Urea cycle
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Urea cycle and disorder
The document discusses the urea cycle, which occurs primarily in the liver and converts toxic ammonia produced by tissues into harmless urea.
There are three transport forms that carry ammonia from peripheral tissues to the liver - glutamate, glutamine, and alanine.
The urea cycle takes place in both the mitochondria and cytoplasm of liver cells. It disposes of two waste products, ammonia and carbon dioxide, and participates in blood pH regulation.
Urea cycle disorder
urea is the end product of protein metabolism. it is synthesized in liver from ammonia and carbon dioxide. deficiency of urea cycle enzymes causes disorders that characterized by hyperammonemia. most frequent type of UCD is ornitine transcarbomylase deficiency which lead to increase orotic acid, ammonia in the blood.
Metabolism of Brached Chain Amino Acid (Valine, Isoleucine, Leucine)
Branched chain amino acids include leucine, isoleucine, and valine. They are broken down by the branched chain alpha-ketoacid dehydrogenase complex in mitochondria. A defect in this enzyme can cause branched chain ketoaciduria, where patients accumulate branched chain amino acids and their keto acids in their urine, which smells like maple syrup or burnt sugar. This rare genetic disorder impairs other amino acid transport and protein synthesis, and can lead to seizures, vomiting, ketoacidosis, coma, and death if not treated with a low-branched chain amino acid diet and thiamine supplementation.
Metabolism of Glycine. .
Glycine is the simplest amino acid that can be synthesized from serine, threonine, carbon dioxide, or glyoxylate. It is involved in the synthesis of proteins, heme, purines, creatine, glutathione, and acts as a conjugating agent. Excess glycine is excreted in urine and can lead to renal stones if accumulated. A rare disorder is glycinuria where large amounts of glycine are excreted in urine due to defective renal reabsorption. Primary hyperoxaluria is an inborn error characterized by high urinary oxalate excretion resulting from a defect in glycine transaminase.
Glycine metabolism
Glycine is an aliphatic amino acid which gives rise to many vital derivatives. This is a non-essential amino acid. This presentation is targeted for MBBS, MD, BDS and general Biochemistry students.
General Reactions involved in amino acid metabolism
1. The document discusses various reactions involved in amino acid metabolism including deamination, desulfuration, transamination, and transmethylation.
2. Deamination is the removal of the amino group from an amino acid, which can occur oxidatively or non-oxidatively. Oxidative deamination uses amino acid oxidases and releases ammonia and hydrogen peroxide.
3. Transamination is the reversible transfer of the amino group between amino acids and alpha-keto acids, producing new amino acids and keto acids. It requires pyridoxal phosphate and does not release free ammonia.
GLYCINE METABOLISM
Glycine is a non-essential amino acid that is involved in many biochemical processes. It can be synthesized from serine, threonine, carbon dioxide, ammonia, and glyoxylate. Glycine is important for the synthesis of heme, purines, creatine, glutathione, bile acids, and hippuric acid. It is metabolized through the glycine cleavage system or converted to serine and then gluconeogenic precursors. Elevated glycine levels can cause neurological issues while deficiencies are associated with hyperoxaluria and kidney stone formation.
Metabolism of Basic Amino Acids (Arginine, Histidine, Lysine)
This document summarizes amino acid metabolism, including the synthesis and degradation pathways of arginine, histidine, lysine, and their importance. It discusses how arginine is involved in nitric oxide synthesis and polyamine synthesis. Histidine degradation produces histamine. Lysine is involved in carnitine synthesis. Disorders are discussed for each amino acid pathway.
Recommended
Urea cycle and disorder
The document discusses the urea cycle, which occurs primarily in the liver and converts toxic ammonia produced by tissues into harmless urea.
There are three transport forms that carry ammonia from peripheral tissues to the liver - glutamate, glutamine, and alanine.
The urea cycle takes place in both the mitochondria and cytoplasm of liver cells. It disposes of two waste products, ammonia and carbon dioxide, and participates in blood pH regulation.
Urea cycle disorder
urea is the end product of protein metabolism. it is synthesized in liver from ammonia and carbon dioxide. deficiency of urea cycle enzymes causes disorders that characterized by hyperammonemia. most frequent type of UCD is ornitine transcarbomylase deficiency which lead to increase orotic acid, ammonia in the blood.
Metabolism of Brached Chain Amino Acid (Valine, Isoleucine, Leucine)
Branched chain amino acids include leucine, isoleucine, and valine. They are broken down by the branched chain alpha-ketoacid dehydrogenase complex in mitochondria. A defect in this enzyme can cause branched chain ketoaciduria, where patients accumulate branched chain amino acids and their keto acids in their urine, which smells like maple syrup or burnt sugar. This rare genetic disorder impairs other amino acid transport and protein synthesis, and can lead to seizures, vomiting, ketoacidosis, coma, and death if not treated with a low-branched chain amino acid diet and thiamine supplementation.
