01 Leave Feedba<

BIOCHEMISTRY OF FED STATE

Fed state/absorptive phase

• Also called as post prandial state.
• Starts within a-4 hours o? ?ood intake.
Digestion absorption o? ?ood tahes place.
Plasma level o? glucose, amino acids, Vatty acids triacyl
glycerol level increases.
Chylomicrons which carry triacyl glycerol also increases.

Insulin secretion oo:Q2:45

Hormone o? Ved state '• Insulin.

Insulin starts -to rise when blood glucose level > 3.9 mmol/ L or
TO mg/dl.
glucose is transported to beta cells o? pancreas through
G4-UT a transporter.
etluT a *• Low aWnity transporter.
Once inside the beta cells :
fucose
<3lucohinase
glucose (o phosphate

Pyruvate > ATP

ATP/ADP ratio increases which results in closure o? ATP

sensitive K channels.
Resulting in depolarisation o? membrane.
Opening o? voltage gated calcium channels opens, resulting in
Caa* in^ux.
Calcium stimulate secretory vesicles carrying insulin, resulting
in its secretion.
space
C peptide is co-secreted along with insulin. Active

Biochemistry • v4.0 • Marrow 6.0 • 2022

 Biochemistry of
fed state

M1 T
Tyrosine Kinase
(Seta subunit)

receptor substrate

T Protein f hene I tnzyme 1 Cell growth

translocation transcription activity
1
T U-uT 4
1
€,lucoKmase
1
Phosphodiesterase
T tosuim receptor phosphatase

Liver in fed state oo:14:58

glucose enters liver through ^LUT a transporter.

Gilut a J Lou) aWmity transporter,

tjucose

—* eiycogen
v
synthesis
glucose » h~<o-P ump shunt

eiycdysis
J J
I A
*
Pyruvate
MAOPH

I TCP
Acetyl CoA Cycle
FA synthesis

Lipcgenesrs

vux

Amino acids enter into liver and undergoes : £

$
• Protein synthesis (major portion).
• Oxidative deamination.
• Carbon skeleton enter ing into anabolic Vote.

Biochemistry • v4.0 • Marrow 6.0 • 2022

 Q4 Biochemistry of
fed state Leave Feedba<

drain depends on oxidative pathways.

^lut I
glucose —>— ejut 3 — jocose glucose (o phosphate

pyruvate

Acetyl coA

atp<

TCA cycle

Metabolic fuels : Fed state 00:26:42

Oryan metabolic Vuel

drain glucose
Liver glucose »> Free Vat-t^ acids
Skeletal muscle glucose » Free Vabtu acids
£dC glucose

Adipose -tissue glucose » Free Vatty acids

Heart glucose « Free VaHy acids
(low qli^colytic activi-tvp

• most oryans depends on ylucose.

• R6C brain solely depend on ylucose.

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 BiochemisfrY gf
02 Fasting state Leave Feedbac

Only source = TAQ gets converted into FA + glycerol

Prolonged starvation : Metabolic changes 00:10:52

more -than S days without Vood intahe, all TQA stores are
depleted, Vatty acids are low.
hetone body synthesis = Decreasing.
muscle proteolysis -* Cachexia.

mechanism o¥ action o? glucagon and epinephrine :

glucagon is secreted when blood glucose level is <SO mg/dl.

I
I

Enzymes are active in phosphorylated state, p^^horyiated

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 Biocherm
02 Fasting si te Leave Feedba

testing skeletal muscle :

quuT is 6iLUT-4.
But cannot act in lasting state.
Rmino acid transported as alanine.

Brain :
a QLUTS : 6<mT I, <dmT 3 (neurons).
KB can only provide ao44 energy.
Prolonged starvation * Brain depends on hB.

Biochemistry • v4.0 • Marrow 6.0 • 2022

 03 Leave Feedbai

CONCEPT OF ENZYME REGULATION

Hormonal regulation.
Allosteric regulation.

Hormonal regulation OO:O1:18

Well Ved/absorptive/post prandial state -* Insulin.

High insulin glucagon ratio.
Fasting state -* glucagon.
Lou) insulin glucagon ratio.

Action o? glucagon •
glucagon binds to Q protein coupled receptor.

Activates Q protein.

Activates adenylyl cyclase.

ATP cAmP

Activates cAmP dependent protein Kinase A.

ATP

ADP
Enzyme enzyme.

Action o? insulin s
• Activation o¥ phospho diesterase =
Converts cAmP to s’ Amp.
Insulin reduces cAmP level
• Converts enzyme into dephosphorylated state. space
Active

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 04
Leave Feedbac

INTRODUCTION TO ENZYMES

Introduction 00:01:50

De^nition : Enzymes are specialised proteins that act as

catalyst in biological reactions.
In I8SO, Louis Pasteur discovered that Sugar can be converted
to alcohol. This process is Known as Vermentation. He termed
the liKely vitalism that catalyses this rection as Verments.

In 1891, Edward Buchner discovered that cell Vrec yeast extract

could catalyse Vermentation.

Freder icK u) Kuhne coined the word enzyme which is derived

Vrom QreeK word enzymos meaning leavened.

Types of enzymes 00:05:19

Simple enzyme :
• Only amino acid residues taKe part in the reaction.

Complex enzyme ;
• Amino acid residue + Chemical component is required Vor
the reaction to occur.
• Amino acid component is Known as apoenzyme.
• Hon enzyme component can be :
Inorganic molecule liKe metals : Fe^/Fe1*, Cuf*, Zna* -*
Co-Vactor.
Organic component liKe organic molecule or metallo-
organic molecule -* Co-enzyme.

5
I

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 04 Introduction to
Enzymes Leave Feedba*

Vitamin 6IA Adenosyl ftia • TransVer o? alhyl groups/

(Cobalamin/ methyl eia H atom
cobamide
enzymes)
Lipoate • Oxidative decarboxylation
as part o? muRienzyme
complexes liKe pyruvate
dehydrogenase,
alpha-heto glutarate
dehydrogenase,
branched chain Keto
acid dehydrogenase

Vitamin C Ascorbate • Hydroxylation reactions

Cofactor 00:21:04

metals as co-?actor ;
metalloenzyme ’•
metal is tghtiy integrated by covalent or non-covalent bonds
to the apoenzyme.
&g. : 2n in carbonic anhydrase.
Cu in tyrosinase.

metal activated enzyme =

metal is not an integral part o? the apoenzyme, but its presence
is required in the surroundings Vor the enzyme to act.
Eg., Lipase requires presence o? Caa’ to act.

