Amino acid metabolism
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This document discusses amino acid metabolism. It notes that proteins are composed of amino acids, which can be classified as essential, non-essential, or semi-essential. The body contains an amino acid pool of around 100g that is dynamic and participates in metabolic reactions. The pool is mostly composed of glutamate and glutamine. Amino acids come from protein turnover and ingestion. Amino acid metabolism involves two steps - transamination and deamination. Transamination involves transferring the amino group between amino acids and keto acids, catalyzed by transaminases. Deamination removes the amino group as ammonia and can occur oxidatively via glutamate dehydrogenase or non-oxidatively via various enzymes.
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SERINE & THREONINE METABOLISM
Serine is a non-essential amino acid that can be synthesized from glycolysis intermediates. It participates in one-carbon metabolism by donating methylene groups, and it is involved in the synthesis of several other amino acids, phospholipids, and sphingolipids. Serine can be converted to pyruvate through transamination and deamination reactions. Threonine is an essential amino acid that can be cleaved to form glycine, acetaldehyde, and derivatives that enter the citric acid cycle or form pyruvate and lactate. Both amino acids play important roles in biosynthesis as carriers of phosphate groups.
Metabolism of amino acids (general metabolism)
Metabolism of amino acids (general metabolism).
Part - I of amino acid metabolism.
This presentation covers Transamination, deamination, formation and Transport of Ammoniaand etc.
integration of metabolism
The integration of metabolism ensures a constant supply of fuel to all tissues. Metabolic pathways are controlled through four mechanisms: substrate availability, allosteric effectors, covalent modification of enzymes, and regulation of enzyme synthesis. During the absorptive state after a meal, elevated insulin and substrate availability promote anabolism through increased storage of carbohydrates, fats, and proteins in liver, adipose tissue, and skeletal muscle. In the fasting state, glucagon stimulates glycogenolysis, gluconeogenesis, and ketogenesis in the liver to maintain blood glucose levels while fatty acids are oxidized in other tissues.
CHOLESTEROL BIOSYNTHESIS
Cholesterol is synthesized from acetyl-CoA in a multi-step process located in the endoplasmic reticulum and cytoplasm. HMG-CoA reductase catalyzes the rate-limiting step and is regulated by transcription, covalent modification, and competitive inhibitors like statins. Cholesterol is transported by LDL and HDL and is used for cell membrane structure, steroid hormone synthesis, or storage.
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.
Metabolism of Amino Acids
1) Amino acids from dietary proteins and cellular protein turnover enter an amino acid pool in the body. Glutamate and glutamine make up about 50% of this pool.
2) Amino acids are used to generate energy, synthesize proteins, and produce other nitrogenous compounds. They undergo transamination and deamination, with the amino groups being converted to ammonia.
3) Ammonia is disposed of through the urea cycle in mammals, where it is combined with carbon dioxide to form urea, which is excreted in urine. Disorders of the urea cycle can cause hyperammonemia and neurological issues.
Nucleic Acid Metabolism
The document provides an overview of nucleic acid metabolism and the synthesis of purines and pyrimidines. It discusses how nucleotides serve as building blocks for nucleic acids and how they are synthesized through both de novo and salvage pathways. The key steps in purine synthesis include the production of IMP from PRPP and glutamine, followed by conversion to AMP and GMP. Purines can also be salvaged from nucleic acid breakdown. Deoxyribonucleotides are synthesized from ribonucleotides by the enzyme ribonucleotide reductase. Defects in nucleotide synthesis can cause diseases.
Pyrimidine Synthesis and Degradation
This document summarizes the de novo synthesis of pyrimidine nucleotides. It describes the precursors and reactions involved in synthesizing the pyrimidine ring and then attaching it to ribose phosphate to form the pyrimidine nucleotides CMP, UMP and TMP. It also discusses the conversion of UDP to CTP and dTMP, the regulation of pyrimidine synthesis, salvage pathways, catabolism of pyrimidines, and the genetic disorder orotic aciduria caused by a defect in the enzyme UMP synthase.
