19th July

'
21

Oxidation :

1- Oz
-

Hz
e-
-

Bedim oxidation number

feta
:p Fey feta
of "
Odidat
feta > fet3

oxidatn
a) I
-1
, I
Iodide ion Iodine
'

Substrate aid"
> Product
✓

Hz -

"TdALYtoTu) : NADT
FAD >
-
NADH

FADHz
+ H+

ETC

AYP
-
 ETC
location Inner membrane
•
:
of Mitochondria

protein complexes complex I

• 5 :

complex I
"
II
11
Ñ
11 ✓

•
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

Phosphorylate I%=yADPtPi ATPsynthase

> fft

It.ro/#.-iI OxidativePhophoylat "

In ETC Oxidative
Phosphorylation
°

ATP
• .
,
is
synthesized by .

1 NADA 1- Ht > 2.5 ATP 's

IFAD Ha > 1.5 ATP's

synthesis of ATP 2

Oxidative
Phosphoryl Substrate level
Phosphorylation
"
at
 NADA + Ht FADHZ

Complex - I
v v

coqfvsiqu.mn Compl e x II -

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
"

complex I. I & II.

Cyt bet
Complex II & I
"
a. -
C :
•

Nncouphrs
1
:

It uncoupled onidat " &

phosphorylation reat
"

: 2,4 DNP
egg
Aspirin
•

Physio3logical Nncouphrs :

i. Thermo
genin
(Brown Fat)
a.
Thyroxi
Free
ne acids
3.
fatty
9. Bilirubin
 -

CARBOHYDRATE METABOLISM :

> Gh£wÑn→%

gestion
Fructose
Intestine
Galactose
maltase
Maltose , Glu + Glu
sucrose sucrase> Glut fructose

I Lactose Glut galactose

lactase
>

Carbs
i. The end
product of digestion of .
is

Glu Fructose Galactose

In Liver converted into
Glu is
Glycogen
•

Glycogenesis
-
-

-
→

quit Glycogen
t -
t
s -

brlycogendysis
 Glu

% 021GW @ c)
am
Glu
02GW
1 Aerobic
1
'
,
Glycolysis jibnaaobie
cytosol ighuotyn
's
1
t
v

Lactate
Zpyruvate @ c) - ✗ →-

Inform '

Pyruvate @ c)
Mito sink
reaction { Acetyl
vPDH(pyruvate dehydrogenase)
CoA @c)
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
-

kinase : transfer of Pgp .

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
- -

→
- -
-

AÉP Glu 661+1206

• -

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

NADH -11ft b- ATP 's

1. G- 3PDH 2 ✗ 2. b- ATP 's

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

Irreversible Reaction 10T¥ ,

t.HR/Gk
2. PFK g-

3. PK
•

Regulation of Glycolysis : -

Rate limiting Enzyme @ LE) : PFK -1

Inhibitor : Fluoride
-0
> Enolase

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
 Anaerobic
Glycolysis : no 02 & mitochondria
•
no

Glu
ATP
✓
G- 6- p

Five -
G p
-

ATP *
Fsu -1,6
bisphosphate
L
>
DHAP
NADIA
G- 3- P a

G- 3- P
*

V '
NADH + H+
1,3
bispg
}
v

ATP '
1,3
bispg v

3bar
{
.

3.
by
2Ñg
2Ñg PEP
v v

NADH + Ht
{
✓
NADT
ATP
PEP < ✓ a

Pyruvate > LACTATE

Pipuvate ✗☐µ

lactate dehydrogenase)
LATP
:O Net
gain of
ATP in anaerobic
glycolysis is
* Clinical Co relation
- : -

Anemia
1.
Pyruvate kinase
deficiency : Hemolytic 3 Not Natkt ATPase
No being bodies
1¥
- -
-
- -

.
-

2kt

Pyruvate Kinard Pkd ATP &

Nat
-

nay

doe ATÑ
.

synthesis -
-
-
-
-
-
-

"

failure of Natkt ATPase

accumulate of Nat Hao +

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§ Tppftlhiaminepyrophate)
NADH + 2.

to A
-

④ 3. CoA

4. NADT
so FAD
 KREB 'S CYCLE CITRIC ACID CYCLE TCA Cycle
Tricarbonylic acid
cycle

Acetyl 6- A @ c)
-1 citrate
synthase
OAA
^ @c)
> Citrate @c)
NIDH NADH + Ht
>
Aconitase
(reversible) µ, , I
* µap+ ✓

Malate Cis Aconitate

-

fumarase µ µzo→✓
Aconitase

Fumarate Isocitrate
farm.

