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chem
Lecture
1
AGAIN Gizmo
notes
NOTE
to
SELF
PETITE
from
amino
acids
tissue
growth
repair
breaking
down
proteins
forenergy
colors
of
highlight
don't necessarily
nodeade.mg
toplasm meananything
itsjusttobe
more
synthesizing degrading
noes
Dna Rna
piggized
andhighlight
theimportant
essential
for
DNA
rep
gene
expression and
energy
storage
1
nucleus cytoplasm
building
up
proteins
for
tissue growthand
repair
in
cyto
I ftp
t
IIuainy.oa
g
ammunate
can
in
mitochondria condensationreaction
2
ALA
molecules
combine porphobilinogenPres
1 4
PBG
condense
linear
tetra
pyrrole
called
preuroporphyrinogen
miff
f
If
Illinois
mid
ff.fi
fiffifii
É
ÉÉfip
finger
E.tn
psiipign
hogenIl
decarboxylation and
desaturation
protoporphyrin
ix
occurs
as
red
blood
cells
120
days
iii
this
T.net.in
es
sedby
irmeatarominogenanastercomin
net
E
iIiiti1d
Q
IS
yinthesis
combines
aminoacid
fe
hemoglobin
product MITOCHONDRIA
steps
p.gg
9 fj
breakdown
nemo
to
bilirubin
key
productsbilirubinuroblinogen
stereobilin
LIVER
INTESTINE
I
1
Old ordamagedred
bloodcells
are
removed
fromblood
stream
1
hemoglobin
heme
oxigen
biliverdin
feat
co
2
heme
oxigenase
converts
heme
biliverdin
releasing
feetand
co
I
ii.it
iiintg
iiEis
in
i iii
in
the
mood
for
transport
tome
liver
iii
mm
li
ii
Ii
i
if
Pippin
converted
to
forkidneys
stereobilinfeces
7
Microbialconversion
intestinalbacteriaconvert
bilirubin
to
orobilinogen
s
unobilinogen
fate
some
reabsorbed
to
blood
converted
to
robilin
excreted
by
kidneys
rest
is
converted
to
stereobilin
osynthesis
of
porphyrins
includes
name
for
hemoglobin sequence
of
enzymatic
reactions
both
ugtgqgstgmit.ba
the
nest
inago
ONLY
step
1 is
in
mito
ae i
telaatinmitocatalgeeabys
aminowvinate
synthase
1
glycine
suing
sala
2
PBG
formation
3
t.info
haggys
aminolovinate
combine
in
cyto
to
form porphobillinogen
Pba
catalized
by
s
aminolewlinic
aciddehydrase
my
m
yim
ifII fi
iigg
g
h
4
PBG
molecules
form
a
linear
precroporphyrinogen
catalyzed porphobillinogen
deaminase
3 4
porphobillinogen preuroporphyrinogen
a.gg
g
gggggg
nmm mn.mn
go.mn mn
J
ggggg.gg
5
Proto
porphyrin
ix
formation
uroporphyrinogen 111 synthase
uroporphyrinogen 111
is
modified
through
decarboxylation
and
desaturation
to
yield
proto
porphyrin 5
Uroporphyrinogen 111
protoporphyrin
be
decarboxylase
desaturase
em
I
is
chelated
into
protoporphyrin
ix
catalyzed
by
ferrochelatase
forming
name
6 proto
porphyrin in
feet Heme
ferrochetalase
PATHOLOGIES
related
to
Hemoglobin
Disorders
Porphyrias
Enzymes
deficiencies
in
heme
biosynthesis
accumulation
of
porphyrins
sensitivity
tolight
and
urine
discoloration
s
aminoluvenate
synth
saminolovelinic
acid
deny
erase
Perprobillingen
deaminase
uroporphyrinogen
in
synth
decarbdesato
ferrochelatase
Premature destruction
of
erythrocytes
and
accumulation
of
Erittltic
porphyria
Insufficient
cosynthase
symmetric
porphyrin
isomers
Thalasemias
Genetic
mutation
affectingglobin
chain
production
Reduced
or
absent
hemoglobinsynthesis causing
anemia
www.i
iiiiiiii
iii
iii
Iii
Metabolism
or
creatine
energy
buffer
in
skeletalmuscle
synthesized
from
arginine
glycine
methionine
creatine
phosphate
rapidly
replenishesATP
during
muscle
contraction
Hemoglobin
IEase
mutation
in
p
globin
gene
abnormal
hemoglobin sickcell
shaped
RBC
Thalasamias
genetic
disorders affectingproduction
of
globin
chains
of
heme
Porphyrias
disorders
or
heme
biosynthesis
leading
to
accumulation