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SERINE & THREONINE METABOLISM
Serine is a non-essential amino acid that can be synthesized from glycolysis intermediates. It participates in one-carbon metabolism by donating methylene groups, and it is involved in the synthesis of several other amino acids, phospholipids, and sphingolipids. Serine can be converted to pyruvate through transamination and deamination reactions. Threonine is an essential amino acid that can be cleaved to form glycine, acetaldehyde, and derivatives that enter the citric acid cycle or form pyruvate and lactate. Both amino acids play important roles in biosynthesis as carriers of phosphate groups.
Metabolism of amino acids (general metabolism)
Metabolism of amino acids (general metabolism).
Part - I of amino acid metabolism.
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integration of metabolism
The integration of metabolism ensures a constant supply of fuel to all tissues. Metabolic pathways are controlled through four mechanisms: substrate availability, allosteric effectors, covalent modification of enzymes, and regulation of enzyme synthesis. During the absorptive state after a meal, elevated insulin and substrate availability promote anabolism through increased storage of carbohydrates, fats, and proteins in liver, adipose tissue, and skeletal muscle. In the fasting state, glucagon stimulates glycogenolysis, gluconeogenesis, and ketogenesis in the liver to maintain blood glucose levels while fatty acids are oxidized in other tissues.
CHOLESTEROL BIOSYNTHESIS
Cholesterol is synthesized from acetyl-CoA in a multi-step process located in the endoplasmic reticulum and cytoplasm. HMG-CoA reductase catalyzes the rate-limiting step and is regulated by transcription, covalent modification, and competitive inhibitors like statins. Cholesterol is transported by LDL and HDL and is used for cell membrane structure, steroid hormone synthesis, or storage.
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.
Metabolism of Amino Acids
1) Amino acids from dietary proteins and cellular protein turnover enter an amino acid pool in the body. Glutamate and glutamine make up about 50% of this pool.
2) Amino acids are used to generate energy, synthesize proteins, and produce other nitrogenous compounds. They undergo transamination and deamination, with the amino groups being converted to ammonia.
3) Ammonia is disposed of through the urea cycle in mammals, where it is combined with carbon dioxide to form urea, which is excreted in urine. Disorders of the urea cycle can cause hyperammonemia and neurological issues.
Nucleic Acid Metabolism
The document provides an overview of nucleic acid metabolism and the synthesis of purines and pyrimidines. It discusses how nucleotides serve as building blocks for nucleic acids and how they are synthesized through both de novo and salvage pathways. The key steps in purine synthesis include the production of IMP from PRPP and glutamine, followed by conversion to AMP and GMP. Purines can also be salvaged from nucleic acid breakdown. Deoxyribonucleotides are synthesized from ribonucleotides by the enzyme ribonucleotide reductase. Defects in nucleotide synthesis can cause diseases.
Pyrimidine Synthesis and Degradation
This document summarizes the de novo synthesis of pyrimidine nucleotides. It describes the precursors and reactions involved in synthesizing the pyrimidine ring and then attaching it to ribose phosphate to form the pyrimidine nucleotides CMP, UMP and TMP. It also discusses the conversion of UDP to CTP and dTMP, the regulation of pyrimidine synthesis, salvage pathways, catabolism of pyrimidines, and the genetic disorder orotic aciduria caused by a defect in the enzyme UMP synthase.
Histidine metabolism
Histidine metabolism involves several steps:
1) Histidine is first converted to urocanate by histidase.
2) Urocanate is then converted to 4-imidazolone 5-propionate by urocanate hydratase.
3) 4-imidazolone 5-propionate is further broken down by 4-imidazolone 5-propionase to N-formimino-L-glutamate (FIGLU).
FIGLU is then converted to glutamate by glutamate formimino transferase in a reaction that requires tetrahydrofolate and produces ammonia.
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- Deficiencies in enzymes involved in galactose metabolism can cause galactosemia, a serious genetic disorder if galactose is not restricted from the diet.