[
>

SDH
*
FAD NAD *

Succinate NADH + He
I④ÑRLE
ADP
[ succinate
thiokinase
NADH +
a
H+
,

stiff succinyl 6A
NAÑ *

④)
,

2- KGDH
L -

RFT

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 B,/ thiamine cycles .

CoA > Vit Bis / Pantothenie Acid

NADT >
VitBz/ Niacin/Nicotinic Acid
FAD >
VitBa/Riboflavin .

Fructose Metabolism : -

nosymptoms
honey >

① y
-

fruit juices Essential FRUCTOSE TT

I ✗
fuectoseuria
kinase
fructose

Jerome {
V
② Fructose -
I -
p

Fructosemn.TL
V
intolerance aldolase BX
qµ pmg.se
DHAP
Glyceraldehyde
j V

Metabolism
Galactose Metabolism :

Mike
Galactose
-

- Milk
products
Galactokinase

| God !g

{ { Yum
p
-
-
-

%dÑd
-
.

UDP Glu
✗
'

£t"
-

" " "

.

"
" "
" "

Transferase (GALPUT)
Galactosemia
Galactose Glee
!1 -
p
Glee
-

Galactose
✓
Metabolism

" "

Oil drop cataract

 Hmp SHUNT RP
hexose
:

monophosphate Pentose Phosphate

.

Pathway -
-

•
Jump Pathway
.
2

Fatty acid Sym Lipids Syn Cholesterol Segno , ,

Steroid hormones

-4
,

sign
1) NADPH RBC
.

Neutrophils
Ribose b- P DNA & RNA
2)
- -
=
.

•
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

Role of NADPH Neutrophils :-O ,

dependent killing
is
of
•

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

GLYCOLYSIS HMP shunt

cytosol
ATP
cytosol
✗

✗ CO2
GLUCONEOGENESIS :

def : fromaticmAminoof Glu from

m&×apt
non -

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- -

cytosol Fib phosphatase

friar
¥&spn%%
P
enzyme
> -

1,6
v4
f- 1,6
bisp .

RLE
DHAP 3- P
G-

iiosbpg
✓

Zpg
 V

2pg
V
PEP
MD "
Malate > OAA cartoony kinase > pep

Ñm€,
Matata
Mito 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
<

Gbu -
Alanine
Cycle Cahill Cycle 's
 GLYCOGEN METABOLISM :

Structure
•

of Glycogen :
1.) Storage form of glucose .

a) Glycogen is polymer of glu .

3) " "
a branched polymer
G-
Go

:¥÷¥÷
-

:-c
,
-

a ,
^

✗ It a) Glycosidic
> bond At the BRANCHING POINT
}
✗ ( 6) Gtywsitic
→ bond
.

a) Glycogen stored in Liver and Skeletal med .

&
Comore )

GLYCOGENESIS :

def :
Glu >
Glycogen
•
location : liver
skeletal mud . Cytosol
• reactions :
 branching
**
RLE
enzyme
>
GLYCOGEN

@I} synthase
>
linear chain

UDP -

Glu

aÉ
activation

GLYCOGENOLYSIS :

•
def : Glycogen > Glu
• location : Liver & Steel .

mslifcytosd .

↳
" a-
•
React a-
g-
g.
G- G-( (G. G. - -

G. -

I -

G
.
-

G -

q -

q
-

for &
-

Glycogen
• • •

9 A

glypgiogporyhhs glucose -1ps glycogen phosphorylase

}

RLFC)
V
 G
G- G
-

g-
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 -

gln Ti linear chain

type dis
akoilysosomat
- .

Gop
activation ,F u
glucosidase
Glu Glu -
l -
P
1 Mutase
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 .

