The document summarizes protein metabolism and the urea cycle. It discusses that 1-2% of body proteins are degraded and renewed daily. Ammonia produced is highly toxic, so the liver converts it to urea. Glutamine synthase fixes ammonia as non-toxic glutamine and glutaminase releases it for urea synthesis. The urea cycle uses ammonia, CO2, and aspartate to synthesize urea using 5 enzymes in the liver. Rare metabolic disorders can cause urea synthesis blockage, increasing blood ammonia and risking intoxication and brain damage. Treatments include low-protein diets and frequent small meals to avoid sudden ammonia increases.
Are most abundantly distributed organic compounds.
70 kg man= protein weight constitute 12 kg
Skeleton and connective tissue contains half
Body protein and other half is intracellular.
Are most abundantly distributed organic compounds.
70 kg man= protein weight constitute 12 kg
Skeleton and connective tissue contains half
Body protein and other half is intracellular.
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All tissues have some capability for synthesis of the non-essential amino acids, amino acid remodeling, and conversion of non-amino acid carbon skeletons into amino acids and other derivatives that contain nitrogen. However, the liver is the major site of nitrogen metabolism in the body.
The urea cycle is the metabolic pathway that transforms nitrogen to urea for excretion from the body. Liver cells play a critical role in disposing of nitrogenous waste by forming urea hrough the action of the urea cycle.
Nitrogenous excretory products are then removed from the body through in the urine.
The urea excreted each day by a healthy adult (about 30 g) accounts for about 90% of the nitrogenous excretory products.
The cycle occurs mainly in the liver.
This presentation is about removal of Ammonia from Aminoacid for further metabolize to Urea.
The slides in the presentation describe the process of removal of ammonia from amino acid.
Presentation includes
1. Source and outlet of ammonia
2. Transportation of NH3
3. Glucose-Alanine cycle
4. organs involved in nitrogen metabolism
5. Ammonia Toxicity
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2. Biochemistry for nurses: Unit 3
• Protein Turnover = Continuous degradation and synthesis of proteins.
Replacement of 1-2% of the total body protein each day
• Amino acid pool = Accumulation of free AA in the liver and the blood: 75 % of
liberated AA from tissue proteins are reutilized
• Degradation (catabolism of AA) = Excess of AA are not stored! but rapidly
degraded for the synthesis of glucose (glycolosis) and lipids. Degradation of excess AA
causes an excess of nitrogen.
• Waste = Nitrogen excess is transformed into urea (80%) and ammonium (NH4
+) in
order to be thrown away in the urine.
(Liver and Blood)
3. Biochemistry for nurses: Unit 3
NITROGEN BALANCE
• The amino acids are the main source of Nitrogen.
• Nitrogen balance (NB) is a comparaison between nitrogen
intake (Dietary proteins) and nitrogen loss (indigested
proteins in feces, waste excretion as urea (80%) and ammonia
(NH4
+) in the urine).
- For normal adult: Ingested nitrogen = excreted nitrogen
- Positive NB = Ingested nitrogen > excreted nitrogen
(children growth, pregnancy)
- Negative NB = Ingested nitrogen < excreted nitrogen
(may follow surgery, advanced cancer, marasmus)
4. Biochemistry for nurses: Unit 3
• Protein Turnover = Continuous degradation and synthesis of proteins.
Replacement of 1-2% of the total body protein each day
• Amino acid pool = Accumulation of free AA in the liver and the blood: 75 % of
liberated AA from tissue proteins are reutilized
• Degradation (catabolism of AA) = Excess of AA are not stored! but rapidly
degraded for the synthesis of glucose (glycolosis) and lipids. Degradation of excess AA
causes an excess of nitrogen.
• Waste = Nitrogen excess is transformed into urea (80%) and ammonium (NH4
+) in
order to be thrown away in the urine.