of
toxic
intermediates
Denovo
nucleotide
andsalvagepathways in
nucleotide
biosynthesis
de
novo
pathways
begin
with
metabolic
precursors amino
acids
ribose
5
phosphate
co uns
hemoglobin
related
diseases
in.fi
ii.t
n
iii
since
Enzymatic and
metabolic
disorders
Enzymes in
the
nemoform process
don't
function
properly
Nucleotide
metabolism
glucose 6
phosphate
dehydrogenase COPD
or
pyruvate
kinase
deficiency
GEE
11 5
the
p p
precursors
or
salvage
pathways recycling
existing
bases
in
p
fi
nEEiti
eiies
ci
iiny
mind
iii
aug
1
Glycine
is
coupled
to
amino
group
phosphribosylamine
2
formyl
group
from
neo
formylletrahydrofolate
THE
transferred
to
amino
groupof
glycinamide
ribonucleotide
3
inneramide
group
phosphorilated
to
ammidine
by
addition
of
NH
derived
from
glutamine
4
ATP
isde
phosphorylated intoADP
P
forming
a
memberimadezole
ring
5
bicarbonate
adds
to
the
exocyticamino
group
and
then
to
a c
atom
of
theimadordering
6
imaclozole
carboxylate
is
phosphorylated andthe
phosphate
is
displaced
by
amino
groupof
aspartate
7
fumarate
is
released
leaving 5
aminoimodazole
4
carboxamide
ribonucleotide
8
a
second
formyl
groupis
added
fromTHE
forming
5
formainoimidazole
4
carboxamide ribonucleotide
a
cyclizationcompletes synthesis
of
inosinate
IMP
Je
novo
pyramidines biosynthesis
1
Carbamoyl
phosphate
formed
by
joining
bicarbonate
and
ammonia
catalized
by
carbonylphosphatesynthetase
11
cpsu
2
carbamoyl
phosphate
reacts
with
aspartate
to
form
carbamoyl
aspartate
3
Carbonyl
aspartate cyclizes
to
form
dihydroo
rotate
4
dihydroo
rotate
is
oxidized
by
NAD
to
form
orotale
5
rotatecouples
to
ribose
in
form
of
Prep
to
create
orotidylate
Disorders
of
nucleotide
meta
away
ftp.fftigy
teis
decarboxylated
to
form
UMP
lesch
Nyhansyndrome
a
genetic
deficiency
of
Heart
leadin
to
over
production
of
uricacid and
severeneuro
sym
recover
purine
bases derived
from
nucleotide
turnover
or
dietand
attach
them
to
PRPP
to
formpurine
nucleotide monophosphates
key
enzymes
adenine
phosphoribosyltransferase
catalyzes
formation
of
adenylate AMP
fromadenine Prpp
hypoxanthine
Guanine phosphoribosyltransferase
Hart
catalyzes
form
GMP
Guanine Prep IMP
hypoxanthine PRPP
protein
metabolism
enetic
code
set of
rules
that
determine
how
DNAsequences
are
converted
into
amino
acidsequences
which
thenmake
up
proteins
each
codon
sequence
of 3
nucleotide
mRNA
specifies particular
amino
acids
or
signals
start
stop
or
translation
there
are
64
codons
be
code
for
aminoacids
and 3 are
stop
codons
I
uaauae
UGA
20
amino
acids
coded
by
be
codons
some
amino
acids
havemultiple
codons
synonymous 1
aminoacid
could
have
5
diff
codons
genetic
code
nearly
universal
across
all
organism
key
characteristics
degenerate amino
acids
can be
specified
by
more
than
one
codon
acuacc
alanine
unambiguous
eachcodonspecifies
only a
aminoacid acualways
codes
for
alanine
nothing
else
nearly
universal
samegenetic
code
is
used
by
almost
allliving
organisms
from
bacteria
to
humans
brings
correct
aminoacids
to
ribosome
has a
clover
leaf
structure
a
specific
anticodon
pairswith
a
codon
on
mRNAthrough
watson
crick
base
pairing
Y
alanine
andhas
anticodon
complementary
to
alaninescodon
tRNA
acts
asan
adapter
molecule
ensuring
eachamino
acid
is
added
in
the
correct sequence
as
determined
by
mRNA
Efrotein
rna
complexes
essential
for
protein
synth
w a
subunits
a
big
a
small
prokaryotic
size70s
subunits
50s 30
eukaryotic size 80s
subunits
00s
40
each
ribosom
has a
