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Protein Metabolism
Dr. Ifat Ara Begum
Associate Professor
Dept of Biochemistry
Dhaka Medical College, Dhaka
2
3
4
5
Protein Turnover
6
7
 Protein turnover is the rate at which body proteins are
constantly being degraded and again resynthesized.
 It is 150-300 gm/day in adult
i.e.
1-2% of total body protein in adult.
[Total body protein in 70kg adult male is 12-14 kg]
8
Catabolized portion
(20%) must be
replaced by dietary
protein to maintain
normal body protein
content & nitrogen
balance
Nitrogen Balance
10
11
 Nitrogen balance is the difference between nitrogen
intake & nitrogen loss in an individual.
 Three types:
i) Nitrogen Equilibrium: In normal adults
ii) Positive Nitrogen Balance : During growth,
pregnancy
iii) Negative Nitrogen Balance : DM, malignancy, TB,
Trauma, Surgery etc
If loss exceeds 30% of total protein: Fatal
Amino Acid Pool
What is Amino Acid Pool?
13
 It is the free amino acid content distributed throughout
the extracellular fluid
 Quantitatively, it is about 100 gm in an adult individual.
 50% : Glutamate & Glutamine
 10% : Essential Amino Acids
 40% : Other Amino Acids
14
Intermediary
metabolism of
Amino acid
What is Amino Acid?
16
Amino group containing carboxylic acid
17
18
Anabolism Catabolism
 Synthesis of:
 NEAA
 Protein
NPN subs
Urea from NH3 via urea cycle
 Glucose, glycogen
 FA, fat, steroid, ketone bodies
 Transamination
 Deamination & removal of NH2 group
as NH3
 Catabolism of amino acid carbon -
skeleton to :
- Pyruvate
- Acetyl CoA
- Intermediates of TCA cycle
 Oxidation of Catabolic end products of
amino acid carbon skeleton via TCA
cycle
Transamination
Site of transamination :
Cytoplasm of:
 Liver
 Kidney
 Heart
 Sk. Muscle
 Brain.
Rate limiting enzyme:
Aminotransferase
Coenzyme needed:
Pyridoxal phosphate which acts as
an intermediate carrier of an NH2
group.
Nature: Amphibolic & reversible
Substrate: One amino acid & one
keto acid
Product: One keto acid & one amino
acid
.
What is Transamination?
21
 It is the transfer of NH2 group from an amino acid to a
keto acid with simultaneous production of corresponding
keto acid & amino acid respectively.
Remember,
No free NH3 is produced here
Only transfer of NH2 group occurs
Amino acid participating
in transamination :
All Amino acids except:
 Lys (Lysine)
 Thr (Threonine)
 Pro (Proline)
Keto acid participating in
transamination:
Three keto acids mostly
participates:
 α- ketoglutarate (ketoacid
of glutamate)
Oxaloacetate (keto acid of
aspartate)
 Pyruvate (ketoacid of
alanine)
23
Example of Aminotransferase / Transaminase
Alanine transaminase
Aspartate transaminase
Glutamate transaminase.
Clinical importance of these enzymes:
Role as hepatic marker / cardiac marker
25
Provides a link b/w
carbohydrate, protein &
fat metabolism
Biosynthesis of
NEAA
Importance of
Transamination
Funneling of NH2 group of different
amino acids ultimately to α-KG. α-KG
will form Glutamate
(The major amino acid that undergoes
oxidative deamination)
Formation of C
skeleton / keto acid of
an amino acid:
which can be
catabolized & oxidized to
generate energy
Oxidative deamination
Site of oxidative deamination:
Mitochondria of:
 Liver
 Kidney
 Heart
 Sk. Muscle
Rate limiting enzyme: Glutamate
dehydrogenase
Coenzyme needed:
NAD.
Nature: Catabolic
Substrate: Glutamate
Product: NH3 & α-KG
Types: Oxidative & Nonoxidative
.
What is Oxidative Deamination?