(Liver and Blood)
5. Biochemistry for nurses: Unit 3
Digestion and absorption of proteins
Digestion = degradation of the protein into AA by the digestive
system to make it absorbable by intestine.
Absorption = Transfert of the AA from the intestine to the blood
6. Biochemistry for nurses: Unit 3
• Proteins are digested by proteases and peptidases.
• Protein digestion starts in the stomach.
• PEPSIN is an endoprotease which degrades food proteins in the stomach.
8. Biochemistry for nurses: Unit 3
• TRYPSIN = Endopeptidase cleaves the peptide bond at the carboxyl
side of the Lysine and Arginine.
• CHYMOTRYPSIN = Endopeptidase cleaves the peptide bond at the
carboxyl side of the Tryptophan, Tyrosine and Phenylalanine.
9. Biochemistry for nurses: Unit 3
Protein digestion is completed in the small intestine by brush border
enzymes carboxypeptidase, aminopeptidase, and dipeptidase.
11. Biochemistry for nurses: Unit 3
Practise
ENDOPEPTIDASE:
• Trypsin = cleaves at the COOH side of Lysine and Arginine.
• Chymotrypsin = cleaves at the COOH side of Tryptophan, Tyrosine and
Phenylalanine.
• Tri or Dipeptidase = cleaves between AA of tri or dipeptides
EXOPEPTIDASE:
• Carboxypeptidase = removes AA from the COOH end
• Aminopeptidase = removes AA from the NH2 end
H2N-Val-Cys-Ala-Leu-Lys-Val-Glu-Arg-Gly-Phe-Phe-Tyr-Thr-Pro-Lys-Ala-COOH
Trypsin + Chymotrypsin
?
Tripeptidase + Aminopeptidase
+ Carboxypeptidase
Final products ?
12. Biochemistry for nurses: Unit 3
H2N-Val-Cys-Ala-Leu-Lys-Val-Glu-Arg-Gly-Phe-Phe-Tyr-Thr-Pro-Lys-Ala-COOH
Trypsin
13. Biochemistry for nurses: Unit 3
H2N-Val-Cys-Ala-Leu-Lys-Val-Glu-Arg-Gly-Phe-Phe-Tyr-Thr-Pro-Lys-Ala-COOH
ChymotrypsinTrypsin
14. Biochemistry for nurses: Unit 3
H2N-Val-Cys-Ala-Leu-Lys-Val-Glu-Arg-Gly-Phe-Phe-Tyr-Thr-Pro-Lys-Ala-COOH
ChymotrypsinTrypsin
H2N-Val-Cys-Ala-Leu-Lys-COOH
H2N-Val-Glu-Arg-COOH
H2N-Gly-Phe-COOH
H2N-Phe-COOH
H2N-Tyr-COOH
H2N-Thr-Pro-Lys-COOH
H2N-Ala-COOH
15. Biochemistry for nurses: Unit 3
H2N-Val-Cys-Ala-Leu-Lys-COOH
H2N-Val-Glu-Arg-COOH
H2N-Gly-Phe-COOH
H2N-Phe-COOH
H2N-Tyr-COOH
H2N-Thr-Pro-Lys-COOH
H2N-Ala-COOH
Tripeptidase
16. Biochemistry for nurses: Unit 3
H2N-Val-Cys-Ala-Leu-Lys-COOH
H2N-Val-Glu-Arg-COOH
H2N-Gly-Phe-COOH
H2N-Phe-COOH
H2N-Tyr-COOH
H2N-Thr-Pro-Lys-COOH
H2N-Ala-COOH
Tripeptidase
+ Aminopeptidase
17. Biochemistry for nurses: Unit 3
H2N-Val-Cys-Ala-Leu-Lys-COOH
H2N-Val-Glu-Arg-COOH
H2N-Gly-Phe-COOH
H2N-Phe-COOH
H2N-Tyr-COOH
H2N-Thr-Pro-Lys-COOH
H2N-Ala-COOH
Tripeptidase
+ Aminopeptidase
+ Carboxypeptidase
20. Biochemistry for nurses: Unit 3
• Protein Turnover = Continuous degradation and synthesis of proteins.