binding
sites
for
tRNA
molecules
1 site a
binds
aminoacyl trnacarrying
thenext
amino
acid
2
site P
occupied
by
peptidyl trna
holds
growing
polypeptidechain
Ribosomes
move
along
mRNA
formingpeptide
bonds
betweenamino
acids
to
createproteins
in
proteinsynthesis a
fundamental requirements
un
c
1
activation
of
each
amino
acids
carboxyl
group
2
establishing
a
link
between eachaminoacidandmRNAcodon
process
occurs
in
cytosol
noton
ribosome
eachamino
acidcovalently
attaches
to
specific
tRNA
molecule
usin
g.fi
qygg
1
carboxyl group of
theamino acid
reacts
with
a
phosphoryl
groupof
ATP
formingaminoacyl
AMP and
releasing pyrophosphate Ppi
Amino
acid ATP aminoacyl
AMP
PP
2
aminoacyl
groupis
transferred
from aminoacylAMP
to
corresponding
tRNA
binding
either
to
the 20H or
3 OH
group
aminoacyl amp trna aminoacyltrna
AMP
tiation
phase
of
protein
synthesis
1st
step
in
protein
synthesis preparing
ribosome
for
translation
1
binding
of
ribosomal
subunit
of
mRNA
30s
ribosomal subunits
prokaryotes
binds
to
a
initiationfactors
IF 1 IF 3
If 3
preventspremature
combination
of
the30s 50s
subunits
mRNA
thenbinds
to
the30s
subunit
with
initiation
codon
AUG
positioned correctlythrough
shine
dalgarnosequence
shine
dalgarnosequence
4
a
purine
residues
guidesthe
mRNA
tothe
correctposition
ma
giiiii.si
i
ia
ist
day
rennet
in
pros
in
the
complex
3
Joining
the 50s
subunit
Sos
ribosomalsubunitcombines
withcomplex
forming
a
functional
70
ribosome
known
as
initiation complex
GTP
hydrolyzed GDP
Pi
anini
factors
F IF 2 If
3 are
released
ngation
phase
of
proteinsynthesis
2nd
stage
or
protein
synthesis
aAare
lengthened
1
binding
of
aminoacyl
tRNA
aminoacyl
tRNA
binds
to
a
complex
of
GTP
bound
EF
to
thiscomplex
thenbinds
to
the
A
site
of
the
70s
initiation
complex
GTP
is
hydrolizedand EFTo
GDPcomplex
is
released
to i
regretted
it
Fries
win
ee.isand
are
2
Peptide bond
formation
peptide
bond
formedbetween
AA in
the A
P
sites
of
ribosomes
Nformy
methionyl
group
from
the
tRNA
is
transferred
to
theamino
group
of
the2nd A A
3
Translation
ribosome
shifts
one
codon
towards
the 3
end of
mRNA
thedipeptidyltrna is
translocated
from
the
A
site
to
P
site
and thedischarged
tRNA
is
translocated
from
the
p
site
to
the
Esite
before
being
released into cytosol
EF
c
and the energyof
GTP are
required forthis
translocation
Roles
or
elongation
factor
in
bacteria
E
the
aminoacyl trnato a
site
mination
phase
supports
ribosome
translocation
polypeptide
is
released
and
ribosomal
complex
disassembles
1
recognition
of
stop
codons
elongation
continues
untilthe
ribosome
encounters
a
stop
codon
Uaa Uaa uaaon
the
mRNA
2
interaction
with
releasefactors
int
the
ribosomal
a
site
3
hydrolysis andpolypeptide
release
RF
catalyzethehydrolysis
of
the
bond
between
the last
tRNA andthe
polypeptide
free polypeptide
is
then
released
from
the
ribosome
4
ribosomal dissociation
t.tt
jpi iip
w sipe
s
subunits
ready
tobegin
new
protein
cycle
at
translation modifications
of
polypeptide
chains
nslation
related
pathologies andgenetic
disorders
fragile
x
syndrome
expansion
of
cac
repeats
in
Fure
gone
causingfure tobe
silenced
stopping
production
of
FMRP
fragile
mental
retardation
protein
RNA
binding
protein
crucial
forregulatingthe
translation
mRNA
in
synaptic
plasticity
vanishing
white
matterdisease
WMD
results
from
mutations
in
EI 2B
genesaffecting
elF2B
essential
for
translating
initiation
esp
during
cellularstress
to
loss
or
white
matter
in
the
brain