Prosthetic group 00:23:58

Chemical component (coenzymes/coVactor) uuhich is tightly

integrated to the apoenzyme by covalent bonds or
non-covalent bonds.

Holoenzyme : Apoenzyme + Chemical component (coenzyme/

co?actor).

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 Q4 IntroducUomo
Enzyme^! Leave Feedbai

Copper (Cua0 • Tyrosnase ‘ Cua* deficiency causes

hypopgmentation as tyrosine required for
melanin production
• Complex IV of ETC Cyt C oxidase = Energy depletion
m CuJ' deficiency.
• Lysyl oxidase ; Required for covalent crosslinhirg
of collagen : menhe rsinhy disease/ Steely hair
syndrome.
• Cytoplasmic Superoxide dismutase.
Michel • urease
Calcium • Lecithinase
• Lipase

Clinical problems 00:40:17

Vitamin deficiency (coenzyme) «

• Energy depletion • Coenzymes are part of oxidoreduetion
reactions which result in formation of reducing
equivalents that goe into electron transport chain for
generation of PTP. Coenzyme deficiency hence causes
energy depletion.
• Collagen depletion : Vitamin C acts as coenzyme of
hydroxylation of lysine and proline which is required for
collage synthesis.
Vitamin C deficiency can cause scurvy.
• Enzyme defect ; PlP defect can halt homocysteine
metabolism.

mineral deficiency (cofactor) «

• Hypopgmentation (Cua" deficiency).
• Oxidative stress • minerals are required for free radical
scavergmgj deficiency of minerals can cause oxidative
stress that leads to atherosclerosis, cancers etc.,
• Collagen defect : Cua* required for lysyl oxidase needed 5
&
for covalent crosslinhing. ?
• Vision : Zinc is cofactor for retinol dehydrogenase, which I
is involved m mold’s visual cycle.

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 05 Classification of
Enzymes Leave Feedba

MADP s

Substate
MADP+ MADPH + H*
an* + ae'

• fucose (o phosphate dehydrogenase.

• (o Phosphogluconate dehydrogenase.
• Cytoplasmic isocitrate dehydrogenase.
• malic enzymes.
Flavoprotein feiboWovin);
Substate
FAD FADH.
an* + ae'

Succinate dehydrogenase (Complex l\).

Acyl CoA dehydrogenase,
mitochondrial glycerol 3 phosphate
dehydrogenase.
J. Oxygenase :

Add oxygen directly to the substrate

’
aa. monooxygenase / mixed function oxidase : Add I atom
o? oxygen.
Hydroxylase •
AH + Oa + ZHa AOH + H O t 2

Tryptophan Hydroxylase. ~
Aromatic amino
Tyrosine Hydroxylase.
acid Hydroxylase.
Phenylalanine Hydroxylase—
1- Hydroxylase. I
Cytochromes
Cytochrome P45O and Cytochrome bS are involved in
modifying and degrading drugs.

Biochemistry • v4.0 • Marrow 6.0 • 2022

 05 Classification of
Enzyme Leave Feedba

4a. Peroxidase •

Electron acceptors *
• Ascorbate
Free radical
• Quinones.

• glutathione.
>- scavenging
• Cytochrome C.

Ha°a + ^Ha > SH^ * R'

E.g. : glutathione peroxidase : a Selenium containing

enzyme.
It is present in erythrocytes and other tissue.

4b. Catalase
’
Electron acceptor ; I molecule of H Oa.

AH O AH O + O .

present in Peroxisomes of :
Catalase is
mucous membrane, Kidney, Liver, Blood, Bone marrow.
Peroxisomes containing s
Catalases scavenge reactive oxygen species.
Oxidases generate reactive oxygen species.

S. Reductases =
They require MADPH.
Are involved in the reductive biosynthesis of steroids, Fatty
acids, and Cholesterol.

Class II - Transferase 00:29:37

Transfer the functional group/ moieties liKe methyl, and

amino groups, Example :
• Any enzyme with TRAMS in its name : Transaminase,
s
transhetolase, transaldolase, transmethylase. I
• Any enzyme that trasfer phosphoryl groups - Kinases.
Donor is ATP : Hexohinase, phosphof ructoKinase
Donor is inorganic phosphate phosphorylase
’

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 05 Classification of
Enzymes Leave Feedbai

Other hydrolases:
Arginase.
Phosphatases.
glucose - (o - Phosphatase
glucose -(o-PO4 Qlucose

HO Pi

Fructose-i,fa Fruetose-I,(o 6is Phosphatase Fructose (o

6isP0 phosphate.
HO Pi

Class IV : Lyases. 00:41:10

Cleavage o? covalent bonds lihe O-O, C-N, and 0-0 without

adding water, by atom elimination and forming a double
bond or adding groups to double bond.
Any enzyme with Lyase in the name:
i. Hme^ Co- A lyase.
J. Arginosuccinate lyase.
3. ATP citrate lyase.

Aldolase :

Fructose
(oC
- I, - bis PO4
(o glyceraldehyde- 3 PO4 + DHAP
3C
- 3C

ftreah / mahe double bond by atom elimination.

enolase :
O O"
HO
O O

H— O— OPOV
enolase
C — 0P0f
HO — OH OH.

a-Phosphoglycerate Phosphoenolpyruvate
= is Kj/mol

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 05 Classification of
Enzymes Leave Feedba*

These dehydrogenase enzymes are multienzyme

complexes require S coenzymes :
• TPP / Thiamine pyrophosphate (vit Gp.
• K1AD+ / Vit
• FAD / v* e>ia.
• Lipoate.
• coA/v*e>s.

Class V - Isomerase 00: 51:45

Catalyze structural and geometric isomers.

Any enzyme with isomerase in its name.
Phosphohexose
glucose - (o-
PO4 <
isomerase
> Fructose - - POA
(o

, , ,
-3 -
_ Phosphotriose
isomerase
Glyceraldehyde POA < > DHAP.

Qacemase :

D glucose < > l Glucose.

D Alanine < > L Alanine.

mutase :
Intramolecular transfer o? groups 5

Phosphoglucomutase
Glucose - G - PO4 < > Glucose - I - POA.
Phosphoglycerate
mutase
3 Phosphoglycerate < phosphoglycerate

Class VI - Ligase 00:56:25

Joins a molecules coupled with the hydrolysis o? ATP.

