Biochemistry by DR - Azam
Biochemistry by DR - Azam
Biochemistry by DR - Azam
CARBOHYDRATE METABOLISM :
Portal View
Egeption
gestion
Fructose
Intestine
Galactose
maltase
Maltose , Glu + Glu
sucrose sucrase> Glut fructose
Carbs
i. The end
product of digestion of .
is
Glycogenesis
-
-
-
→
quit Glycogen
t -
t
s -
brlycogendysis
↳ twose
Tanter
-
I
Nat
Nat InDependent Dependent
GLUT SGLT
Name Location Features
GLUT-3 RBC's
->
Glucose
[Ability to attract
- Placenta
glucose
even
cusing Hypoglycemia]
GLUT-2
-
Lines ->
It allows both
kidney enticy
as wellas
-
of geueose
B-cell release
of pancreas
-
GLUT-Y ·
-
Heart
**
GbUT-5 -
speematoxoa
->-
Transports Fructose
-Testes
-
Intestine
GLUT-1 Endoplasmic Reticulum
-
(Line)
Nat Dependent
SGLT-1 Intestine
Absorption of
-
-
glucose .
SGLT-2
kidney , peabsorption
·
->
(PCT cells
of glucose
.
19th July
'
21
Oxidation :
1- Oz
-
Hz
e-
-
oxidatn
a) I
-1
, I
Iodide ion Iodine
'
Substrate aid"
> Product
✓
Hz -
"TdALYtoTu) : NADT
FAD >
-
NADH
FADHz
+ H+
ETC Electron
Transport Chain)
AYP
-
ETC ELECTRON
Aka
TRANSPORT CHAIN
Chain
Respiratory
complex I
-
Surinate
Dehydrogenase
"
II ·
Cytochrome Reductase
11
Ñ -Cytochrome
Oxidase (co cal,
,
ns)
11 ✓ · -F
,
Particle
•
Mechanism
of ETC
g-F-F.mn#--
!
• Matrix
" ""
¥++Hµ*II¥
-
NADH At
- - -
-
+
-
<
-
"
←
*
-
+
NAD
-
i
EIHXTH-j.es#ET+Eotnoiside.--FADH2
-
Oxidatn ?
↳
-
-
-
-
-
-
]
-
l !
I -
④I•¥
-
→ FAD
-
-
- -
I 02
I
Oxidat
"
II •
→ Hao
+
mil
Phosphorylate I%=yADPtPi ATPsynthase
> fft
In ETC Oxidative
Phosphorylation
°
ATP
• .
,
is
synthesized by .
synthesis of ATP 2
Oxidative
Phosphoryl Substrate level
Phosphorylation
"
at
NADA + Ht FADHZ
Complex - I
v v
coqfvsiqu.mn Compl e x II -
carrier
NADH
dehydrogenase Succinate dehydrogenase
Compt e s Ñ
NADT
"
9-0 1^-0 SFAD
Phenobarbital -
Matonak
Rotenone Cytoaome Otaki Antimyein ,
BAL
Ghc
-
Oz
Ñ
Complex
-0 oxidation
cut,8⑧ > -
Iydase
→
Has HÑ
cytochrome
ADP t Pi
Oligonyein
-0
>
Complex Ñ '
-
Phosphorylation
> ATP
Fo -
F
particle
Mobile carriers
of ETC
•
1.
Coq ubiquinone : bet
"
Cyt bet
Complex II & I
"
a. -
C :
•
Nncouphrs
1
:
: 2,4 DNP
egg
Aspirin
•
Physio3logical Nncouphrs :
i. Thermo
genin
(Brown Fat)
a.
Thyroxi
Free
ne acids
3.
fatty
9. Bilirubin
Act
Glu
qLUT
% 021GW @ c) X
am
Glu
02GW
1 Aerobic
1
'
,
Glycolysis jibnaaobie
cytosol ighuotyn
's
1
t
v
Lactate
Zpyruvate @ c) - ✗ →-
Inform Intermediate
'
step Pyruvate @ c)
Mito
Mitochondrial
Matrix
sink
reaction { Acetyl
vPDH(pyruvate dehydrogenase)
CoA @c)
*A
Oxaloacetate # Citrate
QQ 164
KREB 's Cycle I
f
i 1
Succinyl GAS A-
ketoglu@tarate
@ c) c)
GLYCOLYSIS :akI Embalm
camp) Mayuhoff Pathway
•
Glu >
Pyruvate '
"
Glucose
°
Cytosol .
- c- c- c- c- c- C
-
from
molecule to other
µyp one
☒< Glucokinase
Hexokinase
.
•
Reactions : ^
Glu -
b -
p
c- C -
c -
c -
C -
C -
Isomerase
ttsomuigatn : same
structure
format
diff
F¥_ 6 p
a
- -
→
- -
-
c-c- c- c- c- c -
p
o
few ↳ HROG
ADDv☒ 1)
-
PFK -1 ( phosphofsuktokinase -
cruel
mutase : ⑧
P -
fuel ,6 ,
C -
C -
C -
bisphosphate
C -
C -
C -
p
-
moving
from one 'C b- another
'
'
C' on same molecule
v Aldolase v
DHAP G-3- P
dihydroxy*
acetone
phosphate NAD+
Pi
Glyceraldehyde *
-
Phosphate
3-
G- 3 -
p
dehydrogenase
>
,
.5atp
bisphosphoglyarate
.
a
NADH + H"
1,3
G- 3- p
ADP
Phosphoglyaro
? "ACI% ✓
Kinase
Phosphoglycerate
µ
3-
MUTASE
✓
2-
Phosphoglycerate
H2O # ENOLASE
(PEP) Phosphoenolpyruvate
@P)
ADP
pair Pyruvate kinase
ATP ' ✓
pyruvate
•
Energetics :
'
Mechanism .ofATP
Enzyme No
SLP
2.