Metabolism of Glycine. .
Glycine is the simplest amino acid that can be synthesized from serine, threonine, carbon dioxide, or glyoxylate. It is involved in the synthesis of proteins, heme, purines, creatine, glutathione, and acts as a conjugating agent. Excess glycine is excreted in urine and can lead to renal stones if accumulated. A rare disorder is glycinuria where large amounts of glycine are excreted in urine due to defective renal reabsorption. Primary hyperoxaluria is an inborn error characterized by high urinary oxalate excretion resulting from a defect in glycine transaminase.
Glycine metabolism
Glycine is an aliphatic amino acid which gives rise to many vital derivatives. This is a non-essential amino acid. This presentation is targeted for MBBS, MD, BDS and general Biochemistry students.
General Reactions involved in amino acid metabolism
1. The document discusses various reactions involved in amino acid metabolism including deamination, desulfuration, transamination, and transmethylation.
2. Deamination is the removal of the amino group from an amino acid, which can occur oxidatively or non-oxidatively. Oxidative deamination uses amino acid oxidases and releases ammonia and hydrogen peroxide.
3. Transamination is the reversible transfer of the amino group between amino acids and alpha-keto acids, producing new amino acids and keto acids. It requires pyridoxal phosphate and does not release free ammonia.
GLYCINE METABOLISM
Glycine is a non-essential amino acid that is involved in many biochemical processes. It can be synthesized from serine, threonine, carbon dioxide, ammonia, and glyoxylate. Glycine is important for the synthesis of heme, purines, creatine, glutathione, bile acids, and hippuric acid. It is metabolized through the glycine cleavage system or converted to serine and then gluconeogenic precursors. Elevated glycine levels can cause neurological issues while deficiencies are associated with hyperoxaluria and kidney stone formation.
Metabolism of Basic Amino Acids (Arginine, Histidine, Lysine)
This document summarizes amino acid metabolism, including the synthesis and degradation pathways of arginine, histidine, lysine, and their importance. It discusses how arginine is involved in nitric oxide synthesis and polyamine synthesis. Histidine degradation produces histamine. Lysine is involved in carnitine synthesis. Disorders are discussed for each amino acid pathway.
Purine degradation
This document summarizes purine biosynthesis and degradation. Purine is synthesized through an 11 step pathway forming IMP, the parent nucleotide. IMP is then used to synthesize AMP and GMP. Purines are broken down to uric acid through a multi-step process. Gout is caused by excessive uric acid formation due to increased purine biosynthesis or decreased excretion leading to uric acid crystal deposition in joints.
Urea cycle
1. The urea cycle is a series of enzymatic reactions that occurs primarily in the liver to convert toxic ammonia produced from amino acid catabolism into urea for excretion.
2. The cycle involves five principal reactions: carbamoyl phosphate synthesis, citrulline synthesis, argininosuccinate synthesis, argininosuccinate cleavage, and arginine cleavage into ornithine and urea.
3. The urea cycle serves two major biological roles - detoxification of ammonia into urea and biosynthesis of the amino acid arginine from ornithine in tissues like liver, kidney, and intestine.
Urea cycle and its disorders
Synthesis of urea and disorders resulting from defects in urea synthesis for medical, biochemistry and biology undergraduates
DISORDERS OF PHENYLALANINE METABOLISM
The document discusses several inborn errors of amino acid metabolism including phenylketonuria (PKU), tyrosinemia, alkaptonuria, and albinism. PKU is caused by a deficiency of phenylalanine hydroxylase leading to accumulation of phenylalanine. Tyrosinemia results from defects in tyrosine catabolism. Alkaptonuria is caused by homogentisate oxidase deficiency leading to deposition of homogentisate pigments. Albinism is due to lack of tyrosinase resulting in absent melanin synthesis. These disorders are diagnosed by detecting abnormal metabolites in urine and treated with dietary modifications and supplements.
Urea cycle
The document summarizes the urea cycle, which occurs in the liver to convert ammonia into urea for excretion. It involves several steps spanning the mitochondria and cytosol. Carbamoyl phosphate synthetase activates ammonia and CO2 to initiate the cycle. Ornithine, aspartate, and several other compounds join the cycle through condensation reactions requiring ATP. Arginase produces urea and ornithine at the end of the cycle. The cycle is connected to the Krebs cycle and regulated by factors like dietary protein and N-acetyl glutamate. Deficiencies in cycle enzymes can cause diseases with high ammonia levels like hyperammonemia.