I. Carboxylase.

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 05 Classification of
Enzymes Leave Feedba,

Q) Identify the enzyme involved

I. glucose -G-P04 glucose.
nao Pi

Answer: glucose - - Phosphatase.

(o

HaO is added and inorganic Phosphate is removed

Anexample o? Hydrolase is Phosphatase.
Adding substrate to the name: glucose (o - - Phosphatase.

a. glucose - <o - PO < Fructose - G - PO4.

Answer: Phosphohexose isomerase.
glucose and Fructose are isomersj hence enzyme is
isomerase.
Both are hexose phosphates.

3. glucose - - POA
(o
* glucose - - POA.
l

Answer: Phosphoglucomutase.
A type o? isomerase: mutase.
The substrate is glucose phosphate.

4.
MAD* MADH
Acetul CoA
Pyruvate (ac).
Cao)
CDa
Answer: Pyruvate dehydrogenase.
In these reactions: MAD* -* MADH: hence the enzyme is
dehydrogenase.
The substrate is Pyruvate.

ATP ADP
Pyruvate । Oxaloacetate
(3C) Biotin (4C).
CO,

Answer: Pyruvate carboxylase.

Biochemistry • v4.0 • Marrow 6.0 • 2022

 06 Lea'

MECHANISM OF ACTION OF
ENZYMES

Active site 00:01:08

The reaction is not occurring in the entire enzyme, it tabes

part only in certain site called active site.

Activation energy :
The d^Serence between the Vree energy o¥ substrate and
the transition state.
The standard Vree energy change : Ae^
space
A^- Ae^- A^ Active
bibb’s Vree energy • Q

Biochemistry • v4.0 • Marrow 6.0 • 2022

 06

Energy barriers Enzymes

I. Entropy (disorderly) of system. deduce the entropy.
SLSolvation shell of hydrogen Desolvation of the substrate.
bonded water around the
substrate

3. Improper algnment of reactive Proper alignment of reactive

groups, Enzyme to the groups in the active site to the
substrate substrate.

Proper alignment of reactive groups in the active site to the

substrate It’s explained bg various theories.

Various theories 00:28:30

I. emil Fischer’s template theory/ Loch and Key model ’

Fixed shape for the active site, so that substrate
with complementary shape can bind to the active
site of the enzyme.
a. UJilViam JenK and Linus Pauling theory »
Active site o? the enzyme complementary to the
is
transition state so that more products are formed.
3. Induced $t theory: by Daniel Koshland 09SQ).
Enzymes undergo conformational change when
substrate binds to the active site, which is induced
by multiple weaK interaction between substrate and
active site.

Mechanisms by which the reaction takes place oo:36:15

Catalysis by proximity.
Acid base catalysis.
Covalent catalysis,
metal ion catalysis. §

Catalysis by strain. I
I. Catalysis by proximity :
• For the reaction to occur, the reactant should come in
bond forming distance with the active site.

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 qq
07 Leave Feedbac

ENZYME KINETICS

Enzyme kinetics 00:01:20

Deals with a things.

Rate o¥ reaction. Factors that oMect the rate o?

enzyme catalyzed reaction.
Rate o? reaction •

rI
< r
a >
A +6 P + Q.

h= Rate constant o?
r a caJ ce>l r = h CA1 L61 forward reaction.
ra a CPJ Cql ra = ha CP1 CQl ha = Rate constant oV
backward reaction.

At equilibrium, it is a dynamic state where forward and

backward reaction tabes place, at the same rate.

h CAM = ha CPXql

(Equilibrium constant).

hl CPXqJ
CAM)'

tStQ = Concentration o? products / Concentration o? substrates.

I

• Enzymes don’t alter equilibrium constant (beep. space

• Enzymes lower activation energy. Active
• Enzymes don’t alter Vree energy state CAe<ol

Ae^° = -RT log (R : Qas constant. T : Absolute temperature).

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 07 Enzyme Kinetics
Leave Feedbac

• Unique Vor on enzyme substrate pair.

fca. : Km value o? qlucose hexohinase diners Vrom K
sJ nJ
value o? Vructose hexohmase.
“Signature” o? an enzyme substrate pair.
Higher the K^ Lower is the aV^inity o? the enzyme
towards the substrate.
Kml/a Aridity.
A^initu \/a Cs] -* Km a CSl i/v - variable ‘y’
VmaxXCSJ I _ Km + CSJ
_____ K^/ vmax - ‘a’
Vi = l/CsJ - Constant
Km+CsJ Vi Vmax CSJ
-
1/ vmax constant
I
Vi
Km
— I
= Vmax X LSJ- + Vmax
I z
w
'
- Initial

At x intersect, y =O
V = ax + b

Alternatives to LB plot 00:29:00

Single reciprocal plot : CSJ

Vi
a? Eadie -HoVstee plot,
b) Hanes-uJoolV plot.
CSJ
CSJ
Catalytic constant (AKA Turnover number) :
K^ : measure o? eWiciency o? a homogenous mixture o?
enzyme.

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 Qy Enzyme inetics Leave Feedbac

maximum stability : 45° to S5° C

Temperature Co-eWicient (Q^ s

Every 10° rise in temperature : Eate o? reaction is doubled.
qo = a
Eate o? reaction is doubled because :
• Increased Kinetic energy.
• Increased Collision frequency.
v

“7K / \ Bell shaped curve

Enzymes are denatured

J V
Optimum temperature
Temperature
H+ ion concentration 00:55:07

Optimum pH Mormal : 5 to 9.
Charged state o¥ Amino acid residues var ies with pH.
pn4 : ionization constant. pH = “Charge o? ionizable group varies’.

Aspartate protease -* pepsin

Active in acidic pH.
Aspartate pK^ = a.

Intestine
Chymotrypsin : Catalytic residue : Histidine (pKa = b, active in
alhaline pH).

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 QQ
08
Leave Feedba*

ENZYME INHIBITION

Enzyme inhibition 00:02:44

fill cellular processes need enzymes. Control o? these processes

can be done Via an enzyme inhibitor.
Types :
Reversible inhibition :
• Competitive inhibition.
• uncompetitive inhibition.
• mixed inhibition.
Irreversible inhibition
* Suicide inhibition.
• Transition state analogues.
Mon-competitive inhibition can be both reversible and
irreversible.

Competitive inhibition 00:05:24

It is a type o? inhibition in which the inhibitor is a structural

analogue o? the substrate and hence it competes with the
substrate ¥or binding to the active site.