Glucose transport
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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.
Electron transport chain and Oxidative phosphorylation
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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.
Gluconeogenesis - The Pathway and Regulation
Gluconeogenesis is the process by which glucose is synthesized from non-carbohydrate precursors in the liver and kidneys. It occurs mainly during periods of fasting and involves converting substrates like lactate, glycerol, and certain amino acids into glucose. The pathway overcomes three thermodynamic barriers of glycolysis through smaller successive steps. Regulation occurs through allosteric control of enzymes, hormonal control of fructose 2,6-bisphosphate levels, and transcriptional control of key genes like PEPCK and FOXO1. Together these mechanisms help direct carbon fluxes towards gluconeogenesis or glycolysis based on energy demands.
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1) The de novo pathway synthesizes purine nucleotides from simple precursors through a two-stage process forming IMP and then converting it to AMP or GMP.
2) The salvage pathway recycles purine bases and nucleosides obtained from the diet or cell turnover to form nucleotides.
3) Both pathways work together to synthesize the purine nucleotides needed for nucleic acid synthesis, with the salvage pathway playing a larger role in certain tissues.
Purine degradation
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URONIC ACID PATHWAY
This document summarizes the glucuronic acid pathway, an alternative oxidative pathway for glucose metabolism. It provides UDP-glucuronic acid, which is used to conjugate bilirubin, steroids, and drugs to make them more water soluble and excretable. The pathway also synthesizes glycosaminoglycans and is involved in vitamin C synthesis in many animals. Key steps include the conversion of glucose-6-phosphate to UDP-glucuronate and the subsequent production of L-gulonate, a precursor for ascorbic acid synthesis. Certain genetic disorders can cause excess excretion of metabolites from this pathway such as L-xylulose in essential pentosuria.
Purine and Pyrimidine biosynthesis
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Amino acid metabolism
The document discusses amino acid metabolism. It begins by defining amino acids as derivatives of carboxylic acids with an amino group substitution. Amino acids are essential for building proteins and participate in many metabolic reactions. They are classified by the properties of their side chains. Protein digestion involves proteases in the stomach, pancreas, and small intestine that hydrolyze proteins into amino acids. Amino acids are absorbed into the blood and transported to tissues. Within cells, amino groups are transferred between amino acids and ketoacids in transamination reactions or removed as ammonia by deamination. The liver converts ammonia into less toxic urea via the urea cycle to prevent intoxication. Defects in the urea cycle can
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Histidine metabolism
Histidine metabolism involves several steps:
1) Histidine is first converted to urocanate by histidase.
2) Urocanate is then converted to 4-imidazolone 5-propionate by urocanate hydratase.
3) 4-imidazolone 5-propionate is further broken down by 4-imidazolone 5-propionase to N-formimino-L-glutamate (FIGLU).
FIGLU is then converted to glutamate by glutamate formimino transferase in a reaction that requires tetrahydrofolate and produces ammonia.
METABOLISM OF GALACTOSE, FRUCTOSE & AMINO SUGARS
- Lactose in milk is broken down by lactase into glucose and galactose. Galactose is metabolized mainly in the liver.
- Galactose is converted to glucose through a series of reactions involving galactokinase, galactose-1-phosphate uridylyltransferase, and UDP-glucose 4-epimerase.
- Deficiencies in enzymes involved in galactose metabolism can cause galactosemia, a serious genetic disorder if galactose is not restricted from the diet.
Glucose transport
Glucose transport into cells is mediated by glucose transporter (GLUT) proteins. [1] There are five main GLUT transporters that are involved in glucose transport and each has a distinct tissue distribution and function. [2] GLUT transporters use a flip-flop mechanism to transport glucose across the cell membrane according to the concentration gradient. [3] Insulin regulates glucose transport by stimulating the translocation of GLUT4 and GLUT1 transporters from intracellular vesicles to the cell membrane, increasing the influx of glucose into cells.