29
 Removal of –NH2 group from an amino acid in the form of
free NH3 with simultaneous formation of its corresponding
keto acid (C-skeleton)
 Amino acid unique in the process of deamination: Glutamate
Because,
it is the only amino acid that undergoes rapid oxidative
deamination catalyzed by glutamate dehydrogenase
(an active dehydrogenase)
30
31
Channel nitrogen of AA
as ammonia to urea cycle
Generate C-
skeleton of AA for
catabolic purpose
Importance of
Deamination
Metabolism of ammonia
34
Sources of
Ammonia
Bacterial degradation of urea into NH3
(by bacterial urease in intestinal lumen)
Catabolism of amino acids
( via Transamination &
deamination)
Catabolism of purine &
pyrimidine nitrogenous
bases
Catabolism of Glutamine
(& Glutamate)
36
Glutamine :
The temporary non-toxic storage & transport form
of NH3.
37
Disposal /
Metabolic fates
of Ammonia
Excretion of NH3 with urine as NH4+ salt
Formation of urea in urea
cycle & its excretion in
urine
Formation of Glutamate & Glutamine
in liver, kidney, muscle, brain
39
Toxicity which results
from hyperammonemia
(Normal level : 5-
50μmol/L
Brain tissue is mostly
affected & there is
depression in cerebral
activity
Ammonia
Intoxication
Causes of hyperammonemia:
 Hepatic dysfunction (Cirrhosis of liver, hepatic failure)
 Deficiency of enzyme of the urea cycle
Biochemical basis of ammonia intoxication / Hepatic
encephalopathy
41
 When excessive amounts of ammonia enter the central
nervous system, the brain's defences are severely challenged
42
43
Protein metabolism, july'20
Urea cycle
Site of Urea cycle :
Mitochondria & cytoplasm of liver
Rate limiting enzyme:
Carbamoylphosphate synthase I
Nature: Anabolic
Substrate: NH3
(Two NH3 participates , one directly
and another from aspartate)
Product: Urea (NH2 – CO – NH2)
.
47
48
49
Interaction with TCA
cycle
Disposal of NH3
& CO2
Functions /
Importance of urea
cycle
Conversion of toxic
ammonia into nontoxic
urea
Synthesis of NEAA:
 Arginine
 Proline From ornithine
51
52
Inborn error of protein metabolism
53
 Alkaptonuria
 Homocystinuria
 Phenylketonuria
 Albinism
 Maple syrup urine disease
54

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Protein metabolism, july'20

  • 1. Protein Metabolism Dr. Ifat Ara Begum Associate Professor Dept of Biochemistry Dhaka Medical College, Dhaka
  • 2. 2
  • 3. 3
  • 4. 4
  • 5. 5
  • 7. 7  Protein turnover is the rate at which body proteins are constantly being degraded and again resynthesized.  It is 150-300 gm/day in adult i.e. 1-2% of total body protein in adult. [Total body protein in 70kg adult male is 12-14 kg]
  • 8. 8 Catabolized portion (20%) must be replaced by dietary protein to maintain normal body protein content & nitrogen balance
  • 10. 10
  • 11. 11  Nitrogen balance is the difference between nitrogen intake & nitrogen loss in an individual.  Three types: i) Nitrogen Equilibrium: In normal adults ii) Positive Nitrogen Balance : During growth, pregnancy iii) Negative Nitrogen Balance : DM, malignancy, TB, Trauma, Surgery etc If loss exceeds 30% of total protein: Fatal
  • 13. What is Amino Acid Pool? 13  It is the free amino acid content distributed throughout the extracellular fluid  Quantitatively, it is about 100 gm in an adult individual.  50% : Glutamate & Glutamine  10% : Essential Amino Acids  40% : Other Amino Acids
  • 14. 14
  • 16. What is Amino Acid? 16 Amino group containing carboxylic acid
  • 17. 17
  • 18. 18 Anabolism Catabolism  Synthesis of:  NEAA  Protein NPN subs Urea from NH3 via urea cycle  Glucose, glycogen  FA, fat, steroid, ketone bodies  Transamination  Deamination & removal of NH2 group as NH3  Catabolism of amino acid carbon - skeleton to : - Pyruvate - Acetyl CoA - Intermediates of TCA cycle  Oxidation of Catabolic end products of amino acid carbon skeleton via TCA cycle
  • 20. Site of transamination : Cytoplasm of:  Liver  Kidney  Heart  Sk. Muscle  Brain. Rate limiting enzyme: Aminotransferase Coenzyme needed: Pyridoxal phosphate which acts as an intermediate carrier of an NH2 group. Nature: Amphibolic & reversible Substrate: One amino acid & one keto acid Product: One keto acid & one amino acid .