& + s <-» es -* &+p

& + I (inhibitor) -* enzyme - Inhibitor Complex.

Properties o? competitive inhibition 5 space

• Inhibitor is a structural analogue o? the substrate. Active
• Addition o? excess substrate can replace the inhibitor
?rom the active site.

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 08 Enzyme
Inhibition Leave Feedbai

Ans. Poison was found to be malathion, an organophosphate,

malathion
I
malaxone
I
Inhibits Ach esterase (competitive inhibition)
I
Acetyl choline • Acetate + choline
I
Accumulates in nervous system
I
Stimulates autonomic nervous system
I
Symptoms lihe vomiting, sweating, increased muscle twitching

Initially, the inhibition o? Ach esterase by malaxone is reversible,

but as the dose of organophosphate increases; the inhibition
becomes irreversible.

Case scenar io
In Hooch tragedy, many people were hospitalised, ethanol was
given as an antidote. Why?
Ans. methanol was ingested in hooch tragedy.

Alcohol dehudroaenase
methanol •
Formaldehyde > Blindness.
Ethanolcompetitively inhibits the enzyme alcohol
dehydrogenase and forms acetaldehyde which is relatively
less toxic.
Excess ethanol replaces methanol from active binding site
and prevents formation of toxic formaldehyde.

Non-competitive inhibition 00:19:31

8
Substrate
Another Site i i I
Substrate
Inhibitor e-S-i Complex

The inhibitor is not a structural analogue o? the substrate.

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 08 Enzyme
Inhibition Leave Feedbac

Uncompetitive inhibition 00:28:03

The inhibitor has no aWinrty towards Vree enzyme but it binds

to the enzyme-substrate complex.

Shape : Parallel.
x-intercept moves away Vrom zero.
'/-intercept increases.
&.g., Placental ALP inhibited by phenylalanine.

Case scenario =
Following a short circuit, a house was on ftre at night. In the
morning all the family members were Sound dead but none o¥
the bodies were charred, uohat is the reason behind the death
o¥ the all the family members Vollowirg a ftre?
Ans. Fire Increased carbon monoxide emission.

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 Qg Enzyme
Inhibition Leave Feedbai

Suicide inhibition 00:47:54

The inhibitor is unreoctive, it hijocKs toe mechanism o? toe

enzyme to convert itsel? into a more reactive compound. This
compound binds to the active site o? enzyme irreversibly.
Also Known as mechanism based inhibition.

Examples :
• Allopurinol used Vor treatment o? gout inhibits xanthine
oxidase.
Xanthine
oxidase xO
Hypoxanthine —> xanthine > uric acid
Irreversible
inhibition
Allopurinol —^2 > Alloxanthine

Aspir in inhibits cyclooxygenase.

Di^uoro methyl ornithine inhibits ornithine decarboxylase.
It is used in toe treatment o? trypanosomiasis.

'Transition state analogue 00:51:58

Substrate Transition state Product

Structural
analogue (Drugs)
Substrates gets converted into a transition state before
forming toe end product.
The active site o? the enzyme is complementary to this
transition state o? toe substrate.
Drugs have been developed which are structural analogues oV
transition state o? substrates.

E.g. Penicillin is a structural analogue ?or toe enzyme

transpeptidase which is required ¥or cell wall synthesis o?
bacteria.

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 09 Leave Feedbac

ENZYME REGULATION

In I9th century, Claude Bemarde put forward the concept o?

enzume reaulation.
Regulation

enzyme Quantity (long terrri) enzyme Quality/irrtrmsic

• Control o? enzyme synthesis
(induction and repression), • Allosteric regulation
ey. Cholesterol synthesis, • Covalent modiftcation
urea, cycle etc.
• Control o? enzyme degradation

Control of enzyme synthesis 00:03:50

Also Known as induction and repression.

b.g. i) cholesterol synthesis :
more cholesterol in diet
j depresses
<dene Vor nm€\ CoA reductase (rate limiting enzyme)

a) Heme synthesis t
Succinyl CoA + glycine
| ALA synthase
d ALA
I
Heme.
Increased heme will repress ALA synthase whereas decreased
amount o? heme will activate the enzyme.

Q. Phenobarbitone induces heme synthesis and aggravates

porphyria. LOhy?
Ans. Phenobarbitone gets metabolised with the help o? space
cytochromes, which are heme containing proteins.
Lbhen cytochromes get used up, amount o? heme decreases
Active
and in turn induces ALA synthase. This causes accumulation
o? porphyrins (intermediate), which aggravates porphyria.

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 qq Enzyme AQ
Leave Feedbac

Allosteric activation Positive modifier (m+) binds to an allosteric

site and maKes favourable conformational charges in the
catalytic site, enabling binding of substrate to the active site.
Alloster ic inhibition : Megative modifier (m-) binds -to an allosteric
site and maKes unfavourable conformational changes in the
catalytic site, which inhibits bindirg of substrate to the active
site.

inhibition
Activation

Features of allosteric enzymes ( Correlate with hemoglobin) '•

• most allosteric enzymes are multi-subunit enzyme.
• They possess a quaternary structure.
• The modifier need not be a structural analogue of the
substrate.
• Substrate saturation curve is a sigmoid curve.

Follows a sigmoid Kinetics as it exhibits cooperative

binding.
bndirg of one substrate favour binding of other
substrates to the same enzyme. 5
&
Does not follow michaelis-menten hyperbolic Kinetics. s
(uJhich result in a hyperbolic curve). I

Biochemistry • v4.0 • Marrow 6.0 • 2022

 09 Enzyme
Regulatd
Types:
Irreversible Partial proteolysis (zymogen activation).
’
• Trypsinogen -* Trypsin.
6y chemically cleaving polypeptide chain.
• Chymotrypsinogen -* Chymotrypsin.
• In blood coagulation, fibrinogen -* Fibrin.
Reversible :
• Phosphorylation de-phosphorylation (most versatile).
• Acetylation.
• methylation.
• ADP ribosylation.
• ubiquitin addition.
most common site Vor phosphorylation : OH group-containing
amino acids (serine, threonine, and tyrosine).
ATP ADP

Protein hinose

£ - Ser - OH - O - PO^
Protein phosphatase
H o
Pi'

In process o? glycogen degradation $

ejycogen phosphorylase degrades glycogen in its active
phosphorylated state.
Insulin (Ved state)
glucagon (lasting state)
glucagon glycogen Insulin

Protein
Kinase A
Protein
Phosphatase
—
< space
Active
glycogen phosphorylase a
(Active)
-
Qlycogen degraded

Biochemistry • v4.0 • Marrow 6.0 • 2022

 Enzyme
09 Regulati

Q.The substrate saturation curve given below characterises

an allosteric enzyme system. uJhich o? the Vollowing statement
is true?