Phoqphoglyaro
kinase
LATP 's
Pyruvate /kinase
3. SLP ZATP 's
4.HR/Gk -
IATP
5. PFK I
-
-
IATP
Total RATP
Aerobic 7ATP
i. Net Gain of ATP in
Glycolysis is is
Arcusobic n 2 ATP
10T¥
-
Irreversible Reaction B,
t.HR/Gk [Ist Step ]
2. PFK g-
[RLE]
3. PK [Last
Step ]
•
Regulation of Glycolysis : -
Inhibitor : Fluoride
-0
> Enolase
(NaFS
HK vs GK Glu
•
all tissues oliver
•
✗ • Insulin v
G- G- p
① Aerobic
Glycolysis
Anaerobic
Glycolysis
RBC
↑
I Oa 0.x
& &
No mitochondria
mitochondria Mitochondria
1
Anaerobic
Glycolysis
Mitochondria
8
=>
RBC has Or but no
So No
Aesobis Glycolysis
.
Anaerobic
Glycolysis : no 02 & mitochondria
•
no
Glu
Poconori
:
ATP
✓
G- 6- p Eg
Five -
G p
-
ATP *
Fsu -1,6
bisphosphate
L
>
DHAP
NADIA
G- 3- P a
3- P
i
G-
*
NAD V '
NADH + H+
1,3
bispg
}
v
bispg v
ATP 3bar
{
>
.
1
3.
by
I
2Ñg
{
I
2Ñg
✓
b
PEP
v v
NADH + Ht
NADT
ATP
PEP < ✓ a
SATP
Pyruvate > LACTATE
Pipuvate ✗☐µ
lactate dehydrogenase)
LATP
:O Net
gain of
ATP in anaerobic
glycolysis is
* Clinical Co relation
- : -
-Y
Anemia
1.
Pyruvate kinase
deficiency : Hemolytic 3 Not Natkt ATPase
No being bodies
1¥
- -
-
- -
.
-
2kt
nay
doe ATÑ
.
synthesis -
-
-
-
-
-
-
"
ftp.MOLYSIS ANEMIA :
LINK REACTION
3
conversion
of Pyruvate to
Acetyl co A. -
Cumin
Oxidative
NAD+
Pyruvate ② c) thymine
to
PDH complex me -
enzymes
5 i.
Lipoic Acid
H"cAt§
NADH + Pysvale Dehydrogenase 2.
it )
Tppftlhiaminepyrophate
to A
-
④ 3. CoA
4. NADT
so FAD
Location -
Mitochondrial
Matrix
Acetyl 6- A @ c)
-1 citrate
synthase
OAA
^ @c)
> Citrate @c)
NIDH NADH + Ht
>
Aconitase
(reversible) µ, , I
* µap+ ✓
fumarase µ µzo→✓
Aconitase
Fumarate Isocitrate
farm.
[
>
SDH
*
FAD NAD *
Succinate NADH + He
I④ÑRLE
ADP
[ succinate
thiokinase
NADH +
a
H+
,
·
stiff succinyl 6A
NAÑ *
to succinate
④)
,
2- KGDH
L -
RFT
(S2)
I. Net
gain of
ATP in KREB 's
Cycle is IOATP
from each
molecule of Acetyl G- A
Krebs
Cycle : -
•
XKGDH : oxidative
decarboxylation
• 5-
Coenzymes :< VitBcompkxwM Vitamins Krebs
liloic acid reqd.in
TPP > Vit / thiamine
B, cycles .
Fructose Metabolism : -
nosymptoms
honey >
① y
-
Jerome {
V
② Fructose -
I -
p
Fructosemn.TL
V
intolerance aldolase BX
qµ pmg.se -
sorption
DHAP
Glyceraldehyde
j V
Metabolism
Galactose Metabolism :
Mike
Galactose
-
- Milk
products
Galactokinase
| God !g
{ { Yum
.
-
-
-
p D
%dÑd
-
.
UDP Glu
✗
'
£t"
-
"
" "
" "
Transferase (GALPUT)
Galactosemia
Galactose Glee
!1 -
p
Glee
-
Galactose
✓
Metabolism
" "
-
GLUCONEOGENESIS :
~
Protein
carbohydrate sources .
egg
Acids
Acid
leucine ,
lupine
IPG -
A Pyeuvic
Lactic Acid
Glycerol
} cytosol Mitochondria
tocat " : Liver 90% +
-
.
kidney
10%
? will not
☒ glucose -6
phosphatase
>
Glu Dte : Gluconeogenesis
I occur in Skeletal muscle
G- 6- P bcgofabsenaofG.lu G- -
1,6
v4
f- 1,6
7
bisp .
RLE
DHAP 3- P
G-
iiosbpg
✓
Zpg
V
2pg
V
PEP
MD "
Malate > OAA cartoony kinase > pep
Ñm€,
Matata
Mito MDH
OAA @ c)
gy.carboxylase
ua#Pyuwate&d
I
Biotinlaswengyme)
↑
CORI 's
Cycle Exercising
Skeletal Msl .
* one ,
%
>
!
Pyruvate Alanine
+
amimpymate
tractate
(lactate
Alami?
- ← LACTATE
< Alanine ←←
←
/
Alanine
<
Li
Blood Vessels
Gbu -
Alanine
Cycle Cahill Cycle 's
GLYCOGEN METABOLISM :
Structure
•
of Glycogen :
1.) Storage form of glucose .
3) " "
a branched polymer
G-
Go
:¥÷¥÷
-
:-c
,
-
a ,
^
✗ It a) Glycosidic
> bond At the BRANCHING POINT
}
✗ ( 6) Gtywsitic
→ bond
.