Type VI : Her hepatic glycogen phosphorylase

: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 Maker
's

branching debranching VI her

tired
 Type I Anderson 's dis
a. :
branching :

enzymes
Type I : Mc Arkle dis muscle
. 's
glycogen phosphorylase
:

Type II : Pompe dis Acid maltase

G. 's :
 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
1.
Aliphatic AA : 5. Basic A. A

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.
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-
-

(reqd.in growing children ,

QQ lactation
,
Histidine
eg
.

Arginine •

III. Based on Metabolic fate ¥

A. A
1.
Ketogenic
eg
.Leucine > Lysine
2.
Glucogenic &
ketogenic
eg
.

Tyrosine
PITT Tryptophan
phenylalanine
Isoleucine

3.
Ghecogenic AA .

all
eg. Rest
o 21st AA :
Sdenocystine
I

-
-

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

7÷: ↳ UREA > excretion

 UREA CYCLE ORNITHINE CYCLE KRF-BHHENSELF.it / cycle
location : Liver cytosol + milo .

!e÷÷i÷÷÷**
Ammonium Jon
Nflgt + coz

cytosol
Ornithine otolornithinetrcanscarbamoylase

3
NREA arginase
,
arginosucciinate
NH , CO-
-

Ntlz b- synthase
imginosuccinase ✓

Arginine ✓
A

Fumarate
Arginosuccinak

• Source
ofwua : NH , - CO -

Ntlz

itxpartak
"

Ammonium Io .

ion
Metabolism of Aromatic A. A
•
TyÑsine
Tryptophan
•

Phenylalanine
Metabolism
of Phenylalanine &
Tyrosine
phenylalanine
0VÑ 5) Tyrosine
phenylalanine Johnathan
-
OH > Melanin
Tlztq
Catecholamines
( DA ,
NE ,
Epi)

PA
CONVERSION
of b-
Tyrosine
P.A. # Tyrosine
>

tetra
hydro dihydro
biopterin cbiopterin
Ck :
Phenylketonuria (PKU)
PAH
enzyme deficiency :

CIF : pale skin

Ashore hair
Mental Retardation

Mousy Musty odour

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
"

oooo > I AA-AA-AA-T-AA-A.tt

1
g- > Nt
.
. :*
tyrosine tyrosine
•TPO >I
VV

Tetraiodo
✓ v

Triiodo
•

thymine thyronine
(B) (Tg)
I
akgtysox.im

Formation of Catecholamines :

P.A.

-
OH > PAH

tyrosine
TH
-

OH >
✓

DOPA
(dihydroxy phenylalanine)
 DORA

Cozi
✓
decarboxylase
DOPAMINE

OH >
DH

Nfethyl ✓
Ctb Non
epinephrine
Fmdu%kn%K SAM
-

methyltransferase
8AM a

EPINEPHRINE
S-adenosylhomocysteine

Degradation of Tyrosine :

tyrosine
ttomogentiHomogentisale
sate.tt **
*

I Oxidase

Mateyacetoacetate

Fuimarylacetoacetate
fumarate Acetoacetate
CK :
Atkapbnuria Black Urine disease

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

3. Vit Bz Niacin Nicotinic acid .

Ctc : HART NUP 's Disease

3
A. A. Intestine
• lose absoebtion
of in

o
b TRYPTOPHAN

CIF :
Pellagra like
symptoms .
Metabolism Aliphatic A. A
of
9¥
•

•
Glycine
Alanine
•
Valine
• Leucine
° Isoleucine
*
GLYCINE :

Man : s :
Simplest a. a

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
→
Glycine

i '

¥
3. Glutathione formation
3
(tripeptide) Glutamate Cysteine
- -

Glycine
4. Creatinine

G¥M Glycine Arginine Methionine

-
-

5. Neurotransmitter

6.
Conjugation of Bile Acids
ALANINE
&
•

Glucose Alanine-

Cycle Cahill 's

cycle .

BCA 's : branched chain A. A

Leucine[}
Valine

Isoleucine

✓
Branched chain
✓ keto Acid
dehydrogenase
CBCK D)
Products 3g
co
enzymes
-

3
✓
leads into : Lipoic Acid
deficiency
•

TPP
} Co A

Maple Syrup Urine dfs

+
. NAD
FAD
BCKD
enzyme def :

CIF : burnt
sugar
like odour
 -

MEGALOBLASTK ANEMIA
☒

Vit Brad or Folic Acid &

9
homocysteine P homocysteine
• •

GAP
methylmalonyl
•

Metabolism b-
of containing A. A .