A. Allosteric modifter binds in a concentration dependant

manner :
False, binding is not based on concentration.
6. modifier can aV^ect catalytic site by binding to allosteric
site :
True.
C. Adding more substrate can displace the mod&er ;
False, because they are not structural analogues.
D. Allosteric modder charges binding constant not vmax
False, as allosteric enzyme can belong to h series or V
series where hos or can vary respectively.

Compartmentation 00:50:22

Certain pathways tahe place exclusively cytoplasm or

in
mitochondria, or both. This mechanism provides a saVe space
Vor certain reactions.
&.g., Fatty acid synthesis -* Cytoplasm.
Fatty acid degradation -* mitochondria

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 Clinical
Enzymology Leave Feedbac

used as diagnostic biomarKers.

• Helps to And the location o? the disease.
• Rejects the nature and sever th o? the disease
e.g. : A reversible inflammation in the cells increases cell
membrane permeability, and the cytoplasmic enzymes
are seen in blood

In irreversible cell injury and necrosis, mitochondrial

membrane permeability is also increased, such that
mitochondrial enzymes are also seen in blood

Lactate dehydrogenase 00:10:20

LacWe dehudroqenase
J
Pyruvate Lactate.
Location -* Cytoplasm.
Structure Tetramer with two types o? subunits H and m.
Cased on the subunits, diVflerent isoenzymes are seen.

isoenzyme Subunits mobility at Tissues o? origin fl in serum

pH 8.(0
LOH- I. H4 Fastest Heart muscle 30

LOH- a. hm
% ।
Faster K6C, Kidney 3S

LOH- a. hm
a a
Fast Spleen, lungs, ao
lymph node,
leucocyte, platelet.
LOH- 4. wm
i %
SIOU) Liver, sKeletal 10
muscle (loh- 4
predominant).
LOH- S. m4 Slowest Liver, sKeletal s
muscle

LD- (o -* Seen in severely ill patents.

ldx/ LDC -* Seen in post-pubertal testes.
Clood analysis gives the total amount o? LDH activity. To Know
!
the speciflc isoVorms, electrophoresis is done.
I

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 Clinical Leave Feedbacl
Q
Enzymology

• Giamma ALP :
Seen in mucosa o? intestinal cells.
elevated in ulcerative colitis.
Cleared by sinusoidal cells o? liver.
In case o? hepatitis, it will be elevated

marher o? leucocyte disorders lihe leuhemia

Heyan isoenzyme 5
Also called carcino-placental enzyme.
Similar to placental ALP.
G^erm cell origin.
De-repressed in conditions o? malignant tumors.
Magao isoenzyme, Seen in malignant tumors.
hasahara isoenzyme.

Cardiac Biomarkers 00:30:36

liise when there is injury to heart.

Enzymes and non-enzymatic compounds.

Mame Rise PeaK Return to base line

CH- me> 4- 8 hours 34 hours 48- 73 hours

Troponin T 4-(o hours 34 hours 7- IO days

Troponin 1 4-(o hours 34 hours 7- 10 days

LOH 34 hours 3- <o days 3 weehs

AST 13 hours 48 hours 4- S days

ldh and AST are not clinically used.

Cardiac troponins are more specie than Ch- me>.

First biomarher to rise -* myoglobin (a hours) -* Mon specie
High sensitivity monoclonal Ab based assay :
Detects < I rg/L o¥ troponins.

Flipped ldh pattern ; a

In normal individual -* LDH-a > LDH- I.
In ml LDH-I > LDH-a.

Biochemistry • v4.0 • Marrow 6.0 • 2022

 1Q Clinical
Enzymo Leave Feedbai
.
From the previous fable.
ALT is more specie for liver injury.
(very high values only for liver injury)
AST has very high values for heart, liver, sKeletal muscle,
Kidney and pancreatic injuries- non-speci^c.
ALT is exclusively intra-cytoplasmic.
AST is located in cytoplasm and mitochondria.

AST : ALT ratio (ARE) =

ARIS. < I s rise in ALT > liise in AST.
• Chronic viral hepatitis.
• Non-alcoholic fatty liver disease.
• Toxic hepatitis.
• Acetaminophen toxicity.
ARG. > I :
• Alcoholic hepatitis.
Damage to mitochondria results in rise of AST levels.
• Hepatic cirrhosis.
AST levels increase as the sinusoidal cells of liver are
injured, and AST is not cleared from the plasma.
• Liver neoplasia.
Aminotransferase level
Ischemic or
toxic liver

Acute injury or inflammation of liver -* mar Ked elevation of 8

transaminases.
I
Chronic conditions -* mild elevation of transaminases.
All liver enzymes within normal limits in an asymptomatic
person, with only mild elevation of ALT -* Fatty liver.

Biochemistry • v4.0 • Marrow 6.0 • 2022

 10 Clinical
Enzymo

Mot a specie marKer (also elevated in osteoclastic

injuries).
Prostate specie antigen :
Also called KalliKrein related peptidase-3 (KLK- 3).
Cut oW -* <4rg/ml.

Enzyme profile in pancreatic disease oo:56:55

Serum Amylase «
Mon- specie as rt is elevated in other intra-abdominal
conditions, salivary gland disorders, genitourinary
disorders lil ? ectopic pregnancy.
Lipase
’
Elevated almost 5000 times.

markers oV bone »
bone formation resorption
bone

Orginates Vrom osteoblasts. Originates ?rom osteoclasts.

• Pre- beta AlP. • M- telopeptide 0? type i collagen.
• Osteocalcin. • O telopeptide 0? type I collagen.
• Pro- peptide 0? type I collagen. • urine Vree deoxypyridinoline.

Movel markers o¥ acute Kidney injury 5

• Kidney injury molecule (him- i).
• Meutrophil gelatin associated lipocalin (mqAl).
• IL- I8.
• ALT.
• glutathione- S- transVerase.

• feeta a
microglobulin.
• Alpha a macroglobulin.
• Retinol binding protein.
• Cystatin C. space
• microalbumin.
• Osteopontin. Active
• Liver Vatty acid binding protein.
• Sodium hydrogen exchange isoVorm.
• Exosomal Vetuin.