Diamond
black
fan
anemia
DBA
caused
by
mutations
in
genes
encoding
ribosomal proteins
impairing
ribosome assembly
resulting
in
insufficienttranslation
particularly in
RBC
progenitor
leading
to
SEVERE
anemia
nalstep
in
protein
digestion
in
small
intestineinvolves
enzymes
carboxypeptides
A B
and
aminopeptidase
carboxylase
A B
sequentiallyremovecarboxyl
terminalresidues
fromshortpeptides
zinc
containing enzymes and
differ
in
specificity
carboxypeptidase
a
prefers
bulky
aromatic
residues
Carboxypeptidase
is
prefers
basic
residues
like
lysine
and
arginine
aminopeptidase
hydrolyzes amino
terminalresidues
complementing
carboxypeptidase
shortpeptides
AA
smallerpeptide
iii iii
i
i
Timing
f
iii
aiiai.in
i ainn
genetic
defects
like
I
seas
remove
N
terminal
residues
ALL
aminoacids
AA
can
hinder
aminoacid
absorption
in
blood
transporter
type
Neutral
AA
Cran
glycine
alaninevaline
leucine
Basic
AA
trans
ly
iii
iii
iii
c
KNEE
FEE
I'D
Fall
Acidic
at
trans
mino
acid
degradation
1
amino
group
removal converted
to
ammonia
or
amino
group
of
aspartate
2
conversion
of
carbon
skeletons
to
metabolic
intermediates
likeglucoseor
acetyl
Coa
occurs
mainly
in
liver
ii
are
Iii
ii iii
sina.me
t i
imonia
or
aspartate
3
Carbon
skeleton
transforming
skeletons
to
metabolic
intermediates
excessnitrogen
extreted
as
urea
am
m no
aciddegradation amino
groupis
transferred
from
AAto
a
ketoacid resulting
in
new AApairs
and a
keto
acid
catalyzed
by
amino
transferase transaminase that
usepyridox
phosphate
PLP as
prosthetic
group
primary
amino
group
receptor
a
ketoglutarate
whichforms
glutamate
AA a
ketoglutarate
a
keto acid
glutamate
e of
glutamate
dehydrogenase
ie
ntheu dat
mai
ftp.t
tamind
na
ketoglutarate
during at
degradation
glutamate
acts
as
nitrogen
collector
funellingamino
groups
fromvarious
AA
into
glutamate
through
transaminationbefore
releasing
as
NH
Iii
im
ii
i
iiimtti i
nogutarale
man fiiiii
aiiai
viii
i
ammination
involvesdirect
conversion
of
theiramino
groups
into why
without
first
transferring
to a
ketoglutarate
catalyzed
by
enzymes
serine
dehydratase and
threonine
dehydratase 1
both
requiring
PLP
as
prosthetic
group
1
dehydration serineloses
a
hydrogen
ion
from
its
a
carbon
and
a
nyroxide ion
from
its
β
carbon
to
form
amineacrylate
2
hydrolysis
aminoacrylate
reacts
with
water
to
yield
pyruvate andwhat
ns
deamination
process
C
connectstransamination
and
oxidativedeamination
for
amino
aciddegradation
2
step
degradationmean
efficientlyremovesamino
groups
1
transaminationtransfers
amino
groups
fromvarious
AA to a
ketoglutarate forming
Glutamate
Glu
2
Glutamate
thenundergoes
oxidative
deamination
releasingammonia
and
regenerating
a
ketoglutarate
I fi Eiiii iiiiii
AA a
ketoglutarate
glutamate
ketoacid
a
ketoglutarate NH
ear
ayatt
Tacitus
in
the
removal
of
carboxyl
group
COOH
fromaminoacids
converting
them
into
biogenicamines
on
neurotransmitters
Pyridoxal
phosphate PLP
asa
cofactor
Key
Points
1
he
decarboxylation
3
Products
Neurotransmitters
andbiogenic
amines
Neurotransie
flip ftp
e
tryptophandecarboxylase
tyrosinedecarboxylase
Histamine
n
GABA
ly
aminobutyric
acid
I
glutamate
iii iii I
yi
reactiryptophan
tryptodecarboxyla
serotonin
cos
urotransmitter
synthesis
from
AA
crucial
chemical
messengerssynthesized
from
AA in
brain
key
eg
include
dopaminefrom
tyrosine
serotonin
fromtryptophan GABAfromglutamate
Enzymessuch tyrosinedecarboxylase
andtryptophanhydroxylase are
essential
for
these
conversions