&
Comore )
GLYCOGENESIS :
def :
Glu >
Glycogen
•
location : liver
skeletal mud . Cytosol
• reactions :
G
I
G
Protein
5* branching
**
RLE
4
Gcogenin A
enzyme
>
GLYCOGEN
@I}
synthase
I -
D
>
linear chain
UDP -
Glu
aÉ
activation
GLYCOGENOLYSIS :
•
def : Glycogen > Glu
• location : Liver & Steel .
mslifcytosd .
↳
" a-
•
React a-
g- semoved
I
g.
glucose
G- G-( (G. G. - -
G. -
-
G
-
G -
q -
q
-
for &
-
Glycogen
• • •
RLFC)
V
G
G- G
-
g-
Ge G -
G G -
-
H -
G -
G G G
-
-
3
Limit dextrin
debauching enzyme
V
G -
G -
G -
G -
G -
G -
G
linear chain .
Glycogen Phosphorylase
v
Gbu - 1- p
Mutase
Gbu - 6 p -
Glu -
6- phosphatase
Glu
Glycogen glycogen phosphorylase✗ VI
Heros
branching >
cytosol enzyme
linear chain } limit dextrin cytosol
glucagon synthase
> glycogen
¥2s:)
Tiffani .su
debranchingengyme
/pomp Aajidualtase
"
UDP -
Gop
activation ,F u
glucosidase
Glu Glu -
l -
P
1 Mutase
dysosome Glu b p -
-
1 / Glut b- phosphatase
dis
Glycogen storage :
Glu
Name
Enzyme deficiency
1.
Type -
I :Von Gierksdis :
Glu -
6-
phosphatase
2.
Type :
-
cows dis :
dekranching enzyme
&
.
:p ?s f)
3.
-
:
->
-
⑦ Glycogen
.
Glycogen
muscle
Gap
Gop
.
v ~
I Yoon
HER 's
/vI Mcttrhde 's
I
I Pump
2 A HI Cori
A- B C D
II And
Cori's/
If
Anderson / I
{ I Maker8
's
...
tired
Type I Anderson 's dis
a. :
branching :
enzymes
- ->
Pathway -
-
•
Jump Pathway
.
2
sign
1) NADPH .
•
Location : Adrenal Cortex
Testes
Ovaries
Placenta
Adipocytes →
Cytosol
Lactating Mammary Gland
RBC
Neutrophils
Eyes Class)
Reactions :
Glu b P
"
- -
I NAD.pt )
phosphate dehydrogenase
*
① idat "
p☐§w .co
1 g. g.
>
NADPH + Ht
y
t
Fru G p
-
-
•
Role of NADPH in RBC : Removal
of free radical Halk .
µµµµ!¥h¥hi
g÷¥µ②,µ °
Glu -
b - p
*
I NAD.pt
}
Oxidat
I GGPD
"
leads into
, camping
t , • • • •
Fru 6- P -
•• • •
being bodies
1. Glutathione Reductase ¥
2.
Glutathione Peroxidase
µ Co enzyme) -
Anemia
w GGPD deficiency leads b-
Hemolyticbodies
-
.
Heinz +
-
Anemia
-
1st mcc
of Hemolytic
bacteria .
HMP G- 6- p
shunt
& I NADPT
I GGPD
I NADPH + Ht
neutrophil > 1- Oz
4- 5 lobes ) d
F-Gp ]
Hyon
✓
Kill bacteria
cytosol
ATP
cytosol
✗
✗ CO2
Proteins
Chemistry of : -
Proteins Acids
:
polymers of L d-Amino
-
okay
polypeptides lA¥ÉA? -
AA -
AA -
AA -
AA
peptide bond
Amino Acids : -
• It is a carbon
compound
acid
e- consist
of Amino
group -1MHz)
&
carboxylic group
. -400M)
,R(Alkyl group)
Ntfz f COOH
-
-
*
*
R
o I
C
Nltzt
cool
-
-
H
tnt in our
body
z
+ relation
Sons Twitter ion
-
ve Anion
**
classified of Amino Acids
"
:
I. Based on structure -
Tgp
Aliphatic AA Basic A. A
&
1. : 5.
simplest -
Glycine lysine
Alanine
Valine
arginine
histidine → Some essential
PB.LA
"{ Leucine
Isoleucine 6 .
Aromatic Ant .
2.
Hydroxyl Gp containing
.
A. A.
Tyrosine
Tryptophan
Serine
Threonine
Phenylalanine
7. Amino Acid
5- AA
3.
ulphur containing Proline
Cysteine
Methionine
a. Acidic AA
Aspartic acid
Glutamic acid
Asparagine
Glutamine
II. Classification based on
Nutrionalreqd .
-
Essential A. A (not produced in
body)
eg.TV till 8pm .
Non essential A. A (
produced in
body)
-
-
Rest all
og
.
Semi essential A. d-
-
Arginine •
A. A
1.
Ketogenic
eg
.Leucine > Lysine
2.
Glucogenic &
ketogenic
eg
.
Tyrosine
PITT Tryptophan
phenylalanine
Isoleucine
3.
Ghecogenic AA .
all
eg. Rest
Codon-
Stop
o 21st AA :
Sdenocystine UAA
UAG
I
UGA
-
-
formed
codon :
by
UGA
SERINE
22nd A. A
• :
Pyrro3 lysine
codon : UAG
PROTEIN METABOLISM f.
Protein Rich diet
deaminat
"
:*
!
D
.
go Proteins
r v AYA
Ntlz Keto Acid
Ammonia
!e÷÷i÷÷÷**
Ammonium Jon
Nflgt + coz
Carbonyl Phosphate Synthase I
-
cytosol
Ornithine otolornithinetrcanscarbamoylase
3
NREA arginase
,
arginosucciinate
NH , CO-
-
Ntlz b- synthase
imginosuccinase ✓
Arginine ✓
A
Fumarate
Arginosuccinak
• Source
ofwua : NH , - CO -
Ntlz R
I
itxpartak
"
Ammonium Io .