  • 21. What is Transamination? 21  It is the transfer of NH2 group from an amino acid to a keto acid with simultaneous production of corresponding keto acid & amino acid respectively. Remember, No free NH3 is produced here Only transfer of NH2 group occurs
  • 22. Amino acid participating in transamination : All Amino acids except:  Lys (Lysine)  Thr (Threonine)  Pro (Proline) Keto acid participating in transamination: Three keto acids mostly participates:  α- ketoglutarate (ketoacid of glutamate) Oxaloacetate (keto acid of aspartate)  Pyruvate (ketoacid of alanine)
  • 23. 23
  • 24. Example of Aminotransferase / Transaminase Alanine transaminase Aspartate transaminase Glutamate transaminase. Clinical importance of these enzymes: Role as hepatic marker / cardiac marker
  • 25. 25
  • 26. Provides a link b/w carbohydrate, protein & fat metabolism Biosynthesis of NEAA Importance of Transamination Funneling of NH2 group of different amino acids ultimately to α-KG. α-KG will form Glutamate (The major amino acid that undergoes oxidative deamination) Formation of C skeleton / keto acid of an amino acid: which can be catabolized & oxidized to generate energy
  • 28. Site of oxidative deamination: Mitochondria of:  Liver  Kidney  Heart  Sk. Muscle Rate limiting enzyme: Glutamate dehydrogenase Coenzyme needed: NAD. Nature: Catabolic Substrate: Glutamate Product: NH3 & α-KG Types: Oxidative & Nonoxidative .
  • 29. What is Oxidative Deamination? 29  Removal of –NH2 group from an amino acid in the form of free NH3 with simultaneous formation of its corresponding keto acid (C-skeleton)  Amino acid unique in the process of deamination: Glutamate Because, it is the only amino acid that undergoes rapid oxidative deamination catalyzed by glutamate dehydrogenase (an active dehydrogenase)
  • 30. 30
  • 31. 31
  • 32. Channel nitrogen of AA as ammonia to urea cycle Generate C- skeleton of AA for catabolic purpose Importance of Deamination
  • 34. 34
  • 35. Sources of Ammonia Bacterial degradation of urea into NH3 (by bacterial urease in intestinal lumen) Catabolism of amino acids ( via Transamination & deamination) Catabolism of purine & pyrimidine nitrogenous bases Catabolism of Glutamine (& Glutamate)
  • 36. 36 Glutamine : The temporary non-toxic storage & transport form of NH3.
  • 37. 37
  • 38. Disposal / Metabolic fates of Ammonia Excretion of NH3 with urine as NH4+ salt Formation of urea in urea cycle & its excretion in urine Formation of Glutamate & Glutamine in liver, kidney, muscle, brain
  • 39. 39
  • 40. Toxicity which results from hyperammonemia (Normal level : 5- 50μmol/L Brain tissue is mostly affected & there is depression in cerebral activity Ammonia Intoxication Causes of hyperammonemia:  Hepatic dysfunction (Cirrhosis of liver, hepatic failure)  Deficiency of enzyme of the urea cycle
  • 41. Biochemical basis of ammonia intoxication / Hepatic encephalopathy 41  When excessive amounts of ammonia enter the central nervous system, the brain's defences are severely challenged
  • 42. 42
  • 43. 43
  • 46. Site of Urea cycle : Mitochondria & cytoplasm of liver Rate limiting enzyme: Carbamoylphosphate synthase I Nature: Anabolic Substrate: NH3 (Two NH3 participates , one directly and another from aspartate) Product: Urea (NH2 – CO – NH2) .
  • 47. 47
  • 48. 48
  • 49. 49
  • 50. Interaction with TCA cycle Disposal of NH3 & CO2 Functions / Importance of urea cycle Conversion of toxic ammonia into nontoxic urea Synthesis of NEAA:  Arginine  Proline From ornithine
  • 51. 51
  • 52. 52
  • 53. Inborn error of protein metabolism 53  Alkaptonuria  Homocystinuria  Phenylketonuria  Albinism  Maple syrup urine disease
  • 54. 54