Metabolism of amino acids
Digestion of proteins, absorption of amino acids, synthesis of amino acids, catabolism of amino acids and synthesis of specialised non-protein compounds from amino acids for undergraduates
Urea cycle and disorder
The document discusses the urea cycle, which involves a cyclic set of chemical reactions that occur in the liver to convert ammonia into urea for excretion. It details the 5 enzyme-catalyzed reactions, participating amino acids and cofactors. One molecule of urea requires 3 ATP and utilizes ammonia, bicarbonate, and aspartate. The cycle is regulated by N-acetyl glutamate and compartmentalized between mitochondria and cytosol. Disorders cause hyperammonemia due to deficient enzymes, with earlier blocks causing more severe symptoms like vomiting and lethargy.
Cholesterol Biosynthesis
This document summarizes the biosynthesis of cholesterol in 5 steps:
1) Mevalonate is formed from acetyl-CoA in the cytosol. 2) Isoprenoid units are formed from mevalonate. 3) Six isoprenoid units condense to form squalene. 4) Squalene is cyclized to form lanosterol. 5) Lanosterol is modified through a series of changes to ultimately form cholesterol in the endoplasmic reticulum. Cholesterol biosynthesis is a major regulatory point for cholesterol levels and is the target of statin drugs.
urea cycle & its regulation
The urea cycle is a metabolic pathway that occurs in the liver to convert excess nitrogen from amino acid catabolism into urea for excretion. It involves five enzymes and five steps to synthesize urea from ammonia and carbon dioxide. Defects in the urea cycle can cause hyperammonemia, where high ammonia levels impair the citric acid cycle and ATP production in the brain.
TRYPTOPHAN METABOLISM
Tryptophan is an essential amino acid that is metabolized through two main pathways - the kynurenine pathway and serotonin pathway. The kynurenine pathway leads to the production of NAD+ and takes place mainly in the liver. This pathway involves the enzymes tryptophan pyrrolase and kynureninase. Deficiencies in these enzymes or vitamin B6 can cause reduced NAD+ synthesis and manifestations of pellagra. The serotonin pathway produces the neurotransmitter serotonin from tryptophan in various tissues like the brain, gut and blood platelets. Serotonin is involved in behaviors, sleep, and gastrointestinal function. Melatonin is also derived from serotonin metabolism and regulates circadian rhyth
BRANCHED CHAIN AMINO ACID METABOLISM
This document summarizes the metabolism of the branched chain amino acids valine, leucine, and isoleucine. It describes how they are first transaminated to their corresponding keto acids, then undergo oxidative decarboxylation by alpha-keto acid dehydrogenase to form acyl-CoA thioesters. These are further dehydrogenated and enter different pathways, with valine being converted to propionyl-CoA and being glycogenic, leucine producing acetyl-CoA and acetoacetate and being ketogenic, and isoleucine undergoing both glycogenic and ketogenic fates. Defects in these pathways can cause diseases like maple syrup urine disease.
Transamination & deamination
A comprehensive presentation on Transamination & Deamination for MBBS, BDS ,B.Pharm & biotechnology students to facilitate self study.
Beta oxidation of fatty acid
This document summarizes fatty acid oxidation and beta-oxidation. It describes that fatty acid oxidation occurs in the mitochondria to break down fatty acids into acetyl-CoA, generating energy. Beta-oxidation involves four steps - oxidation, hydration, oxidation again, and cleavage - to sequentially remove two-carbon acetyl-CoA units from the fatty acid. The acetyl-CoA can then enter the citric acid cycle to generate more energy through oxidative phosphorylation.
Urea cycle
1) Ammonia is produced in tissues and transported to the liver where it is detoxified to urea in the urea cycle. The three main transport forms are glutamate, glutamine, and alanine.
2) The urea cycle converts ammonia and carbon dioxide to urea using enzymes in the liver mitochondria and cytoplasm. This prevents ammonia toxicity.
3) Genetic defects in urea cycle enzymes can cause hyperammonemia, leading to complications like cerebral edema, seizures, coma and death if not treated. Treatment aims to reduce ammonia levels and promote its excretion through alternate pathways.
Disorders of pyrimidine metabolism
This document discusses disorders of pyrimidine metabolism. It provides an overview of pyrimidine synthesis pathways including de novo and salvage pathways. It describes one specific disorder, hereditary orotic aciduria, which is caused by a defect in UMP synthetase, resulting in excess orotic acid excretion. Treatment involves supplementing with UMP, which downregulates the pathway via feedback inhibition. The document contrasts pyrimidine and purine synthesis, regulation, catabolism, and salvage pathways.
Amino acid catabolism - Part-2 (Urea cycle and clinical significance)
The document discusses the urea cycle, which is the process by which excess nitrogen from amino acid catabolism is converted to urea for excretion. It describes the six amino acids and five enzymes involved in the cyclic urea formation reactions, which take place in the liver. Defects in the urea cycle enzymes can cause hyperammonemia due to the buildup of toxic ammonia, often presenting in newborns but sometimes not until later in life. Laboratory tests of blood ammonia levels, amino acid levels, and genetic testing can help diagnose specific urea cycle disorders.