->
At NHst- C-COO-
I
ion
H
Metabolism of Aromatic A. A
Que
Tryptophan
•
TyÑsine ①Melatonin
•
Tryptophan ② Serotonin
/5-H5
•
Phenylalanine ③ it-By/niacin/Mctinic
I
[boing tryptophan -> Longniacin)
peartrop's d/1
42
Absontice oA A From intet
Metabolism
of Phenylalanine &
Tyrosine
.
-
& iryptophan
e Pallagra likerptur
F
phenylalanine
0VÑ 5) Tyrosine
phenylalanine Johnathan
-
OH > Melanin
Tlztq
Catecholamines
( DA NE Epi)
, ,
Idopamine Nosepis
,
PA
CONVERSION
of b-
Tyrosine
P.A. -
# Tyrosine
on
>
tetra
hydro dihydro
biopterin cbiopterin
CBM) (BMeS
Ck :
Phenylketonuria (PKU)
PAH &oft
enzyme deficiency :
FORMATION of Melanin
tyrosinase
Tyrosine > Melanin
Ck : Albinism
vitiligo
FORMATION of Tz Ta > follicular cells :TzTq
i.IT?i-8.:i.Jii- A- cavity
Para Cells
follicular
¥ %jo
> -
a
. C- Cells
Calcitonin
-
>
z
Sakitoner
sympostudvi.SI
-
Natal
①
Ñh"d"*
÷÷!÷¥
>
follicular cavity
-
"
I AA-AA-AA-T-AA-A.tt
oooo
Tyrosine
>
1
g- I
> Nt
.
-
. :*
d -•TPO > I
tyrosine tyrosine
I
VV
Tetraiodo
✓ v
Triiodo
•
thyronine
&
thymine
•
Formation of Catecholamines :
P.A.
PAH
-
OH >
Phenyl Alanine Hydroxylase
C -
↳
OH
tyrosine
>
✓
DOPA
TH
(dihydroxy phenylalanine)
Tysosine Hydroxylase
DORA
Cozi
✓
decarboxylase
DOPAMINE
DH
-
OH >
Dopamine Hydroxylase
Nfethyl ✓
Ctb Non
epinephrine
Fmdu%kn%K SAM
-
methyltransferase
8AM a
EPINEPHRINE
S-adenosylhomocysteine
Degradation of Tyrosine :
Pathway Needed
Nos
tyrosine
-
ttomogentiHomogentisale
sate.tt **
*
I
I Oxidase
Mateyacetoacetate
Fuimarylacetoacetate
fumarate Acetoacetate
CK :
Atkapbnuria Black Urine disease e
enzyme def : H 0. .
color
CIF : urine
-
on
long standing turns BLACK Coke .
(
Ochronosis accumulate
of HQ .
in the
cartilage pinna
, ,
sclera etc
,
)
TRYPTOPHAN -
Anp products
. : i. Melatonin
2. Seretonin 5- HT
o
b TRYPTOPHAN
CIF :
Pellagra
-> like
symptoms .
Metabolism Aliphatic A. A
of
9¥
•
•
Glycine
Alanine
Valine
SBCA'S
•
• Leucine
° Isoleucine
*
GLYCINE :
Man : s :
Simplest a. a I smallest
most abundant
s : a. a in
collagen
Protein
3 : bends
flexibility in
functions : >
1. home
synthesis Ltdb)
Succinyl to -
A +
Glycine
s -
ALA
Home
Purine
2.
CaCñN7
Ring formation I
→
Glycine
i '
¥
3. Glutathione formation
3
(tripeptide) Glutamate Cysteine
- -
Glycine
4. Creatinine
5. Neurotransmitter
6.
Conjugation of Bile Acids
ALANINE
&
•
Glucose Alanine-
Leucine[}
Valine
Isoleucine
✓
Branched chain
✓ keto Acid
dehydrogenase
Products
CBCK D)
co
3g & epyeuvate
complex
Dehydrogenase
enzymes
-
->
Intrate
areti drogmas
3
✓ e
leads into : =-
Lipoic Acid
deficiency
•
CIF : burnt
sugar
like odour
-
MEGALOBLASTK ANEMIA
☒
9
homocysteine P homocysteine
• •
GAP
methylmalonyl
•
(MMC)
Metabolism b-
of containing A. A .
Non -
epinephrine
1µF , >
Methionine > SAM -
methyltransferase
homocysteine
/itB1
methyltransferase
Homocysteine
ftp.fthyl - - - -
r
SAME
Tetra
Hydrofolate b- adenosyl EPINEPHRINE
T homocysteine
Folic Acid
VitB9
Propionic Acid Pathway
FÑendmnµf¥→
✓ : Valine
0 Odd chain
:
Fatty Acid
M : Methionine
1 : Isoleucine
Propionyl to A
T : Threonine
coz , Propionyl CoA ¥
,
carboxylase/Biotin
Methylmalonyl CoA (MMC)
Methylmalonyl CoA
mutase
/Vit Bit
Succinyl 6A
Metabolism of Basic A. A
☐ Histidine
*
decarbonylation
> Histamine
•
Arginine >
Urea Cycle
Nitric Oxide (No)¥
#
L
Arginine
nitric oxide synthase @
% No
Topic : LIPIDS
chemistry of Lipids /
lipid : Esters
of of fatty acid and
glycerol
organic chemistry :
Estrification
carboxylic acid
COOH
+ Alcohol
OH
Ester t Hao
É
-
-
3 I o
-
- -
fatty acid +
glycerol → Estee Cupid)
§ -
FA
Y
-
FA
e
F-
-
FA
R
O
I
Lipid triglycerides fats
FATY ACIDS
def long
: chain
C- C
carboxylic
-
C - C -
C
acid
-
COOH
1
classification of F. A
1. Based on no.
of double bonds
•
Saturated FA > no double bonds
• Unsaturated FA
z
MUFA : 1 double bonds
PUFA : 1 double bonds .
c-)
r
* Essential F. A. :
:
I most essential
#
no .
of double bonds :D
-omega
1. LINOLEIC ACID 1.8 : I 4,12¥ : no
no .
ofcarbons positionofdb prega
LINOLENIC ACID 18 :3 (9112,1-5) :
-oregant
.