Replacement of 1-2% of the total body protein each day
• Amino acid pool = Dietary proteins and the catabolism of tissue proteins
provide free AA. 75 % of liberated AA from tissue proteins are reutilized.
• Degradation (catabolism of AA) = Excess of AA are not stored! but
rapidly degraded for the synthesis of glucose (glycolosis) and lipids.
Degradation of excess AA causes an excess of nitrogen.
• Waste = Nitrogen excess is transformed into urea (80%) and ammonium
(NH4
+) in order to be thrown away in the urine.
(Liver and Blood)
21. Biochemistry for nurses: Unit 3
Definition of the Keto Acid
• The deamination of an Amino Acid (= removing of the amino group) forms
the corresponding Keto Acid.
• The Keto acid is also called « the carbon skeleton »
22. Biochemistry for nurses: Unit 3
Definition of the Keto Acid
• The deamination of an Amino Acid (= removing of the amino group) forms
the corresponding Keto Acid.
• The Keto acid is also called « the carbon skeleton »
WASTE
REUSED!
23. Biochemistry for nurses: Unit 3
BIOSYNTHESIS of UREA
Biosynthesis of urea is composed
by 4 stages:
1. Transamination
2. Oxidative deamination of
Glutamate
3. Ammonia transport
4. Reactions of the urea cycle.
80% of the excess amino acid
nitrogen forms Urea in order to
be thrown away in the urine.
Tissues
Liver
24. Biochemistry for nurses: Unit 3
Transamination
•Transfert of the α-amino group (NH2) to the ketoglutarate to give GLUTAMATE
• The reaction is reversible.
• The reaction is catalysed by an enzyme (Aminotransferase) in presence of a
co-enzyme (PLP = Vit B6)
(TISSUES)
25. Biochemistry for nurses: Unit 3
Oxidative deamination of Glutamate
• Formation of ammonia (NH3) from the amino group (NH2) of the Glutamate
by oxidative deamination.
• Glutamate is the only Amino Acid that undergoes oxidative deamination.
• Enzyme = Glutamate Dehydrogenase (GDH); Coenzyme = NAD+
(LIVER)
26. Biochemistry for nurses: Unit 3
Amino acid oxidase reaction
• The amino acid oxidase (AAO) of liver
and kidney removes the nitrogen as
ammonium ion (NH4
+).
• Conversion of Amino Acids to an Imino
acids which are decomposed to a Keto
acid with release of NH4
+.
• Enzyme = AAO ; Coenzyme = Flavin
• The reduced Flavin is reoxidized by O2,
forming hydrogen peroxide (H2O2) which
then is split to O2 and H2O by
CATALASE.
(LIVER and KIDNEY)
27. Biochemistry for nurses: Unit 3
Ammonia (NH3) Transport
• NH3 is very toxic to the nervous system!
• The NH3 produced by tissue are rapidly removed from circulation by the
Liver and converted to UREA
• Only traces (10-20 uG/dL) of NH3 are present in blood in normal
conditions
• Liver damage and metabolic disorders are associated with elevated
concentration of NH3 in the blood.
• In case of CIRRHOSIS (hepatic disease), NH3 rises to toxic levels,
consequently: Tremor, blurred, coma and ultimately death.
• The transport of NH3 from the tissue to the liver is done by
GLUTAMATE or GLUTAMINE as nontoxic forms.
28. Biochemistry for nurses: Unit 3
Glutamine Synthase fixes NH3 as Glutamine.
• NH3 is fixed by GLUTAMATE to give
GLUTAMINE
• Enzyme = Glutamine Synthase (inside
tissue mitochondria)
• That reaction needs ENERGY to work!