Heme catabolism and jaundice
1) Hemoglobin is broken down in red blood cells, producing bilirubin at a rate of approximately 250-350 mg per day.
2) Bilirubin binds to albumin and is transported to the liver, where it is conjugated and secreted into bile ducts.
3) Jaundice occurs when there is excessive bilirubin that cannot be processed by the liver, resulting in a buildup that discolors the skin and eyes. It can be caused by hemolytic anemia, liver disease, or bile duct obstruction.
TRANSAMINATION & DEAMINATION
The document discusses protein and amino acid metabolism. It states that proteins are made of amino acids and perform many important functions in the body. Amino acids can be synthesized by the body or obtained through diet. They undergo breakdown and interconversion through various pathways including transamination, oxidative deamination, and the urea cycle to generate energy, synthesize other compounds, and regulate nitrogen balance in the body. Precise control of protein and amino acid metabolism is crucial for many physiological processes.
Branched chain amino acid metabolism
This document summarizes key information about the metabolism of the branched chain amino acids valine, leucine, and isoleucine. It discusses that they are essential amino acids whose metabolism begins in muscle tissue. The first three reactions - transamination, oxidative decarboxylation, and dehydrogenation - are common to all three amino acids. Conditions like maple syrup urine disease and isovaleric acidemia occur due to defects in later steps of this metabolic pathway.
PHENYLALANINE METABOLISM
Phenylalanine is converted to tyrosine by the enzyme phenylalanine hydroxylase in the liver. Tyrosine can then be incorporated into proteins or converted to important compounds like melanin, thyroid hormones, dopamine, norepinephrine, and epinephrine. The metabolism of phenylalanine and tyrosine involves multiple enzymatic steps and requires cofactors like biopterin, ascorbic acid, and molecular oxygen. Disorders in these pathways can lead to conditions like albinism or Parkinson's disease.
Lec 3 level 3-de(protein metabolism &urea cycle)
1) Proteins are digested in the stomach by pepsin and in the small intestine by trypsin, chymotrypsin, and other pancreatic enzymes into dipeptides and tripeptides.
2) Amino acids are absorbed in the small intestine through carrier-mediated transport systems and used to build new proteins or for energy production.
3) Excess amino acids are broken down through transamination and the urea cycle to form urea, which is excreted in urine to remove waste nitrogen from the body. Disorders of the urea cycle can cause toxic buildup of ammonia in the blood.
METABOLISM OF PROTEINS B.sc Generic Nursing .pptx
This document discusses protein metabolism and amino acid catabolism. It covers:
1. The two major enzyme systems that degrade proteins - the ubiquitin-proteasome system and lysosomal system.
2. Amino acid catabolism involves removing amino groups to form ammonia, then converting carbon skeletons to energy-producing intermediates.
3. Ammonia is transported to the liver as glutamine or alanine and converted to urea via the urea cycle for excretion, preventing hyperammonemia.
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Purine degradation
This document summarizes purine biosynthesis and degradation. Purine is synthesized through an 11 step pathway forming IMP, the parent nucleotide. IMP is then used to synthesize AMP and GMP. Purines are broken down to uric acid through a multi-step process. Gout is caused by excessive uric acid formation due to increased purine biosynthesis or decreased excretion leading to uric acid crystal deposition in joints.
Urea cycle
1. The urea cycle is a series of enzymatic reactions that occurs primarily in the liver to convert toxic ammonia produced from amino acid catabolism into urea for excretion.
2. The cycle involves five principal reactions: carbamoyl phosphate synthesis, citrulline synthesis, argininosuccinate synthesis, argininosuccinate cleavage, and arginine cleavage into ornithine and urea.
3. The urea cycle serves two major biological roles - detoxification of ammonia into urea and biosynthesis of the amino acid arginine from ornithine in tissues like liver, kidney, and intestine.
Urea cycle and its disorders
Synthesis of urea and disorders resulting from defects in urea synthesis for medical, biochemistry and biology undergraduates
DISORDERS OF PHENYLALANINE METABOLISM
The document discusses several inborn errors of amino acid metabolism including phenylketonuria (PKU), tyrosinemia, alkaptonuria, and albinism. PKU is caused by a deficiency of phenylalanine hydroxylase leading to accumulation of phenylalanine. Tyrosinemia results from defects in tyrosine catabolism. Alkaptonuria is caused by homogentisate oxidase deficiency leading to deposition of homogentisate pigments. Albinism is due to lack of tyrosinase resulting in absent melanin synthesis. These disorders are diagnosed by detecting abnormal metabolites in urine and treated with dietary modifications and supplements.