2. wz
LIPIDS
simple complex
1
volgate
I
( FAT Abe ) (FAtAkt PCH
)
Protein
Fpd
z
i.
Phospholipid
Glycolipids
waxes
Oils
fats a.
3 3.
Lipoprotein
(FAT Glycerol) ( FAT Alcohol Except
Glycerol)
PHOPHOLIPID
FAT Alcohol +
Phosphate
< >
FA 1- Glyurdtp FAT
sphingosine + P
F-
spingomydin
Neiman Pick
dlsbpingomydinaseYVGLYWLIPIDFATA-lc.tc.t
-
L
s
FAtAkot monosaccharide FAtAk 1-.
Ol&igosaccharides
3
Cerebroside Gangliosides .
I &
Gluwurebroside Galactoarebroside
GAUCHER
's FABRY dls Galaetocaebsosidase
's d-
Types of LP 's :
Chyhomiown
•
" >
•
VLDL
lipid t
Apoproteins IDL
•
LDL
ApoA Apoc
•
TG
cholesterol HDL
ApoBqgApoE
•
Metabolism
of Chylomioons :
g. g.
.
"tApoÉ
, A- pot 1
And .
d-
e + receptor
a
¥i¥÷÷
Chylomiowns
Bloodhound
}
↳
①-n_ Lipoprotei
Es ↳PL -
TG ApoB.az
and Lipase
Aport
.
Chylomieron Remnant
Metabolism
of VLDL : -
fat
Endogenous
!mxqq¥poB
>
synthesize
Kei *
Chol .
-
Apoc "
^
Blood[) }
e " Ph
VLDL
•\TqtApoBi00 And
Apo E
.
-
TG -
Apo Bioo
Chol .
LDL
HDL
AMA
Tg
-
:
Apo F-
Chol
-
Apoc
.
-
Composition of LIPOPROTEINS
cholesterol ? LDL
Name Apoproteins Lipids { c-
c-
has highest
has highest TG ? VLDL
culgamicrons
e)
Chybmioons Apo Base Esc,
In Apopaoo ,
HDL Apo A ,
E ,C
Functions
of Apo proteins
}
ApoBA8
Apo Bioo interaction
of lipoprotein c-
Receptor
Apo E
Acyltransferase)
LIPID METABOLISM
Synthesis of cholesterol
•
AÑgAf+ Acetyl GA
Auto
acetyl CoA
acetyl bA→ v
* *
1 RLE
HMGGA
HMGCoAReductase_mm)
&
inhibits @ 0A)
Statin
i
Y
Mevalonate
↳ renoid Units
Squalene
Chibstrd
cholesterol
degradation of :
CHOLESTEROL
Vit?D
' >
duty ↳ A ¥ÑmwÑ¥ÑÑonyl
CO2
↳A
tatty acid synthase
complex
>
fatty Acids
Degradation of F. A : -
LIPIDS
lipolysis
f- A GLYCEROL
B- oxidatn
of
Fatty Acids
Acetyl Co -
ketogenesis
ketone Bodies
B- oxidation of F. A .
I
3
stages
Activation
g. -
Cytosol
2.
Transport
[carnitine Shuttle] *
I. ACTIVATION :
cytosol
FACPALMATICAUD : 164¥
-
c -
c -
c - c -
c -
COOH
LATP
>
Acyl CoA Synthase
v
-
Acyllott
C- C- C- C- c- CoA
"%m.{[
matrix
cytosol
"& " " Gomi" carnitine
^ '
Acyllott
CAT -1 CAT -2 (carnitine acyl
transferase)
CoA
' s Acyl → Acyl CoA
carnitine carnitine
II. B- oxidation Proper : Mitochondrial Matrix
>
FAD
Ayllo A
Oxidation Y
FADH2 <
B- keto
Acyl CoA
*
Cleavage
' >
Acyl CoA
Acetyl(CoA
2C)
ENERGETICS 8
gain of
Net ATP : 106 TFADH x 1 5.
=
10 5
.
5 17 5
NADU2 X 2
-
↑
- =
.
- Acetyl (Krebcycle)
8 CA x10 =
80
1
- -
-
108
< Activat 2
-
Note
End Product
Fatty Acid
Even Chain
fatty acid Acetyl CoA
Odd "
(OMIT)
" •
Propionyl GA
KETONE BODIES
1. Acetoacetate
2. Acetone
3.
B-
Hydroxy Butyrate
KETOGENESIS
z Retone Body Acetyl CoA +
Acetyl CoA
i. VK.rs : acetoacetate
D. location : liver Mitochondria
D. K B. cannot be utilized
✓
Acetoacetyllott
.
Acetyl CoA →
AMIGA
Acetyl bA←✓
Acetoacetate
>
<
Acetone B-
hydroxy
butyrate
21st '
21
July
NUCLEIC ACIDS
DNA RNA
C- rely
DNA
charged)
•
§{
-
double stranded
nucleotide
-
helical
strand :
-
polymer of
complementary pairing
-
-
anti
parallel
-
IN
Nucleotide in
i.