(hydrolysis of ATP )
Tissues
29. Biochemistry for nurses: Unit 3
UREA CYCLE
• UREA is the major end product of Nitrogen catabolism in human body.
• Synthesis of 1 molecule of UREA requires:
1. 3 molecules of ATP (Energy!)
2. 1 molecule of NH4+
3. 1 molecule of α- amino group (NH2) of Aspartate
• 5 enzymes catalyse the Urea Cycle in the liver cells:
1. Carbamoyl Phosphate Synthase I
2. Ornithine Transcarbamoylase
3. Argininosuccinic Acid Synthase
4. Argininosuccinase
5. Arginase
31. Biochemistry for nurses: Unit 3
Summary of the Urea Cycle
2 NH3 + CO2 + 3 ATP
UREA + 2 ADP + Pi
+ AMP + Pi
Liver
32. Biochemistry for nurses: Unit 3
Summary of the ammonia elimination
Amino acids
degradation
Amino group
Keto acids
« carbon skeletton »
Synthesis of glucoses
and lipids
33. Biochemistry for nurses: Unit 3
Summary of the ammonia elimination
• 1 – 2 % of the body proteins are degraded and renewed daily
• Ammonia (NH3) is highly toxic.
• Ammonia (NH3) is converted to Urea
• Glutamine synthase converts NH3 to nontoxic glutamine
• Glutaminase releases NH3 for use in urea synthesis
• NH3, CO2 and the amide nitrogen of aspartate provide the
atoms of urea
• Hepatic urea synthesis takes place in part in the mitochondrial
matrix and in part in the cytosol.
35. Biochemistry for nurses: Unit 3
Metabolic disorders of urea synthesis
• Extremely rare: Dysfunction of enzymes
• Disorders in urea synthesis
36. Biochemistry for nurses: Unit 3
Metabolic disorders of urea synthesis
• Extremely rare: Dysfunction of enzymes
• Disorders in urea synthesis
[NH3] in blood increases
37. Biochemistry for nurses: Unit 3
Metabolic disorders of urea synthesis
• Extremely rare: Dysfunction of enzymes
• Disorders in urea synthesis
[NH3] in blood increases
NH3 intoxication
Intoxication is more severe
when the urea synthesis is
blocked at reactions 1 or 2
38. Biochemistry for nurses: Unit 3
Metabolic disorders of urea synthesis
• Extremely rare: Dysfunction of enzymes
• Disorders in urea synthesis
[NH3] in blood increases
NH3 intoxication
Intoxication is more severe
when the urea synthesis is
blocked at reactions 1 or 2
Clinical symptoms:
•Vomiting
• Avoidance of high protein foods
• Irritability
• Lethargy
• Mental Retardation (Brain damage)
39. Biochemistry for nurses: Unit 3
Metabolic disorders of urea synthesis
• Extremely rare: Dysfunction of enzymes
• Disorders in urea synthesis
[NH3] in blood increases
NH3 intoxication
Intoxication is more severe
when the urea synthesis is
blocked at reactions 1 or 2
Clinical Treatments:
• Low protein diet ingested
• Frequent small meals to avoid
sudden increase in blood of the
NH3 levels.
Clinical symptoms:
•Vomiting
• Avoidance of high protein foods
• Irritability
• Lethargy
• Mental Retardation (Brain damage)
40. Biochemistry for nurses: Unit 3
Metabolic disorders of urea synthesis
• Extremely rare: Dysfunction of enzymes
• Disorders in urea synthesis
[NH3] in blood increases
NH3 intoxication
Intoxication is more severe
when the urea synthesis is
blocked at reactions 1 or 2
Clinical Treatments:
• Low protein diet ingested
• Frequent small meals to avoid
sudden increase in blood of the
NH3 levels.
Clinical
improvement and
minimization of
Brain damage.
Clinical symptoms:
•Vomiting
• Avoidance of high protein foods
• Irritability
• Lethargy
• Mental Retardation (Brain damage)