Urea cycle
The document summarizes the urea cycle, which occurs in the liver to convert ammonia into urea for excretion. It involves several steps spanning the mitochondria and cytosol. Carbamoyl phosphate synthetase activates ammonia and CO2 to initiate the cycle. Ornithine, aspartate, and several other compounds join the cycle through condensation reactions requiring ATP. Arginase produces urea and ornithine at the end of the cycle. The cycle is connected to the Krebs cycle and regulated by factors like dietary protein and N-acetyl glutamate. Deficiencies in cycle enzymes can cause diseases with high ammonia levels like hyperammonemia.
Metabolism of amino acids
Digestion of proteins, absorption of amino acids, synthesis of amino acids, catabolism of amino acids and synthesis of specialised non-protein compounds from amino acids for undergraduates
Urea cycle and disorder
The document discusses the urea cycle, which involves a cyclic set of chemical reactions that occur in the liver to convert ammonia into urea for excretion. It details the 5 enzyme-catalyzed reactions, participating amino acids and cofactors. One molecule of urea requires 3 ATP and utilizes ammonia, bicarbonate, and aspartate. The cycle is regulated by N-acetyl glutamate and compartmentalized between mitochondria and cytosol. Disorders cause hyperammonemia due to deficient enzymes, with earlier blocks causing more severe symptoms like vomiting and lethargy.
Cholesterol Biosynthesis
This document summarizes the biosynthesis of cholesterol in 5 steps:
1) Mevalonate is formed from acetyl-CoA in the cytosol. 2) Isoprenoid units are formed from mevalonate. 3) Six isoprenoid units condense to form squalene. 4) Squalene is cyclized to form lanosterol. 5) Lanosterol is modified through a series of changes to ultimately form cholesterol in the endoplasmic reticulum. Cholesterol biosynthesis is a major regulatory point for cholesterol levels and is the target of statin drugs.
urea cycle & its regulation
The urea cycle is a metabolic pathway that occurs in the liver to convert excess nitrogen from amino acid catabolism into urea for excretion. It involves five enzymes and five steps to synthesize urea from ammonia and carbon dioxide. Defects in the urea cycle can cause hyperammonemia, where high ammonia levels impair the citric acid cycle and ATP production in the brain.
TRYPTOPHAN METABOLISM
Tryptophan is an essential amino acid that is metabolized through two main pathways - the kynurenine pathway and serotonin pathway. The kynurenine pathway leads to the production of NAD+ and takes place mainly in the liver. This pathway involves the enzymes tryptophan pyrrolase and kynureninase. Deficiencies in these enzymes or vitamin B6 can cause reduced NAD+ synthesis and manifestations of pellagra. The serotonin pathway produces the neurotransmitter serotonin from tryptophan in various tissues like the brain, gut and blood platelets. Serotonin is involved in behaviors, sleep, and gastrointestinal function. Melatonin is also derived from serotonin metabolism and regulates circadian rhyth
BRANCHED CHAIN AMINO ACID METABOLISM
This document summarizes the metabolism of the branched chain amino acids valine, leucine, and isoleucine. It describes how they are first transaminated to their corresponding keto acids, then undergo oxidative decarboxylation by alpha-keto acid dehydrogenase to form acyl-CoA thioesters. These are further dehydrogenated and enter different pathways, with valine being converted to propionyl-CoA and being glycogenic, leucine producing acetyl-CoA and acetoacetate and being ketogenic, and isoleucine undergoing both glycogenic and ketogenic fates. Defects in these pathways can cause diseases like maple syrup urine disease.
Transamination & deamination
A comprehensive presentation on Transamination & Deamination for MBBS, BDS ,B.Pharm & biotechnology students to facilitate self study.
Beta oxidation of fatty acid
This document summarizes fatty acid oxidation and beta-oxidation. It describes that fatty acid oxidation occurs in the mitochondria to break down fatty acids into acetyl-CoA, generating energy. Beta-oxidation involves four steps - oxidation, hydration, oxidation again, and cleavage - to sequentially remove two-carbon acetyl-CoA units from the fatty acid. The acetyl-CoA can then enter the citric acid cycle to generate more energy through oxidative phosphorylation.
Urea cycle
1) Ammonia is produced in tissues and transported to the liver where it is detoxified to urea in the urea cycle. The three main transport forms are glutamate, glutamine, and alanine.
2) The urea cycle converts ammonia and carbon dioxide to urea using enzymes in the liver mitochondria and cytoplasm. This prevents ammonia toxicity.
3) Genetic defects in urea cycle enzymes can cause hyperammonemia, leading to complications like cerebral edema, seizures, coma and death if not treated. Treatment aims to reduce ammonia levels and promote its excretion through alternate pathways.
Disorders of pyrimidine metabolism
This document discusses disorders of pyrimidine metabolism. It provides an overview of pyrimidine synthesis pathways including de novo and salvage pathways. It describes one specific disorder, hereditary orotic aciduria, which is caused by a defect in UMP synthetase, resulting in excess orotic acid excretion. Treatment involves supplementing with UMP, which downregulates the pathway via feedback inhibition. The document contrasts pyrimidine and purine synthesis, regulation, catabolism, and salvage pathways.