Neurotransmitters Precursor
Enzyme
function
Dopamine Tyrosine Tyrosinedecarb
controlsmovement
reward
Serotonin
Tryptophan
T.pt
maygqgase
regulates
mood
sleep
GABA
Glutamate
inhibitory
neurotransmitter
and
aminotransferase
as
diagnostic
marker
iii
iii
ii
is.tti
Ii
ii i
i
iiiiiiiiiiii
eat
iiiin
amiii.mn
i iii
i
ji
ALT
GPT
T.gg
n9nYetsraTincicate
nati
onsite
titis
or
excessive
alcohol
consumption
helping
doctorsassess
liver
health
and
guide
treatment
PE
hear
Teins
to Aa
and
rebuilding them intonew
proteins has
4 key
stages
1
digestion in
stomach
and
small
intestine
2
Absorption
of
AA
intothe
bloodstream
3
Catabolism
which
breaks
down
AAforenergy or
elimination
4
Anabolism
which
rebuilds
amino
acids
into
body
proteins
AMMONIA
produced
when
AA are
brokendown
to
generate
energyor
build
new
proteins
key
sources
of
ammonia
1
deamination removal
of
amino
groups
of
AA
2
hydrolysis breaking
down
AAduring
digestion
I
high
levels
of
ammonia
are
toxic disrupting
function
by
interferingwith
neural
signal
elimination
occurs
to
throughurea
cycle
in
liver
converts
NH to
urea Nhs acofor
excretion
in
urine
itrogentransport
andglucose
alanine
cycle
glutamine
acts
as key
nitrogen
transport
during fo
prolonged
exercise
fasting
diets
muscles
use
branched
chainaminoacids
for
ener
ggiiiig.gg
iienernauaiab
thenitrogen is
transported from
muscles
to
theliver in 2
principal
forms
muscles
by
preserving
high
energy
e
for
alanine
cycle
N
transport
form key
concepts
chemequals
glutamine
gzed
by
Glucosealanine
go
t.tt
iiig
nthet
gnua
ftp.teatjcigthlgghf
nfai.tt
a
lgiatrat
ftp.t
ft
guttaPima
to
formalanine
Type
Ketogenic
Glucogenic
Keto
GlucogenicAmino
acids
leucine
lysine
Alanineaspartate
glycine
glutamate
Isoleucine
phenylalanine tryptophan
tyrosine
threonineMetabolic
intermediate
Aceto
acetyl
CoA
acetylcoa
Pyruvateoxaloacetate
a
ketoglutarate succinyl coa
fumarate
Aceto
acetyl
CoA
acetylcoa
pyruvate
oxaloacetateassify
ketogenic andglucogenic amino
acids
AAs
canbe
classified
into
ketogenic glucogenic or
bothbased
on
whatthey
are
converted
toduring
metabolism
Ketogenic
AAs
converted
to
ketone
bodies
or
acetyl
Coa or
acetoacelyCoa
contribute
to
lipid
metabolism
butnotglucose
production
only
purelyketogenic
AAs
are
leucine
andlysine
Glucogenic AAs
transformed
intoglucosethrough
intermediates
like
pyruvate
oxaloacetate
cc
ketoglutarate
helps
maintainblood
sugar
levels
Both
ketoglucogenic AAs
canbe
converted
intoboth
ketones
and
glucose
includeisoleucine
pheny
alanine tryptophan
tyrosine
threonine
etabolic
pathways
of
pyruvate
oxaloacetate
a
ketoglutarate succinylCoA and
fumarateAA
include
alanine
arginine
aspartate
cysteine glutamate glutamine
glycine
histidine
proline
ser
couldn't
be
asked
to
write
itdownkey
equations
Pyrova acetylcoa
Pyruvate
CoatNadt
AcetylCoA
co
NADH
oxaloacetate_
phosphoenolpyruvate
oxaloacetate
GTP phosphoenolpyruvate
of GDP.sorders
AA
metabolism
Alkaptonuria
caused
by
deficiency
in
homogentisate dioxygenase
leading
to
excretion
of
large
quantities
of
homogentisic acid
darkens
urine uponair
exposure
PhenylketonuriaPKU caused
by
inability
to
hydroxylate phenylalanine
deficiency
in
phenylalanine hydroxylase
increased
level
of
phenylalanine
in
blood
symptoms
include
mentalretardation
Treatment
low
phenylalanine diet
supplemented with
tyrosine
Maple
syrup
urine
diseaseMSUD
branched
chain
dehydrogenase
is
missing
of
defefective
blockingthe
oxidative
decarboxylation
of
a
keto