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Biosynthesis and degradation of porphyrin and heme
This document summarizes the biosynthesis and degradation of porphyrin and heme. It discusses how glycine and succinyl CoA are condensed to form δ-aminolevulinate, the starting material for porphyrin synthesis. Four molecules of porphobilinogen then condense to form the porphyrin ring. A series of reactions incorporates iron to form heme. Heme is degraded through heme oxygenase to form biliverdin and bilirubin, which is transported to the liver bound to albumin.
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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.
Electron transport chain and Oxidative phosphorylation
The document summarizes electron transport chain (ETC) and oxidative phosphorylation. It describes that NADH and FADH2 produced during metabolism are oxidized via ETC complexes I-IV to create a proton gradient, then ATP synthase uses this gradient to synthesize ATP. The ETC consists of Complexes I-V located in the inner mitochondrial membrane, with Complexes I, III, and IV pumping protons from the matrix to the intermembrane space during electron transfer, building up proton motive force used by Complex V to drive ATP synthesis from ADP and phosphate.
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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.
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Gluconeogenesis is the process by which glucose is synthesized from non-carbohydrate precursors in the liver and kidneys. It occurs mainly during periods of fasting and involves converting substrates like lactate, glycerol, and certain amino acids into glucose. The pathway overcomes three thermodynamic barriers of glycolysis through smaller successive steps. Regulation occurs through allosteric control of enzymes, hormonal control of fructose 2,6-bisphosphate levels, and transcriptional control of key genes like PEPCK and FOXO1. Together these mechanisms help direct carbon fluxes towards gluconeogenesis or glycolysis based on energy demands.
De novo and salvage pathway of purines
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1) The de novo pathway synthesizes purine nucleotides from simple precursors through a two-stage process forming IMP and then converting it to AMP or GMP.
2) The salvage pathway recycles purine bases and nucleosides obtained from the diet or cell turnover to form nucleotides.
3) Both pathways work together to synthesize the purine nucleotides needed for nucleic acid synthesis, with the salvage pathway playing a larger role in certain tissues.
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.
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URONIC ACID PATHWAY
This document summarizes the glucuronic acid pathway, an alternative oxidative pathway for glucose metabolism. It provides UDP-glucuronic acid, which is used to conjugate bilirubin, steroids, and drugs to make them more water soluble and excretable. The pathway also synthesizes glycosaminoglycans and is involved in vitamin C synthesis in many animals. Key steps include the conversion of glucose-6-phosphate to UDP-glucuronate and the subsequent production of L-gulonate, a precursor for ascorbic acid synthesis. Certain genetic disorders can cause excess excretion of metabolites from this pathway such as L-xylulose in essential pentosuria.
Purine and Pyrimidine biosynthesis
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This document discusses protein metabolism and the metabolism of amino acids. It notes that proteins are the most abundant organic compounds in the body, making up 10-12kg of dry weight, and perform many structural and functional roles. Amino acids are the building blocks of proteins and there are 20 naturally occurring amino acids, with 10 being non-essential and needing to be synthesized by the body. The amino acid pool is maintained through intake from dietary proteins and synthesis of non-essential amino acids, and is utilized for protein synthesis and other metabolic processes. Protein metabolism involves the constant breakdown and resynthesis of body proteins.
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Amino acid metabolism
Amino acid metabolism involves several key reactions: transamination, deamination, and the urea cycle. Transamination is the transfer of amino groups between amino acids via pyridoxal phosphate. Deamination removes amino groups via oxidative or non-oxidative pathways, producing ammonia. The liver's urea cycle converts ammonia into urea for excretion to detoxify ammonia. Disorders of the urea cycle can cause high ammonia levels and neurological issues if not treated. Amino acids undergo breakdown and synthesis to form proteins, peptides, and other nitrogenous compounds essential for cellular metabolism and function.