Amino acid catabolism - Part-2 (Urea cycle and clinical significance)
The document discusses the urea cycle, which is the process by which excess nitrogen from amino acid catabolism is converted to urea for excretion. It describes the six amino acids and five enzymes involved in the cyclic urea formation reactions, which take place in the liver. Defects in the urea cycle enzymes can cause hyperammonemia due to the buildup of toxic ammonia, often presenting in newborns but sometimes not until later in life. Laboratory tests of blood ammonia levels, amino acid levels, and genetic testing can help diagnose specific urea cycle disorders.
Heme catabolism and jaundice
1) Hemoglobin is broken down in red blood cells, producing bilirubin at a rate of approximately 250-350 mg per day.
2) Bilirubin binds to albumin and is transported to the liver, where it is conjugated and secreted into bile ducts.
3) Jaundice occurs when there is excessive bilirubin that cannot be processed by the liver, resulting in a buildup that discolors the skin and eyes. It can be caused by hemolytic anemia, liver disease, or bile duct obstruction.
TRANSAMINATION & DEAMINATION
The document discusses protein and amino acid metabolism. It states that proteins are made of amino acids and perform many important functions in the body. Amino acids can be synthesized by the body or obtained through diet. They undergo breakdown and interconversion through various pathways including transamination, oxidative deamination, and the urea cycle to generate energy, synthesize other compounds, and regulate nitrogen balance in the body. Precise control of protein and amino acid metabolism is crucial for many physiological processes.
Branched chain amino acid metabolism
This document summarizes key information about the metabolism of the branched chain amino acids valine, leucine, and isoleucine. It discusses that they are essential amino acids whose metabolism begins in muscle tissue. The first three reactions - transamination, oxidative decarboxylation, and dehydrogenation - are common to all three amino acids. Conditions like maple syrup urine disease and isovaleric acidemia occur due to defects in later steps of this metabolic pathway.
PHENYLALANINE METABOLISM
Phenylalanine is converted to tyrosine by the enzyme phenylalanine hydroxylase in the liver. Tyrosine can then be incorporated into proteins or converted to important compounds like melanin, thyroid hormones, dopamine, norepinephrine, and epinephrine. The metabolism of phenylalanine and tyrosine involves multiple enzymatic steps and requires cofactors like biopterin, ascorbic acid, and molecular oxygen. Disorders in these pathways can lead to conditions like albinism or Parkinson's disease.
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Amino acid catabolism - Part-2 (Urea cycle and clinical significance)
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1) Proteins are digested in the stomach by pepsin and in the small intestine by trypsin, chymotrypsin, and other pancreatic enzymes into dipeptides and tripeptides.
2) Amino acids are absorbed in the small intestine through carrier-mediated transport systems and used to build new proteins or for energy production.
3) Excess amino acids are broken down through transamination and the urea cycle to form urea, which is excreted in urine to remove waste nitrogen from the body. Disorders of the urea cycle can cause toxic buildup of ammonia in the blood.
METABOLISM OF PROTEINS B.sc Generic Nursing .pptx
This document discusses protein metabolism and amino acid catabolism. It covers:
1. The two major enzyme systems that degrade proteins - the ubiquitin-proteasome system and lysosomal system.
2. Amino acid catabolism involves removing amino groups to form ammonia, then converting carbon skeletons to energy-producing intermediates.
3. Ammonia is transported to the liver as glutamine or alanine and converted to urea via the urea cycle for excretion, preventing hyperammonemia.
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The document discusses amino acid catabolism and the urea cycle. It explains that amino acids are first transaminated, removing their amino groups as ammonia. Ammonia is highly toxic, so it is converted to urea via the urea cycle in the liver and excreted in urine. The urea cycle involves several enzymatic steps that incorporate ammonia and aspartate to form the relatively non-toxic urea molecule for excretion. Deficiencies in urea cycle enzymes can cause hyperammonemia, which is particularly dangerous for the brain.
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The urea cycle occurs in the liver and involves several enzymatic steps to convert the toxic ammonia produced from amino acid catabolism into urea. Ammonia enters the liver from the blood and is converted to carbamoyl phosphate by carbamoyl phosphate synthase I in the mitochondria. It is then converted to citrulline by ornithine transcarbamoylase. Further reactions involving argininosuccinate synthetase, argininosuccinase, and argginase in the cytosol ultimately produce urea from arginine. An increased blood urea level can indicate problems with the liver, kidneys, or diet, while a decreased level may point to liver disease. Certain amino acids
Protein-Metabolism.ppt
The document discusses protein metabolism and degradation. It covers:
1) The processes of protein synthesis and catabolism as well as the digestion and absorption of dietary proteins in the stomach and intestines.