Biochemistry • v4.0 •Marrow 6.0 • 2022

 1Q Clinical
Enzymo Leave Feedbac

Best marker is s’ nucleotidase.

Q:A Koyear old female patient was admitted in medical ward

with fever, anorexia, vomiting, generalized weakness and
jaundice. She gives history of recent travel to Bangalore. Acute
viral hepatitis was diagnosed ulhich is the non- functional
enzyme elevated in this case?
A. Allsaline
phosphatase.
6. Alanine aminotransferase.
C. Ramona glutamyl transferase.
D. Creatine Kinase.
&. Lactate dehydrogenase.

Q:A BByear old lady was admitted following a Qoad Traffic

Accident. During her hospital stay an intern in the ward while
going through her case ftle noticed that her serum ALP was
elevated and SKull X-ray showed-Osteoporosis circumscripta,
thicKening of diploic areas and sclerosis of portions of SKull
bones.
Out of his curiosity he sends a blood sample to Biochemistry
lab. ulhich of the following is the BiomarKer he sent?
A. Serum osteocalcin.
ft. ProBMP.
C. AMP.
D. Kim-i.
&. Bxosomal Fetuin-A.

Q. A40year old female with history of inadvertent use

of MSAIDs develop olguria Her serum creatinine and BUM
elevated and Acute Kidney Injury CAKlJ was diagnosed
LOhich of the following are novel marKers of AKI which can
be done in this case? 5
&
A. M terminal pro BMP. ?
6. Clusterin.
I
C. Meutrophil e^elatinase Associated Lipocalin.
D. Cross linKed M-Telopeptide.

Biochemistry • v4.0 • Marrow 6.0 • 2022

In solution, 99% glucose and fructose exists in ring form.
Fructose :

C =0

3I
-C-OH

Straight fcCHOH

Disaccharides 00:15:44

Depending on which carbon atoms are engaged in -the

glycosidic bond formation, they are divided into reducing and
nonreducing disaccharides.
Mon reducing : Functional groups are engaged in linkage, and
no free group present.
Reducing : Free functional group present.
Examples of reducing disaccharides :
Mame monomer units Linkage
maltose glucose + Qlucose at - 4 glgcosidc linkage
Isomaltose glucose + glucose ai - glgcosidic linkage
(o

Lactose galactose + educose Pi - 4 glgcosidic linkage

Lactulose galactose + Fructose

Examples of non-reducing disaccharides :

Mame monomer units Linkage
Sucrose glucose + Fructose ai - pa linkage
Trehalose ejucose + glucose ai -l linkage

Polysaccharides 00:21:34

j:
Homopolysaccharide
1
Heteropolysaccharide
One type of monomer > l type of monomer units.
I
glycogen ; 3
• Storage carbohydrate in humans/animals.
• made of a D glucose.
• Branched polymer.

Biochemistry • v4.0 • Marrow 6.0 • 2022

 Chemistry of

• Favours satiety.
s
Carbohyr— Leave Feedba

• Fibre particularly yums (Venuyreeb) and pectin reduce

post prandial blood ylucose level in the blood
Inulin :
Fructose, Fructosan.
Inulin clearance test ; used to access ylomerular Nitration
test (ideal) but not used now.
Chitin In exosheleton o? crustaceans.
made o? M-acetyI o ylucosamine.

Pectin : Heteropolysaccharide.
Predominantly made o? yalacturonic acid
Dextrin : Hydrolytic product o? starch.
Dextran • Polysaccharide o? a D ylucose.
• used as plasma volume expander.
• Synthetic dextran : Size exclusion chromatoyraphy.
• Dental plaque.
Isomerism in carbohydrates 00:38:34

Isomers are compounds with same molecular formula but

diV^erent structural orqanisation.

Structural isomerism/ Optical isomerism =

Stereoisomerism s
D L isomerism (enantiomers) Dextro or levo rotatory
Anomerism
Epimerism
Asymmetric carbon atom :
4 valencies o¥ carbon atom occupied by 4 d&Serent yroups.

Biochemistry • v4.0 • Marrow 6.0 • 2022

Epimerism 00:53:47

Difference in orientation of H and OH CH ch

group at a single carbon atom other OH H-C-OH
than the functional and penultimate HO— —
C H OH-C-H
carbon atom.
ho-c-h h-c-oh

,H-C-OH
C
L
C
L
OH H— C— OH

I ho—c—h
Ca epimer CH OH CH OH
ho-c-h HO-C-H galactose glucose

H-C-OH mannose : epimer of glucose.

h c OH H C OH galactose : 4* epimer of glucose.
CH OH CH OH
Qlucose mannose

Pilose 3rd epimer of glucose.

Diastereoisomers :
Difference in orientation of H and OH groups in > I carbon
atom other than the functional and penultimate carbon atom,
mannose and galactose are diastereoisomers.

Optical isomerism 00:57:41

Ability to rotate the plane polarised Ight.

Occurs due to asymmetric carbon atom.
• glucose 5 R.ight/clochu)ise direction = Dextrorotation
Cd’ glucose or ‘+1). Hence glucose is Known as dextrose.
-
Fructose : Left/anticlocKwise direction Levorotation
( V glucose or
Sucrose is initially dextrorotatory and after it is hydrolysed,
becomes levorotatory. Hence aKa invert sugar.

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 12
Leave Feedba<

GLYGOSAMINOGYCANS AND
MUCOPOLYSACCHARIDOSES

Introduction 00:00:08

Repeating disaccharide unit.

Also called as Heteropolysaccharide/ mucopolysaccharide
Long unbranched heteropolysaccharide consisting o¥ a
repeating disaccharide unit.

Overall negative charge

Properties o¥ €\A6\S :
• Megatively charged/Polyanions.
• Form hydrogen bond with water.
• Absorb water and Vorm a hydrated gel acting as a
lubricant.
space
I.Compressibility oV cartilage. Active
a. mobility and resilience o? joints.
—
• Occupy large space > molecular seive
• Selective transport o? molecules.

Biochemistry • v4.0 • Marrow 6.0 • 2022

 Glycosamino
r
glycans and
Mucopoly!
Leave Feedba

Heparan SulVate :
• Present in synaptic vesicles.
• Present in the renal basement membrane making it
responsible ?or the charge selectiveness o? the
glomerular basement membrane.
• G^ives a net negative charge to the basement
membrane, therefore doesn’t let negatively charged
Albumin to pass through.
• Anchors lipoprotein Lipase to the endothelial surface.
• Acts as plasma membrane receptor.
Hepar in
• The only intracellular GA€v
• Inj. Heparin dislodges lipoprotein lipase ?rom its
anchoring site.
• Maturally occurring anticoagulant which binds to
Anti-Thrombin III.