Non -

epinephrine
1µF , >
Methionine > SAM -

homocysteine methyltransferase
methyltransferase
Homocysteine
ftp.fthyl - - - -

r
SAME
b- adenosyl EPINEPHRINE
T homocysteine
Folic Acid
Propionic Acid Pathway

FÑendmnµf¥→
✓ : Valine
0 : Odd chain
M : Methionine
1 : Isoleucine
Propionyl to A

T : Threonine
coz , Propionyl CoA ¥

,
carboxylase/Biotin
Methylmalonyl CoA

Methylmalonyl CoA
mutase
/Vit Bit

Succinyl 6A

Metabolism of Basic A. A
☐ Histidine
*
decarbonylation
> Histamine
•

Arginine >
Urea Cycle
Nitric Oxide (No)¥
#

Arginine
nitric oxide synthase @
% No
Topic : LIPIDS

chemistry of Lipids

lipid : Esters
of of fatty acid and
glycerol
organic chemistry :

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 .

2. Based on nutritional requirement -

-
-
-

c-)
r

* Essential F. A. :
:
#
I most essential no .

of double bonds :D

1. LINOLEIC ACID 1.8 : I 4,12¥ : no

no .
ofcarbons positionofdb
2. LINOLENIC ACID 18 :3 (9112,1-5) : wz

3. ARACHIDONIC ACID 20 : 4 ( 5,8 , 11,14 ) : we

Classification of LIPIDS :

LIPIDS

simple complex
1
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

glyuropholipid sphingo phospholipid

.

F-
spingomydin
Neiman Pick

dlsbpingomydinaseYVGLYWLIPIDFATA-lc.tc.t
-

L
s
FAtAkot monosaccharide FAtAk 1-.

Ol&igosaccharides
3
Cerebroside Gangliosides .

TAY SACH 's d- hexosaminidase

< S
FAT Atetbiu FATA let Galactose SAND Hoff 's B- hexosaminidase
.

I &

Gluwurebroside Galactoarebroside
GAUCHER
's FABRY dls Galaetocaebsosidase
's d-

dls ghewaeebsosidase KRABBE dts B- 's "

✗ ,
,
 LIPOPROTEINS •

Types of LP 's :

Chyhomiown
•

" >
•
VLDL

lipid t
Apoproteins IDL
•

LDL
ApoA Apoc
•

TG
cholesterol HDL
ApoBqgApoE
•

Metabolism
of Chylomioons :

dietary fat exogenous

✓

{ fun
g. ,
yqÑRBa
And .

"tApoÉ
a
A- pot 1

+
d-
Peripheral

receptor
tissue .

g. Adipocytes

¥i¥÷÷
Chylomiowns
Bloodhound
}
①-n_
Es
TG ApoB.az
and
Aport
.

Chylomieron Remnant
Metabolism
of VLDL : -

fat
Endogenous

?⃝mxqq¥poB
>

synthesize
Kei *
Chol .

-
Apoc "
^

Blood[) }
" Ph

•\TqtApoBi00 And
Apo E
.
-

L VLDL remnant IDW

TG -

Apo Bioo
Chol .

LDL

HDL
AMA
Tg
-
:
Apo F-
Chol
-

Apoc
.
-
Composition of LIPOPROTEINS
has highest cholesterol ?
Name Apoproteins Lipids { c-

c- has highest TG ?

e)
Chybmioons Apo Base ,
Esc

VLDL Apo Bioo ,

C- ,C

In Apopaoo ,

LDL Apo Bioo

HDL Apo A ,
E ,C

Functions
of Apo proteins

}
ApoBA8
Apo Bioo interaction
of lipoprotein c-
Receptor
Apo E

Apoc > Activation

of LPL (lipoprotein lipase
Apo A > Activation of LCAT ( lecithin chd .