2) How cells degrade cellular proteins at different rates and have mechanisms to detect and remove damaged proteins using ubiquitin tags.
3) The ubiquitin tagging system involves three enzymes (E1, E2, E3) that attach ubiquitin to target proteins to mark them for destruction by the proteasome.
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Nitrogen metabolism (metabolic fate of amino acid, catabolism of amino acid, ...
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Ammonia is toxic to animals and the terminal stages of ammonia intoxication in humans are characterized by a comatose state and cerebral edema. High levels of ammonia lead to increased levels of glutamine in brain astrocytes, causing cellular swelling and the observed symptoms. Most terrestrial animals excrete amino nitrogen in the form of urea through the urea cycle, which occurs in the liver and converts ammonia to less toxic urea in five enzymatic steps before urea is transported to the kidneys and excreted in urine.
urea cycle.pptx
The document outlines key aspects of amino acid metabolism and the urea cycle. It begins by describing the breakdown of muscle proteins and the transport of amino acids between tissues like liver and muscle. It then details the formation of ammonia from amino acid catabolism and its detoxification via the urea cycle in the liver. The summary concludes by mentioning several urea cycle disorders that can result from deficiencies in cycle enzymes, causing hyperammonemia.
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Protein metabolism-Catabolism
The document provides an overview of protein metabolism. It discusses the key topics of:
- Protein structure and functions in the body.
- The amino acid pool and how tissues draw from and contribute to it.
- The digestion of proteins in the body.
- The two phases of protein metabolism - anabolism and catabolism.
- The major catabolic pathways in the liver that break down amino acids including deamination, transamination, decarboxylation, and transmethylation.
- The ornithine or urea cycle, which occurs primarily in the liver and converts ammonia into urea for excretion from the body.
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This document discusses amino acid metabolism and the urea cycle. It begins with an introduction to amino acids, their roles in the body, and how they are broken down into individual amino acids. It then describes the processes of transamination and deamination, by which amino groups are transferred between amino acids and their carbon skeletons are converted to keto acids. One key reaction is glutamate serving as a collection point for amino groups. The urea cycle is then introduced as the process by which ammonia produced from amino acid breakdown is detoxified into urea for excretion. The urea cycle involves 5 enzymes and 4 ATP and occurs primarily in the liver.
Metabolism protein
1) Proteins in the diet are broken down into smaller peptides and individual amino acids through digestion by proteolytic enzymes in the stomach, pancreas, and intestines.
2) In the liver, amino acids are broken down through transamination and transdeamination reactions to produce ammonia, which is highly toxic.
3) Ammonia is detoxified in the liver through the urea cycle into urea, which is excreted in the urine. Deficiencies in urea cycle enzymes can cause a toxic buildup of ammonia in the blood.
Nitrogen Balance.pdf
Ammonia is produced from amino acid catabolism and transported to the liver for urea synthesis. The urea cycle converts ammonia to urea using enzymes in the liver mitochondria and cytosol. Defects in the urea cycle can cause toxic hyperammonemia. Treatment focuses on limiting ammonia intake and increasing excretion through drugs and diet modification. High blood urea levels can occur from prerenal causes like dehydration or heart failure reducing kidney function, or renal failure impairing excretion.
AMINO ACID power presentation that describes amino acids
Here are the answers to your review questions:
1. The regulatory reaction for the urea cycle is the formation of carbamoyl phosphate, which is catalyzed by carbamoyl phosphate synthetase I in the liver mitochondria.
2. Ornithine, citrulline, arginine, aspartate, argininosuccinate.
3. Three ATP molecules are needed to make one molecule of urea in the urea cycle.
4. The Krebs bicycle links the urea cycle and citric acid cycle. CO2 produced in the citric acid cycle is used for urea synthesis, and fumarate can be converted to oxaloacetate, linking the two cycles.
Lec3 level3-nunitrogenmetabolism-130204053253-phpapp01
1) Nitrogen enters the body through dietary protein and is metabolized through amino acids. Amino acids are broken down and the nitrogen is removed as ammonia, which is converted to urea to be excreted.
2) The amino acid pool and protein turnover are key concepts in nitrogen metabolism. Amino acids from protein breakdown replenish the amino acid pool, which is also used for protein synthesis and other processes.
3) Dietary proteins are digested by enzymes in the stomach and pancreas into dipeptides and tripeptides, then fully into amino acids by intestinal enzymes for absorption.
PROTEIN METABOLISM.pptx
The document summarizes key aspects of amino acid metabolism, including transamination and deamination. Transamination involves the transfer of amino groups between amino acids and keto acids, catalyzed by transaminases. Deamination results in the liberation of ammonia from amino acids for urea synthesis. Ammonia produced from amino acid breakdown is toxic, so mammals excrete it as urea via the urea cycle in the liver and kidneys. The urea cycle involves several enzymes that incorporate ammonia into urea to allow its excretion and prevent toxicity.
