
acid, isoleucine from
amino acid, threonine
 isoleucine becomes
the allosteric
inhibitor of the first
step in the pathway

 as product
accumulates it
collides with enzyme
more often than
substrate does
Other example – insulin, oxytocin
AP Biology
isoleucin
e
Don’t be inhibited!
Ask Questions!
AP Biology
2007-2008
Ghosts of Lectures Past
(storage)
AP Biology
2007-2008
Cooperativity
 Substrate acts as an activator



substrate causes conformational
change in enzyme
 induced fit
favors binding of substrate at 2nd site
makes enzyme more active & effective
 hemoglobin
Hemoglobin
 4 polypeptide chains
 can bind 4 O2;
 1st O2 binds
 now easier for other
O2 to bind
AP3Biology