acids
from
valine
isoleucine leucine
leads
to
maple
syrup
odorfromurine
and
cause
mental
physical
retardation
treatment
requires diet
of
law
valine
isoleucine
leucinezyme
deficiencies
proteinmeta
consequences2notable
deficiencies
arginine
succinase
def
arginine
succinase converts arginine
succinate
to
argine
fumarate
inurea
cycle
lack
of
enzyme
results
in
hyperammonemia due
to
accumulate
arginine
succinate
Treatment
protein
restricted
and high
arganine
diet
CPSand
otc
Cps
initiates
ureacycle
while
one
converts
carbonyl
phosphate
to
citruline
deficiency
disrupt
ureacycle
UHHH causing hyperammonemia
Treatment
protein
restricted
diet
benzoate
andphenyl
acetate
supplements
eliminates
nitrogen
as
hippurate
and
phenyl
acetylglutaminee or
vitsand
cofactors
in
protein
metabolism
elaryAA
Essential
AA
obtained
fromdiet as body
can't
produce
them
histidineisoleucineleucine
lysine
methionine
phenylalanine
threonine
tryptophan
valine
Non
Essential
AA
Alanine
arginine
asparagine
aspartic
acid
cysteineglutamicacidglutamine
glycine
prolineserine
imbalanced
proteinintake
excess
insufficient
can
lead
to
healthissues
Deficiency
stunted
growth
muscleweakness
impairedimmune
function
Excess
liverandkidney
stress
weight
gain
increased
risk
of
cardiovascular
diseasesegulation
of
protein
metabolism
a
Hormonalcontrol
Insulin
promotes
protein
synthesis
and
inhibits
degradation
Glucagon
stimulates protein
breakdown
to
provideglucose
for
energy
Cortisol increases
proteindegradation
to
mobilize
AA
C
Enzyme
control
feedback
inhibition
by
downstream products
eg
leucine
on
branched
chain
aminotransferase
regulation
by
substrate availability
eg
AApoolaffecting
proteinsynthesisrates
3
transcription
control
gene
expression regulated
by
nutrient
availabilityand
hormone
signalsLipid
metabolism
lipids
typically
referred
as
fats
Essential
lipid
roles
Energy
storage lipids arelong
term
energy
source store
more
energy
carbohydrates
structural components biological
membranes
that
surroundcells
providing
structure
and
controllingwhat
entersexits
Hormones
and
vits somelipids
actas
hormones
or
help
transport
vitamins
vital formaintaining
normal
bodily
functionsalegorization
of
lipids
Types
of
lipids
1 fatty acidsExample
Palmitic
acid
trislearin
lecithin
sphingomyelin
cholesterol
estersstructure
long
carbonchainswith
carboxyl
group
3 fatty
acids
esterified
to
glycerol
backbone
2 fatty
acids
esterified
to
glycerol
3
phosphate
derived
fromsphingosine
4
fused
rings
withhydroxyl
groupfunction
energy
storage and
building
blocks
1
energy
storage
infat
cells
major
components
of
cell
membrane
comp
ofcm
especially
in
nerves
strengthensmemb
precursor
to
norm
2
triglycerides
3
Glycero
phospholipids
4
sphingolipids
5
Cholesterolatty
acids
long
chaincarbonatoms
with coolt
at 1
end
can be
saturated
or
unsaturated
w
double
bonds
sat
fats
are
solid
unsat
fats
are
liquids
key
properties
chain
length
typically
12
24
carbons
Even
number
of
carbons
as theyare
synthesizedfromacetyCoa
Double
bondpositions
at Δ 9
Δ 12 Δ 15 in
polyunsaturated
acidsaffecting
theirstate
at
room
temp.iglycerides
composed
of
glycerol
esterified
with
3
fatty
acids
chains
1
form
of
energy
storage
in fat
cells
key
characteristics
nonpolar H2o
insoluble
store
more
energy
thancarbohydrates
Anhydrousstorage
unlike
glycogen
which
binds
water
glyceride
more
energy
g
anhydrous
Aerobicmetabolism
onlycomparison
withglycogen
energy
storage
water
binding