Amino acid catabolism
The document summarizes the catabolism of amino acids. It discusses how excess amino acids are degraded by removing their amino groups via transamination and oxidative deamination, forming ammonia and keto acids. Most ammonia is incorporated into urea in the liver via the urea cycle for excretion. The amino acid pool is supplied from endogenous protein breakdown, dietary protein, and nonessential amino acid synthesis. It is depleted through protein synthesis, incorporation into other molecules, and oxidation. Protein turnover constantly synthesizes and degrades proteins. The steps of amino acid catabolism include transamination, oxidative deamination, ammonia transport to the liver, and the urea cycle.
UREA CYCLE AND UREA CYCLE DISORDERS
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.
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- 1. Urea Cycle Dr. Amro Yousef Al-Amleh
- 2. Urea Cycle • One nitrogen of the urea molecule is supplied by free ammonia, and the other nitrogen by aspartate. • Glutamate is the immediate precursor of both ammonia. • The carbon and oxygen of urea are derived from CO2.
- 4. • The first two reactions leading to the synthesis of urea occur in the mitochondria, whereas the remaining cycle enzymes are located in the cytosol. 1. Carbamoyl phosphate synthetase I (CPS-1) 2. Ornithine transcarbamoylase (OTC) 3. Argininosuccinate synthetase 4. Argininosuccinate synthetase 5. Arginase
- 9. Regulation of Urea cycle
- 10. Fate of Urea
- 12. Hyperammonemia • Acquired hyperammonemia Liver disease is common cause of hyperammonemia • Congenital hyperammonemia Genetic deficiencies of each of the five enzymes of the urea cycle. • Ornithine transcarbamoylase deficiency, which is X-linked, is the most common of these disorders. • All of the other urea cycle disorders follow autosomal recessive inheritance pattern.
- 13. Catabolism of Amino Acids Breakdown of the carbon skeletons
- 14. Catabolism of the amino acids 1. Removal of a-amino groups 2. Breakdown of the resulting carbon skeletons • Oxaloacetate. • a-ketoglutarate • Fumarate • Succinyl CoA • Pyruvate • Acetyl CoA • Acetoacetate
- 16. Amino acids that form oxaloacetate 1. Aspartae 2. Asparagine
- 17. Amino acids that form a-ketoglutarate 1. Glutamate 2. Glutamine 3. Arginine 4. Proline 5. Histidine
- 18. Glutamate
- 19. Glutamine
- 20. Proline
- 21. Arginine
- 22. Histidine
- 24. Amino acids that form pyruvate 1. Alanine 2. Cysteine 3. Serine 4. Threonine 5. Glycine 6. Tryptophan
- 25. Alanine
- 26. Cysteine
- 27. Serine
- 30. Tryptophan
- 31. Amino acids that form fumarate 1. Tyrosine 2. phenylalanine
- 34. Amino acids that form succinyl CoA 1. Methionine 2. Valine 3. Threonine 4. Isoleucine
- 36. Methionine
- 38. Fate of Homocysteine • Homocysteine has two fates:- 1. Resynthesis of methionine: Homocysteine accepts methyl group from N5-methyltetrahydrofolate (N5-methyl-THF) in reaction requiring methylcobalamin, coenzyme derived from vitamin B12. 2. Synthesis of cysteine and production of succinyl CoA
- 41. Catabolism of the branched-chain amino acids • The branched-chain amino acids, isoleucine, leucine, and valine, are essential amino acids. • They are metabolized primarily by the peripheral tissues (particularly muscle), rather than by the liver.
- 42. 1. Transamination branched-chain amino acid aminotransferase. 2. Oxidative decarboxylation branched-chain a-keto acid dehydrogenase complex 3. Dehydrogenation FAD-linked dehydrogenation 4. End products: • The catabolism of isoleucine acetyl CoA and succinyl CoA, rendering it both ketogenic and glucogenic. • The catabolism of Valine succinyl CoA and is glucogenic. • The catabolism of Leucine, acetoacetate and acetyl CoA and is ketogenic
- 44. Amino acids that form acetyl CoA or acetoacetyl CoA 1. Leucine is exclusively ketogenic in its catabolism, forming acetyl CoA and acetoacetate. 2. Isoleucine acetyl CoA + propionyl CoA. 3. Lysine: An exclusively ketogenic amino acid. Lysine is ultimately converted to acetoacetyl CoA. 4. Tryptophan alanine + acetoacetyl CoA. 5. Phenylalanine acetoacetate + fumarate 6. Tyrosine acetoacetate + fumarate
- 45. Oxaloacetate Alpha-KGlu Pyruvate Fumarate Succinyl CoA Acetyl CoA or acetoacetate