Sugar
P : poi
'
2.
gp
-
.
3.
Nitrogenous Base
5
Sugars 3 CH o
•
•
q p
deoxyribose sugar ¥4 3 I
Base
Nitrogenous :
major
Purines
Pyrimidines
adenine
cytosine
- -
guanine thymine
- -
minor
hypoxanthine
-
Xanthine
-
Uric Acid
O O
NB
P 4
←
I NB
K g s •
2
3
NB nucleoside nucleotide
NBTS NBTSTP Adenosine
pay
-
guanine Guanosine
GMP.CMP.
GDP.GCTPpyycytosi
DP.
n el
CTPthymine.MU
Thymidine
y ti d . m e TMP.TDP.TW
1
Uracil Uridine UMPGUDPGUTP
@N*)
Structure of DNA :
-
Watson Crick DNA
B- DNA µ bond
zgnpzi.ms
-
: weak
P ↳
<
-
s -
A
Phosphodiester o
MtMP'(break)
bond P -
s + A Mph .
I
-
S
-
-
bond
p
strong P -
s
q
-
C S
Hemp
-
•
-
p
.
p.ph P -
S A T
-
S
1
-
-
p
-
does not P -
S c
G
-
-
S p
break 3
. -
51
Chargeftp.s Rule
No
•
of purines of pyrimidine
•
.
=
no .
At G = C + T
2.
Complementary Pairing
A
:)
pie
÷
Mr T
A- In . a DNA
, if G. = 15% ,
then 1- =
?
A = -1
G=C
Of .
In a DNA ,
if A =
75%
z
,
then 1- =
?
not
possible
1
does not exist
for could be
•
ss -
DNA
Types of DNA
A B C D E 2
& I
0
B- DNA
Watson-Crick DNA
I
•
As • ds
Denaturation / Renaturation
Melting Annealing
vice versa
Atemp9pH
ht bonds Break
-
Organization of DNA
Mmmmm
⑦hgT
chromatin
to
mmr
ou v
nucleosome
3
Einar v
•
histone protein Linker DNA
DNA
+
bats
H i
,
Histone Protein
core : Octamer
•
of histone
protein
Itza Hz
2
copies
.
HZB Hq
'
+ I + !! +
DNA : -
Histone : +
rely charged : A
Arginine Lysine
&
NUCLEOTIDE metabolism
double
ring
•
Purine
Ring -
Heterocyclic
~
CO2
i
> Glycine
6 Mt ?
Aspartate µ ? '
is THF
-
, ,
gas
① I
1
Trip ,
Yes
,
,
am
NÑ a
Glutamine
synthesis of Purine
H&¥Ribose 5- P
IÑP
AMÑ
>
Gmp
IMP ? Inosine Monophosphate
P
th
hypoxanthine
De Novo Ribose
•
synthesis .
5- P
ATP
PRPP
synthase
AMP <
N
**
Phosphorihosyl
Pysophoshateprpp)
Amidotransfoau
Glutamine
N
Phosphoribosyl
Amine -> NHc
v
Ni Aspartate
f Caco -
THF
I NzNs
I
-
Glutamine
y Calvin -
Glycine
G- Coz
IMP
"
"
AMP GMP
Salvage Pathway
Adenine -
Phosphosikosyl
PTPÉTRP + Adenine transferase
sppi
> ⑨YpÉf④
PRPP
AMP
P-p¥Éµ× HGPRT
'
>
"
p-
"*
Papp PPI
Imp
'p①
P P
PipG
- -
HGPRT
+ Guanine →
,
ppi
GAP
*A
4C Lesch
Nyhan Synd .
Monophosphate Monophosphate
:
Adenosine
Monophosphate
HYPOXANTHINE
xanthine oxide <
-0
Allopurinol
Xainthine
Xanthine Oxide
*
End
product : ÑRK ACID
Pseudo Gout
CK GOUT 3
??
crystals
3
Rosphlgestals
c-
Calcium
hypomania diaydsate
•
MSU
crystals
°
Monosodium
}
Urate
Cystals needle shape Gouty
Arteritis
RNA polymerase
m -
ÑNA
MIRNA
Translation}z
Proteins
Replication
.
: -
DNA DNA
def : DNA
dependent
>
DNA
polymerase
location : Nucleus
?
when : S -
phase of cell
Cycle }
r ye DNA-A ssotein
I
} separates
Hemi Conservative
-
Process
1
half of parent DNA will be conserved .
the strands
* DNA A Protein :
separate *
-
Protein
*
Single Strand Binding :
stabilized the
single strand [5SB'S]
* Helicases : uncoil helix
~ Topoisomerase
-
I
Nick 's
*
Topoisomerase : relax
supercool by Seating
XII/DNA gyrase
- -
I
DNA A
-
T I -
✓
T -
I DNA
gyrase SSB 's
Bag
<
- /
Replication e
I
-
DNA-A Protein 3
Topoisomerase
'
Reading
'
3 → 5
DNA
polymerase III.
-
New Strand 5
'
> 3
'
RNA Primer
•
'M
strand continuous
Replicating Bubble -
.
Primrose
>
h.GG C
TA
I'D
-
T C C
G AT
'
5 > 3
'
Replicating fork
imam'
J
'
3
5
'
D
?
z
☐
'T
5 31
LAGGING strand :
away
•
•discontinuous
1
OKAZAKI
fragments
•
RNA Prima :
formation
removal
:
:
Primrose
RNase H
I
Gap filling : DNA
polymerase -
ligation : DNA
ligase .