metabolismGlycogen
less
energy
g
bindsabout
2
itsweightinthe
can be
metabolized
anaerobically
hylomycrons
Chylomicrons
transport
dietaryfats
from
intestines
to
various
tissues
of
body
assembled
by
intestinal
mucosa
andmovethrough
lymphatic
vessels
into
largebody
veins
once in
bloodstream
chylomicronsadhere
to
capillaries
especially in
skeletal
muscle
and
adipose
tissue
Lipoprotein
lipase LPL hydrolyzes
triglycerols
in
chylomicrons
releasing fatty
acidsthat
can be
used
for
energy
store
as
chylomicrons losetheir
triglycerides
they
shrink
becomingchylomicron
remnants
RICH
in
cholesterol
remnants
re
enter
circulation
and
are
taken
up
by
liverFeature
composition
function
sizeChylomicrons
mostly
triglycerides
transport
dietary
fats
LARGEchylomicrons
remnants
Primarily
cholesterol
Deliver
cholesterol
to
liver
smallerry
lowdensity
lipoprotein VLDL LDLLow
density
lipoprotein
crucial
for
transporting
lipids
in
bloodstream
VLDL
is
synthesized
in
livercarriestriglycerides and
cholesterol
to
various
tissues
key
steps
in
VLDL
LDL
metabolism
1
VLDL
released
fromliver
and
travels
to
peripheral
tissues
2
LPL
lipoprotein
lipasehydrolyzes
the
triglycerides
in
VLDL
releasingfatty
acids
3
VLDLlosestriglycerides
becomes
IDL
intermediate
density
lipoprotein
4 IDL
furtherprocessed
to
form LDL rich in
cholesterol
5
CDC
carries
cholesterol
to
extrahepatic
tissues
via
LDL
receptors
maintains
cholesterolbalance
in
body
dysregulation
can
lead
to
I
as
VLDL
is
converted
to
LDL
deliverstriglycerides
to
skeletal
muscle
and
adipose
tissue
and
eventually
delivers
cholesterol
to
tissues
via
LDL
receptors
hypercholesterolemia
and
atherosclerosisxmetabolism
crucial
forremoving
cholesterol
from
tissues
andtransporting
to
liver for
excretion
unlike
LDL
VLDLHDLacts
as
cholesterol
scavanger reducing riskof
plaque
build
up
in
arteries
key
functions
cholesterol uptakefromcell
membranes
and
otherlipoproteins
conversion
of
cholesterol
to
cholesterolesters
by
LCAT
activated
by
Apoa I
Transfer
of
cholesteryl
esters
to
theliver
for
processingand
excretion
LDL
VLDL
metabolismFeatureHDL
Metabolism
cholesterolremoval
Apoat Cat
Reduces
plaque
buildup
function
key
proteins
Effect
on
arteries
w
density
lipoproteins
How
it
works
cholesterol
triglyceridedelivery
ApoB 100
LPL
can
contribute
to
plaquebuild
up
LDL
binds
to
LDLreceptor
on
cell
surface
2
LDL
receptor
complex
is
taken
intothecell via
endocytosis
ENDOSOME
3
Endosomes
fuses
with
a
lysosome
breaks
downcholesterol
esters
HYDROLYSIS
OF
CHOLESTERYL
ESTERS
releasing
cholesterol
andfatty
acids
LYSOSOME
LDL
receptor
returns
to
cell
surface
tograb
moreLDL
RECEPTOR
RECYCLING
CELL
SURFACEProcess
helpskeep
blood
cholesterol
levels
in
check prevents hypercholesterolemia
atherosclerosisiglycerides
biosynthesis
uses
twomainprecursors
acyl
Coa
left cn
right
formed
when
fatty
acids
are
activated
by
thio
kinase
acylCoasynthetase
using
ATP
L
glycerol
3
phosphate comesfromdihydroxy
acetone
phosphate DHA
via
glycerol 3
phosphatedehydrogenase
or
from glycerol via
glycerol
kinasePrecursor
Acyl
Coa
c
glycerol
3
Phosphate
from
DHAD
L
glycerol
3
phosphate
from
glycerolAction
Activates
fatty
acids
Reduces
DHAPEnzymes
involved
Thiokinas
acyl
coa
synthetase
Glycerol
3
phosphate
dehydrogenaseATP
usage
YES
NoGlycero
kinasePhosphorylates
glycerolYES
tivation
offatty
acids
first stepin
fatty
acids
metabolism
involves
the
formation
of
thioester
linkage
to
coenzyme
A
CoA transforming
a
fatty
acid