Hyaluronic Acid.
• Mot covalently bound to protein.
• Polysaccharide.
• Mo sulVate group.
• Helps in cell migration (mound Repair,
Embryogenesis, morphogenesis, metastasis) .

Proteoglycan Structure 00:21:14

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 Glycosamino
glycans and Leave Feedbai
MucopolysR
• Beaming o? vertebrae.
• Tip o? metacarpal degeneration leading -to
Bullet shaped phalanx.

Hurler’s Disease/ mPS l-H :

• mutation o? IDUA e^ene.
AV^ecting a-L Iduronidase enzyme.

Scheie’s Disease / mPS l-S »

• mutation o? IDUA Qene.
• AVSecting a-L Iduronase enzyme but the enzyme
activity is partially preserved
• Mormal intelligence.
• Presenting age is aVter s years.

Hunter Disease/ mPS II j

• mutation o? IDS €\ene.
• AWecting Iduronate SulVatase enzyme.
• x-Linhed Recessive condition, hence only males are
• aV^ected
• Clear vision. (k!o corneal clouding)
Matouuicz Syndrome/ mPS IX : Affecting Hyaluronidase
enzyme.
Disease enzyme defect mental Comeal
Deficiency Clouding
mPS l-H (Hurler) L Iduronidase Present Present

mPS l-S (Scheie) L Iduronidase Absent Present

mPS II (Hunter) L Iduronate Sulfatase Present Absent

mPS III (Sanfilippo) fenzyme that degrades Present Absent

Heparan Sulfate
mPS IV (morquio) ^alactosamine- Absent Present
(o-Sul?atase,
&eta-€,alactosidase

mPS vi M-Acetyl Qalactosamine- Absent Present

(moroteaux Lamy) 4-Sul?atase

Biochemistry • v4.0 • Marrow 6.0 • 2022

 Glycosamino
glycans and Leave Feedbai
Mucopolysae
Clinical scenario I
A (o year old mentally retarded girl with protuberant abdomen,
Umblicol Hernia, short stature

Answer = mucopolysaccharidoses.
Explanation mental Retardation/ Intellectual disability.
Umbilical Hernia
Short stature.
Comeal Clouding.
Coarse Facial features frontal bossing, depressed nasal
bridge^ macroglossia
Claw hand
All o? which are features o? mPS.

Clinical scenario A :
A IG year old boy with short stature, coarse facial feature,
and nirsuitism and normal intelligence

Answer : Scheie’s Disease

Explanation s Ho year old boy with Short Stature, Hirsuitism,
Normal intelligence, Coarse facial Ventures,
Comeal clouding Abdominal protrusion
Claw hand I? L-lduronidase enzyme is aWected, we can
conclude it to be Scheie’s Disease.

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 13 Leave Feedbai

GLUCOSE TRANSPORTERS

Types of Glucose transporters 00:01.54

Sodium dependent glucose transporters : SQLT.

Sodium independent glucose transporters glut. =
Glucose is a. hydrophilic compound It must be transported
through the hydrophobic plasma, membrane. Hence
Transporter is required

SGLT 00:04:28

Types Location Function

SG\LT-I Intestine Luminal side. Absorption o¥ glucose.
Proximal lienal tubules.

SQLT-a Proximal lienal tubules. Absorption o? glucose.

SG\LT-l ; characteristics

• -
Sodium dependent.
• unidirectional transport.
• Secondary active transport.
• Is a symport Transports jocose along with Sodium.

Ma* h’ ATPase pumps 3 Ma’ out and a h’ in with the utilization

o? I ATP.
Hence in sea-T-l, Ma’ is transported along the concentration
gradient while glucose is transported against the
concentration gradient.
Primarily SG4-T-I does not require ATP but to pump out the space
Ma’ and to bring in h’ (to maintain neutrality^ the MA’/h’
ATPase pump utilizes ATP. (secondary active transport)
Active

Biochemistry • v4.0 • Marrow 6.0 • 2022

 Glucose
transpoi|
• Bidirectional.
Along the concentration gradient.
Ping Porg mechanism :

High concentration

lou) concentration

-
Ping state Faces towards high concentration o? glucose and
attaches to it.

-
Pong state Faces towards the interior o¥ the plasma
membrane. Ping state conVormationallg changes to Pong state
and glucose is transported along the concentration gradient.

A hyperbolic curve on velocity v/s substrate

concentration graph.

S - Solute concentration.
-
v Rate o? absorption o? solute.

Hyperbolic curve - The rate o? absorption o? solute raises s

&
initially as the solute concentration increases and remains 8

the same a?ter a particular concentration (vmax).

I
Reason - all the carriers o? glucose get saturated at v max.
In simple diV^rusion, S is directly proportional to V.

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 Glucose
Leave Feedbai

Absorption of Glucose in the intestine 00:35:53

Lumen intestinal cell Blood

^lu
^al

Fru

Luminal side of Intestine !

Absorption via S<=<LT-i ; galactose > glucose > Fructose.
eiUT-5 ; Carrier mediated transport of Fructose along the
concentration gradient. It is facilitated diffusion.

CjLUT -a = Transport of glucose, galactose and Fructose from

intestinal cells to the blood. It is Insulin Independent.

In fl cells of the Pancreas and Liver, Qlucose is transported

into the cells via GLUT-a.
It has a low affinity to Qlucose.
Hence it is transported when the concentration of glucose is
more in the Blood.
In the liver, glucose is stored as e^lgcogen.
I
In Pancreas it helps in the secretion of Insulin.

In the Presence of Insulin, ^WT-4 is recruited to the plasma

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•

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GLYCOSI
Active space
 Glycolysis
14 Leave Feedbai

Preparatory phase »

I ATP I ADP

(reversible) Phospho hexose

isomerase

Fructose G phosphate

I ATP —, Phospho fructohinase l

I ADP

Fructose I,(a
bisphosphate

Aldolase (reversible)

Dihydroxy acetone €j|ycera)dehyde 3

phosphate (DMAP) phosphate (ejy 3 p)

PhosphoTriose
isomerase

o z x Hexohinase/olucoh 5 / \

—r glucose G phosphate

I ATP I ADP

Significance $

• Ist irreversible step.