DNA Polymerase
Prokaryotes Eukaryotes
DNAP ✗ -
: Primrose
DNA I : gap
filling
-
DNA -
I: DNA
repair
&
DNAP-8 :
Replication of Mito DNA
DNA -
III :
leading
lagging strand
}
DNAPS
leading &
lagging strand
DNAP E -
PROTEIN SYNTHESIS
DNA
transcription
hn? RNA Chetwonuclear RNAS
nucleus *A
post-transcriptional modification
cytosol v
m -
RNA
I
m -
RNA
Translation
ein
}
Post-translational modification
TRANSCRIPTION
RNA
•
def : DNA
DNA -
dependent
>
RNA polymerase
•
location : nucleus .
Elongation Termination
zi Initiation 5
,
"
if ¥
"
TATAAT - - - - -
- -
go
2¥&dequen% C G G CAU
p >
51 3'
Region 31
'
5 Promotion
PROKARYOTES
losequnce TATA Boxthibnow
'
f-
Reading
'
Box 5
-
:3 >
(Rho)
dependent
TATAAT ' termination
RNA ; 51 > 3 z .
-35
sequence g- protein stops
RNA
formation
TTGACA remove RNA
A- = i
f- independent
EUKARYOTES ✓
termination
Box U
-25
sequence Hogness 2g '
TO to -80
-
sequence
CAAT Box
CAAT
RNA POLYMERASE
XX
:
PORKARYOTES EUKARYOTES
}
RNAP I RNA
RNAP -
=
8-
except 5s subunit
1
subunits RNAP I hn RNA, RNA
:zgµµ
-
= - m -
RNAP -
II = t -
RNA 5s RNA
factor : •
factor
1
It PROMOTAR
recognise region
Post-transcriptional Modification of
his - RNA
I " "
{☒ l 1
' ' ' '
g. q e
z@a-a-A-a.a.a
ñcapping-hmu Poly-A?ailmwM
7-
1 Introns :
non-functional
methyl Exons :
Guanosine functional
ÉPLICING : removal of Intron &
ligation of Exon
I
done
by : spliceosome snRNP 's
Snurps .
GENETIC CODE CODON
which
for an Amino
AUG Methionine
egg
: codes
for
No 64 Codons
of CODONS =
.
A "
0
pm
G
(4)
'
(g) =
4×4×4=64
'
•
Py u
mRNA UAAIUAG/UGA
AY ,
G
, " t
' 31
5
f
1
Initiation Codon Terminal Codon
"
1
Stop Codon non sense
-
codon
z
.
i. e start codon C
i.
estop .
I
Characteristic
•
feature of CODON
2. Commaless and
non-overlapping AUG )
Specificity Unambigous ( Met
'
3. > .
a.
Degenerate codon { than 1 codon }
AA can be coded
by more
3 I
RIBOSOMES :
Eu
Promos 80s
RNA :
stranded
single
•
•
linear N -
N -
N -
N -
strand :
polymer of nucleotide
•
i.
Sugar : Ribose
gp Poa
2. P -
: -3
Adenine
3. NB Pu :X Guanine
Cytosine
Py :-, Uracil
Types of RNA : .
RNA -
Funchon
Transfer of
-
RNA ( abundant )¥ of
1. r -
most
Amino feid
2. m -
RNA
3. f- RNA (smallest)
q
tiniest
f- RNA :
structure :
cloverleaf shaped
Amino Acid
DHU arm
qE±mam
Anti Codon
Arm
-
-
-
TYC
variable Arm
Arm
Post-translational Modification of Collagen
DNA
Collagen : Hydroxylation
I
✓
RNA
at
lysine &
proline
m -
OH odt
AA AA AA AA AA
lysine AA AA Proline AA
- -
-
- -
- - -
v lysyl Prolyl
Proteins hydroxylase Vitt hydroxylase viii. c.
.
Co-enzyme
->
collagen OH OH
OH
wring
on
Triple helix -
tysyl
Oxidase cu
Note : is .
DNA
MYRNA
Hotin
no defect defective
%fei.nu i Ubiquitin
"
Protein
folding -
¥ "ÑHAPEROpvEs
"
^^ ^
Proteasome
Structure Proteins
2.
of
40 linear
✗ Helix &
¥20
-
/
B- pleated sheets -==
3° 3. dimensional
40
a.
Blotting techniques
Northern blotting RNA
Southern " DNA
Wiston "
Proteins
VITAMINS -
(3-59)
vt c -
Vit A
-
Retinol Gttcohd)
chemistry ii. OH
-
2. Retinal -01+0
Aldehyde)
3.
Patino :c acid coat
-
( carboxylic Acid)
3.
Reproduction
Oxidant
Germ Cells >
Sperm
a. Anti -
deficiency diseases
1.
Nyctalopia -
night Blindess
2.
Xeropthahnia -
Complete Blindness
3. Keratomalacia corneal -
ulceration
a.
dry rough & scaly skin
,
5
Infertility
Vit - D
Vit Di Calciferol
2 Ergocalciferol
3 Cholecalciferol .
= i
hunkering
7-
dehydsodobsterd
v.v
rays
cholecalciferol
•÷m①
CC
-
OH →
25 hydroxylase
25
hydroxy
-
UCC
cholecalciferol
picot 25 Hit
-
actircatn
of Vitas >
1- ✗
hydroxylase
-
OH >
Functions
the blood calcium level
a.
Regulate " ^
ÑW
dl
r n 9-
11mg .