into
acyl
coa
Uses
2
macroergic
ATP
bonds
How
it
works
A
fattyacid
reacts
withCoA
Acyl
CoAsynthetase
also
called
fatty
acid
thiokinase
catalyze
reaction
ATP is
used
to
form
the
thioester
bond
reaction
takesplace
on
the
outer
mitochondrial
membranefattyacid
free
fatty
acid
requires
activation
using
ATP
m
in
cytosolFeature
structure
Energyusage
locationAcyl
CoA
fatty
acid
esterified
to
CoA
activated
and readyfor
metabolic processes
formed
on
outermitochondrial
membranelycerol
3
phosphate
key
building
blocks
for
triglycerides
synthesized through 2
pathways
1
from
dihydroxy
acetone
phosphate DHAP
Enzyme
Glycerol
3
phosphate dehydrogenase
Process
DHAP
a
glycolytic
intermediate reduced
to
glycerol
3
phosphate
Location
Cytosol
Uses
ATP
No
from
glycerol
Enzyme Glycerol
kinase
Process
Glycerol
is
phosphorylated
to
glycero
3
phosphate
Location
Liver
and
kidney
uses
ATP
YESiglyceride
formation
2
main
steps
glycerol 3
phosphate
is
esterified
by
2
molecules
offattyacyl
Coa
forming
diglycerol
3
phosphate
phosphatidic acid
CATALYZED
BY
ACYL
Transferases
Glycerol
3
phosphate
2
fatty
acyl
Coa phosphatidic acid
a
coat
Phosphatidic
acid
is
hydrolyzed
by
phosphatidic
acid
phosphatase
to
diglycerol
3rd
molecule
offatty
acyl
CoAthen
added acyltransferase
to
form
triglyceride
Phophatidic
acid diglycerol phosphate
Diglycerol
fatty
acyl
Coo
trigliceride
Coa
Acylation
transesterificationipolysisglyceride
metabolism
regulation
crucial
for
energy
balance
insulin
glucagon
epinephrine
play
distinct
roles
insulinpromotes
triglyceride
storage
by
stimulating fatty
acid synthesis
and
inhibitinglipolysis
activates phosphodiesterase
PD
whichreduces
cAMP
levels
and
decreases
activity
of
proteinkinase
A
PKA
PKArequired
to
activatehormonesensitive
lipase
HSC
ratelimiting enzymein
typolysis
Glucagon epinephrine
stimulate
triglyceride
breakdown
duringfasting or
stress
Activate
adenylate
cyclase
AC
increasing
cAMP
cAMP
activates
PKAwhich
then
phosphorylates and
HSL promoting
lipolysis
and
raising
blood
fatty
acid
levels
a
oxidation
of
odd
chain
fatty
acids
the final
round
yields
propionyl
CoA
then
converted
to
succinylCoA
to
enter
cytric
acid
cycle
STEPREACTION
carboxylation
Isomerization
mutaseProducts
Propiony Coa
D
methylmalonyl
coa
D
methylmalonyl coa
c
methylmalonylCoa
C
methylmalonyl c
a
succinyl
coa
oxidation
of
monounsat
FA
when
dealing
with
monounsat
FA
2
additional
enzymes
are
needed
in
addition
to
standard
1
Isomerase converts
cis
doublebonds
to
the
trans
configuration requiredfor
B
oxi
2
Reductase reduces
any
remaining
cis
double
bondsEnergy
yield of β
oxidation
energyyieldis
significant each
molecule
of
acetylCoagenerated
enters
krebs
cycle
3
molecules
of
NADH
a
molecule
of
FADHI
1
molecule
of
GTP
After
the
resp
chain
oxidizes
the
reduced
coenzymes
each
acetyl
CoA
yields
12
ATP
more
plus
each
β
oxidation
stage
generates NADH IFAD H
totalATP
yield
from
beta
oxiis
calculated
as
TotalATP acetylCoa
molecules
times
21
t
NADH
3
FAD
2
2 2
eg
Palmitic
acid 116
s
acetylCoa
7
NADH FFADH
ATP
timestimestimesrightrightrightleftleftleft 82322377111
ATPFatty
acidbiosynthes
process
of
building
FA
fromsmaller
molecules
2 key
comp
1
malonylCoa
formed
fromacetylcoaand
bicarbonate
catalyzed
by
acetyl
Coacarboxylase RATE
LIMITING
STEP
acetyl
Coa
bicarbonate
malony
Coa ADP
I
2 FA
synthetase multi
enzyme
complex
that
assembles
FA
up
to
116 palmitic acid
containsactive
thiol
groups
and an
acyl
carrierprotein ACP