• Regulatory step.
• Aux generating step.
• Phosphorylation by hexoKmase -traps glucose for
cellular metabolism.

a) In isomerisation of QG phosphate to fructose G phosphate,

the OO group is transferred to ca so that a free hydroxyl
group is available at Cl.
It is a reversible step.

I Fructose G phosphate j &

8
I ATP —- Phospho fructoKinase I
I
I AOP^,

Fructose i,G
bisphosphate

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Biochemstry
•

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•

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Active space
 14 Glycolyss Q4
Leave Feedbai

Aerobic glycolysis = 7 ATP.

PDH = a.S X a = 5 ATP
TCA cycle = a X IO = ao ATP
Total ATP generated 3a ATP.

Inhibitors of glycolysis 00:55:02

I. glyceraldehyde 3 phosphate dehydrogenase inhibited by

• lodoacetate.
• Arsenate • Decreases -the availability o? Pi.
a. enolase Inhibited by fluoride by reducing the availability
o¥ mg3' or mna\
Clinical signiflcance • MaF oxalate mixture used in
estimation o? blood glucose.

Rapaport Leubering cycle 00:58:05

Tabes place inside

Only IO# glucose enter this cycle.
Also called C.-L Shunt / a, 3 6P€* Shunt.

space
Active

Biochemistry • v4.0 • Marrow 6.0 • 2022

 Glycolysis QQ
14 Leave Feedbai

Clinical questions 01:12:09

Q. An elderly COPO patent admitted in emergency dept with

loss o¥ consciousness due to bleeding Vrom a stomach ulcer.
Her respiratory rate is rapid, cyanosis +, 6P lower shin is cold
and clammy. Emergency management started and blood
send Vor lab investigation.
uJhy is there loss oV consciousness?
Ans. Aerobic oxidation o? glucose aVXected which is the
primary metabolic Vuel Vor brain.
6rain cannot survive i? glucose is not going into oxidative
phase, resulting o? loss o? consciousness.
Q. The hypoxia induces the gene transcription o? enzymes o?
which metabolic pathway?
<HIF l) will
Ans. Hypoxia induced transcription factor I
increase expression o? enzymes o? glycolysis.

Q. Lach oV this pathway results in haemolysis. UJhy?

Ans. £66 solely depend on anaerobic pathway, which &
disrupted will lead to swelling and haemolysis o? £60.

Q. £60 need ATP -to maintain ion gradients in the membrane.

The loch o? it results in swelling o? £60 and lysis. To maintain
the ion gradient the major source o? ATP is which pathway?
Ans. Anaerobic glycolysis.

Q. Enzyme defect in glycolysis cause muscle Vatigue. idhy?

Ans. Exercising muscle inhypoxic state depends on anaerobic
glycolysis. Lach o? ATP production results in muscle Vatigue.

Q. Heart is susceptible to hypoxia but not skeletal muscle.

Why?
Ans. Heart has very low glycolytic capacity ord hence is
susceptible to hypoxia. This when compared to skeletal
muscle that has hgh glycoltic capacity and switches over to
anaerobic pathway Vor ATP production.

Biochemistry • v4.0 • Marrow 6.0 • 2022

 15 Applied aspe
Of Glycolysis

Cancer cells induce Hypoxia Induced Transcription Factor-l

Glycolysis & radiology 00:10:00

a Fluorodeoxy glucose (FdG) labelled glucose) is given to

locate the cancer.
FdQ injected into the cell -* Fd^ preferentially taKen inside
through g^ut transporters -> Qlucose concentrated inside
cancer cell io times -* Labelled glucose undergoes first step
of glycolysis-* HexoKinase step Phosphofluorodeoxy glu¬
cose -» Accumulation in cell-* Decay -* Emits positrons -*
Detected with PET scan.

Chemotherapeutic agents (under trial) :

glycolysis used to Kill cancer cells.

Inhibitors of
• a deoxy glucose (aoo) inhibits glycolytic pathway at the
level of hexoKinase.
• Lonidamine.
• 3 bromopyruvate.

8
I

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 16 Leave Feedbac

PYRUVATE DEHYDROGENASE

Fates of pyruvate 00:01:56

Pyruvate Dehydrogenase (PDH) =

• Site • mitochondria.
• Formed as a. result o? glycolysis (in cytoplasm).
• Proton symporter transports pyruvate Vrom cytoplasm to
mitochondria.
PDH : multienzyme complex :

S enzymes S coenzymes

• & I pyruvate dehydrogenase • Thiamine Pyrophosphate (TPP).

• ca dihydrolipoyl transacetylase • CoP
• Lipomide
• 63 dihydrolipomide • FAD
dehydrogenase • MAD*

• This multienzyme complex is similar to other multienzyme

space
complexes $ Active
(TCP Cycle).
51. feranched-chain Keto acid dehydrogenase complex

Biochemistry • v4.0 • Marrow 6.0 • 2022

Regulation of pyruvate dehydrogenase 00:15:26

This enzyme is active in well Ved state -* under influence o?

hiyh insulin-ylucayon ratio -* Dephosphorylated PDH (Active
state).

Increased ATP $ ADP ratio.

Increased MADH : MAD* ratio
Increased acetyl CoA CoA ratio .
— PDH is inhibited

Syniflcance o? pyruvate dehydroyenase :

Irreversible reaction
I. Pyruvate Acetyl CoA
a. Mo enzyme in human body can circumvent ths
irreversible enzyme.
Acetyl CoA cannot be converted into pyruvate.
Acetyl CoA is never a substrate Vor yluconeoyenesis.

Fat and glucose 00:21:26

3. Fat (Tri Acyl QlyceroO cannot be converted to ylucose.

• a exceptions :
i. glycerol.
it Propionyl CoA (formed Vrom odd chain Vatty acid).
4. excess carbohydrate is stored as Vat in adipose tissue.

excess carbohydrate -* fucose -* Pyruvate -* Acetyl CoA

TCA cycle Fatty acid + ejycerol -* TAQ -»

Stored in adipose tissue.

S. in chronic alcoholics -* eneryy depletion (less ATP

production). space
• deduced absorption o? thiamine (co-?actor) -* Less ATP.
• Mutritiona) deflciency (6 complex vitamins low • 6i, Ba,
Active
63, 6S) -> Less ATP.

Biochemistry • v4.0 •Marrow 6.0 • 2022