§
"
" "
it " ⇐
<
D
Ppabsospt Kx
,
Vit -
Cata
a
€
Difeciency disease :
>
Children :
Rickets
Vil:D
>
Adults :
Osteomalacia
Vitter
Vit ks
Phylloquinone} natural
°
.
kz : Mena
quinone
Ks : Menadione synthetic
&
water soluble
Functions :
Lut
8- Carboxylate
?É
at
vikk
Glutamate
required for
activator
dfd :
BlP.T.lt
eeding disorder
Vit f-
-
active
form : d- tocopherol
Anti oxidant
n
fund :
-
dld :
neurological disorders
Vit B Complex
Name
Coenzyme did
Enzyme
VI. B. Thiamine TPP tipoioacid Beri Beri
}
1. -
PDH - -
-
✗ KGDIH TPP
CoA
-
BCRDH
NAD
☒Cw3 FAD
Transkilobase TPP ,
> Wernicke -
KorsakoffSym
G : Global confusion
0:
opthalmopkgia
A : Ataxia
2. Vit Bz Riboflavin
-
FAD -
dehydrogenase Chidosis
.pµµ AngularStomatitis
Glossitis
3. VitBz Niacin
Nicotinic Acid NADT - "
Pellagra
Tryptophan Nitz
-
Dementia
60mg
1m Cphohtsensitive) -
Dermatitis
-
Diarrhoea
3
Death .
a. V-d-Bspanb-thenic.CA Burning foot
-
synd .
Vit Bg ALA
5.
Pyridoxine PLP 1.
synthase -
Sideroblastic
(Pyridoxal Chemosynthesis) Anemia
phosphate)
2. AST ALT
Aspartate (transaminases) Alanine
i. VitB , Biotin i.
Pyruvate carboxylase Allopecia
Biotin 2 .
3.
mcc >
Bqv Consumption of
Raw Eggs
Egg While
}
Bio-%{hnw)
" "
AVIDIN
+
3
Excreted
Urmocysteine Methyltransferase
Vit Bis
8.
Cobalamin
Vit Biz
"
i. MMT
MMC mutase
•
Mlgaloblastio
Anemia
Methy/Malony/COA •
Peripheral neuropathy
9. Vit Bq
Fdicidcid
food
DHF
1. } folate Titan
'
folic acid > > Diff > THF DNA and RNA
,
111-2 H2
{→ in
Absorption
Jejunum
did :
Megaloblastic
NTD
Anemia Y
's
Vit .
C Ascorbic Acid
functions : i. Posttranslational modification of collagen
a.
Absorption of Irun
3. Anti oxidant
-
.
dd :
scurvy
Note : Antioxidant
{
A C C-
I
most
potent
ENZYMES
A
def : velocity of Reaction
nature ? Protein t Won Protein
3 3
Apoenzyme co -
/
enzyme
Co
factor/
-
Prosthetic
group
.
Factors ?
Enzyme
EA
p
i. Conan
of E ✗ V s >
substratt Product
in .
Conan of s ✗ v
5. PH
•
of "
React I
d) I
,
t
optimum temp
temp @ 0-450)
•
of "
React I
d) I
I.
)
p 7 19
pm
PM
optimum
Michaelis Menten Graph .
: Ym3 )
constant
(8) V m.mg
.
or
concentrate
man Vel
of substrate at Half
.
Imax -
-
-
- -
-
- - -
vet of
React
" parabolic
Vms
-
(4
-
- -
,
-
i pin
i. A
1·
Is]
-
Enzyme inhibition
Competitive : Vmax same Kmt
g. Reversible Non-competitive Vmaxlv
-
knnsame
2. Irreversible
Isoenzymes ok -3 Creatine
Kinase
: LDH -5 Ck mm : skomsl
eg
-
.
Lactrite
Dehydrogenase
}
↳ Hi OR BB
Heart
-
:
Brain
LDHZ
* MB Heart
CK
Brain RBC
spleen
:
LDH }
.
-
LDH
LDHstgsk.ms
a
.
LDNz
Normally
LDD, >
-DA , <LD42
MI
Haemoglobin :
structure of theme
4
Pyrrole ring M
• I :[ :-#I
r
Piolo
porphyrin LET
home
?
feet >
Home
home
¥¥É¥¥jÉÉɱÉÉÉt
Gabin
{{ "
chain
B X or B
HEME
Synthesis of :
Succinyl GA t
Glycine
Ala synthase
pLpRhH
Vv
8- Aminolevukeniic acid
G- ALA)
lead/Pb H2O
⑦
e
'ALA -
dehydratase
PooÑobilinogen(PB4)
V
Nnoposphyrinoqen
I
Copwphyrinogen
I
Piutophyninogen
Proto Gysin
/ Foowchelatase
-
head Pb Fia _ j
>
HEME
DEGRADATION of HAEMOGLOBIN :
Hemolysis
.!
① >
rise
420days) hemoglobin
(will
release out)
EDIE &Ñ
spleen
i. :
Bilirubin A. A
°hddd
UDP
-
Glucosuria>
Arid v
°
Bilirubin
diqluooyonide > .
Soluble
Coyiucalid
-
.
won :-|
.
i. F-
.
I 1
I ✓
I 1
1 I
'
'
L -
- - - - - - -
d l
p-z.eir-w.mn#-.ui -isiein
'
Urine
- - - - -
>
Sterabilin → Stool .
v
Biochemistry LMR - Dr. Mohammed Azam
Pathway Site Rate limiting enzyme
CARBOHYDRATE METABOLISM
Glycolysis/Embden Mayerhoff Cytosol Phosphofructokinase-I (PFK-I)
Pathway (EMP)
Krebs Cycle /TCA cycle /Citric Acid Mitochondrial Matrix Isocitrate Dehydrogenase
Cycle
Carbohydrates
Inhibitor
Flouride (NaF) Enolase ( Glycolysis)
Barbiturates(PhenobarbitONE) and RotenONE Complex-I (ETC)
Malonate Complex-II (ETC)
Antimycin, British Anti Lewisite (BAL) Complex-III (ETC)
CO, CN, H2S Complex-IV (ETC)
Oligomycin Complex-V (ETC) - ADP to ATP Conversion
Nucleosomiz
ET
Boat BATE
Isoenzymes
tRNAs
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