Acyltransferase)
LIPID METABOLISM

Synthesis of cholesterol
•
AÑgAf+ Acetyl GA

Auto
acetyl CoA

acetyl bA→ v
* *
1 RLE
HMGGA
HMGCoAReductase_mm)
&
inhibits @ 0A)
Statin
i
Mevalonate

↳ renoid Units

Squalene

Chibstrd
cholesterol
degradation of :

CHOLESTEROL

?D
' >

Steroid hormones Vit Bile Acids

Synthesis of F. A :
cytosol

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
*

B- oxidation Mitochondrial Matrix

proper
a. -

I. ACTIVATION :
cytosol
FACPALMATICAUD : 164¥
-
c -
c -
c - c -
c -
COOH

LATP
>
Acyl CoA Synthase
v

-
Acyllott
C- C- C- C- c- CoA

II. TRANSPORT : Carnitine Shuttle

"%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
FADH2 <

Delta 2 trans CoA

enoyl
Hao >
Hydration
V

B- Hydroxy Acyl CoA

NADT
Oxidation
NADH + Htc
v

B- keto
Acyl CoA

Cleavage
' >

Acyl CoA
Acetyl(CoA
2C)

ENERGETICS 8

Dalmatic Acid @ c)
gain of
Net ATP : 106
 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 Acetyl CoA +
Acetyl CoA

i. VK.rs : acetoacetate
D. location : liver Mitochondria
D. K B. cannot be utilized
✓

Acetoacetyllott
.

LIVER & RBC

by .

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

Nucleotide STPTNB Nucleoside STNB

O O

NB
P ← NB
g s •
 NB nucleoside nucleotide
NBTS NBTSTP
adenine Adenosine AMRADP, ATP
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

Righthanded helix left handed helix

•
•

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 : -

rely charged : dlt Poof gp .

Histone : +
rely charged : A
Arginine Lysine
&
MOLECULAR BIOLOGY
Central Dogma of Molecular
DNA Replication DNA
biology DNA
polymerase
Transcript
"

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

}
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
* Helicases : uncoil helix
Nick 's
*
Topoisomerase
I
: relax
supercool by Seating
DNA A
-

T I -

✓
T -

I DNA
gyrase SSB 's

UNM Helicases > ÑÑ

Bag
<

3
Topoisomerase
 '

Reading
'

3 → 5

DNA
polymerase III.
-

New Strand 5
'
> 3
'

RNA Primer
•

LEADING : towards replied" fork

%
-

'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 :

from optical fork

-
"

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
-

DNAP B : DNA repair

-

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

nucleus
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 '

forms hairpin /bend

TATA RNA

TO to -80
-

sequence
CAAT Box
CAAT
 RNA POLYMERASE :

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
codon combination 3 nucleotides
def : is a
Acid
of e codes

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

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

1. Universal
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

50s 30s 60s 40s

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 : .

1. r -

RNA (most abundant)¥

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
•

function off
-
RNA : transfer of Amino Acid

a
DNA
Met ACA)

to V

m -
RNA

}
A&É< m -
RNA

TRANSLATION :
DNA

^
50s

¥70s 30s

m - RNA

peptidyl transferase
(peptide bond)
f
>

EÉ"
mjpnaiti "Yi ¥ É '

ai
m -
RNA

3¥
 Initiation
Elongation Termination

m -
⑤gf *
RNA i
s
'

30s

-^**
Met

m-RM-itigi -i gby.iq?dirandoeat
50%3
"

①
' '
5 3

30s

"^^?⃝
"" •

^^

50h3 §
m-rnn-i-iiaiiiiii.cn? UAAIUAG /UGA
111

30¢
' '
5 3

3
a- will continue till stop codon
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.
.

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)

Lipid Soluble Water sdube

ADEK Vit B complex-

vt c -

Vit A
-

Retinol Gttcohd)
chemistry ii. OH
-

2. Retinal -01+0
Aldehyde)
3.
Patino :c acid coat
-

( carboxylic Acid)

Good source : Beaudine digestion > 2. Retinal

vita Vita
pro
-

Best source : Hdlibut Fish liver oil .

Funtime : i. Vision Rhodopsin ( opsin +11 Cis Retinal)

-

Epithelium Gandhi & differentiate

"
a.

3.
Reproduction
Oxidant
Germ Cells >
Sperm
a. Anti -
deficiency diseases
1.
Nyctalopia
2.
Xeropthahnia
3. Keratomalacia
a.
dry rough & scaly
,
skin
5
Infertility
Vit - D

Vit Di Calciferol
2 Ergocalciferol
3 Cholecalciferol .

Synthesis & Activation

liver of vittles =
Akin
kidney
- -

= i
hunkering
7-
dehydsodobsterd
v.v
rays
cholecalciferol

•÷m①
-
OH →
25 hydroxylase
25
hydroxy
-

cholecalciferol
picot 25 Hit
-

actircatn
of Vitas >
1- ✗
hydroxylase
-

OH >

1,25 dittcc Vit Dos Cakitriol (active form)

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 :
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
(transaminases)

i. VitB , Biotin i.
Pyruvate carboxylase Allopecia
Biotin 2 .

PropionylCoA "

Vit H
Acxtyl CoA
"
-

3.

mcc >
Bqv Consumption of
Raw Eggs

Egg While
}

Bio-%{hnw)
" "

AVIDIN
+

3
Excreted
 Vit Bis
8.

Cobalamin
Vit Biz
"
i. MMT
MMC mutase
•

Mlgaloblastio
Anemia

•
Peripheral neuropathy
9. Vit Bq
Fdicidcid
food
DHF

1. } folate Titan
'

folic acid > > Diff > THF DNA and RNA
,
111-2 H2

{→
Jejunum
did :
Megaloblastic
NTD
Anemia
's
Vit .
C

functions : i. Posttranslational modification of collagen

a.
Absorption of Irun
3. Anti oxidant
-
.

dd :
scurvy
Note : Antioxidant
{
A C C-
I
most
potent
 NUCLEOTIDE metabolism
double
ring
•
Purine
Ring
CO2

i
> Glycine
6 Mt ?
Aspartate µ ? '

is THF
-

, ,
gas
① I
1
Trip ,
Yes
,
,
am
NÑ a

Glutamine

synthesis of Purine

Synthesis Salvage Pathway

< •
Denaro

H&¥Ribose 5- P

IÑP
AMÑ
>

Gmp
 IMP ? Inosine Monophosphate
P
th

De Novo Ribose
•

synthesis .
5- P

ATP
PRPP
synthase
AMP <

Phosphorihosyl
Pysophoshateprpp)
Amidotransfoau
Glutamine
N

Phosphoribosyl
Amine
v
Ni Aspartate
f Caco -
THF

I NzNs -

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

4C Lesch
Nyhan Synd .

eny
.

def : HGPRT

elf :
Neurological
GOUT
deficit
self Mutilation
 Degradation of Purines :

AMP GMP IMP

:
HYPOXANTHINE
Allopurinol
-0
xanthine oxide <

Xainthine
Xanthine Oxide

*
End
product : ÑRK ACID

Pseudo Gout
CK GOUT 3

3 c-
crystals ? ?
hypomania
•

MSU
crystals
°

}
needle
shape Gouty
Arteritis

Rx : Acute GOUT : NSAIDs

Chronic Gout : Allopurinol
 ENZYMES
A
def : velocity of Reaction
nature ? Protein t Won Protein
3 3
Apoenzyme co -

/
enzyme
Co
factor/
-

Prosthetic
group
.

Factors ?

EA
p
i. Conan
of E ✗ V s >

in .
Conan of s ✗ v

* Conon of Port Bell

shape graph
4. Temp .

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
Vms
-

(4
-
- -

,
-

i pin

i.
1

Is]
-
Enzyme inhibition
Competitive : Vmax same Kmt
g. Reversible Non-competitive Vmaxlv
-

knnsame
2. Irreversible

Isoenzymes ok -3

: LDH -5 Ck mm : skomsl
eg
-
.

}
↳ Hi OR BB
Heart
-
:
Brain
LDHZ
* MB Heart
CK
Brain RBC
spleen
:
LDH }
.
-

LDH
LDHstgsk.ms
a
.
 Haemoglobin :

Non protein protein

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

conjugation MATEY Ctfeutiliged)

°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 .