Amino acid metabolism
Amino acid metabolism involves several key reactions: transamination, deamination, and the urea cycle. Transamination involves transferring amino groups between amino acids and keto acids with pyridoxal phosphate as a cofactor. Deamination removes amino groups via oxidative or non-oxidative pathways, producing ammonia. The liver's urea cycle incorporates ammonia into urea for excretion to detoxify high levels. Disorders can occur if urea cycle enzymes are deficient, causing hyperammonemia. Blood urea levels provide clinical information about liver and kidney function.
Metabolism of amino acid
Proteins are essential macromolecules that make up the structure and carry out functions in the body. They are composed of amino acids, which can be synthesized by the body or obtained through diet. Amino acids undergo catabolism through four main stages: transamination, oxidative deamination, ammonia transport, and the urea cycle. The urea cycle is crucial for detoxifying ammonia produced from amino acid catabolism and involves six enzymes that convert ammonia to urea in the liver for excretion. Defects in the urea cycle can cause hyperammonemia, which can be toxic to the brain if not addressed.
proteiin_metabolism_med7.pptx
1) Amino acids are used primarily for protein synthesis rather than as an energy source. They can be used for energy only when carbohydrate and lipid availability is low.
2) Amino acids enter the body through digestion of proteins and are used for protein synthesis, specialized non-protein product synthesis, and as an energy source.
3) Excess amino acids are deaminated, producing ammonia which is converted to urea to prevent toxicity. Urea is synthesized in the liver through the urea cycle and excreted by the kidneys.
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1. Amino acids are obtained from digestion of dietary proteins, breakdown of body proteins, endogenous synthesis, and are used for synthesis of body proteins, non-protein specialized products, and as an energy source.
2. Amino acids are broken down into ammonia and carbon skeletons. Ammonia is converted to urea in the urea cycle to prevent toxicity, while carbon skeletons can be used for gluconeogenesis or ketogenesis.
3. Some amino acids are essential in the diet while others can be synthesized endogenously. Disorders of amino acid metabolism can occur if enzymes are deficient, leading to accumulation of intermediates.
Protein metabolism
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2. Proteins take on many forms in the body including enzymes, transporters, structural supports, and regulators. Protein turnover constantly synthesizes and degrades proteins.
3. Dietary proteins supply essential amino acids and are broken down into amino acids during digestion. Amino acids are absorbed and incorporated into tissues or oxidized to produce energy, ammonia, and ketone bodies.
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This document summarizes protein digestion and metabolism. It describes how proteins are broken down into peptides and amino acids via proteolytic enzymes in the stomach, pancreas, and intestines. The amino acids are then absorbed. Amino groups from amino acid catabolism form ammonia, which is detoxified to urea in the urea cycle in the liver to prevent toxicity. Disorders of this cycle can cause hyperammonemia. Blood urea levels indicate renal function, while urea is the main organic component excreted in urine.
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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.
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This document discusses protein metabolism, including essential and non-essential amino acids. Essential amino acids cannot be synthesized by the human body and must be obtained through diet. Non-essential amino acids can be synthesized from other amino acids or compounds. The document also outlines the processes of protein digestion, amino acid catabolism through transamination and the urea cycle, and analytical techniques for purifying and characterizing proteins like polyacrylamide gel electrophoresis and Edman degradation.
TOBIAS BIOSYNTHESIS OF AMINO ACIDS PRESENTATION.pptx
HUTCHISON’S
CLINICAL
METHODS
24th Edition
HUTCHISON’S
CLINICAL
METHODS
An integrated approach to clinical practice
Edited by
Michael Glynn MA MD FRCP FHEA
Consultant Physician, Gastroenterologist and Hepatologist
Barts Health NHS Trust;
Honorary Senior Lecturer
Barts and the London School of Medicine and Dentistry;
Former National Clinical Director for GI and Liver Diseases
NHS England
William M. Drake DM FRCP
Professor of Clinical Endocrinology
St Bartholomew’s Hospital
London, UK
Edinburgh London New York Oxford Philadelphia St Louis Sydney Toronto 2018
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AMINO ACIDS.pptx
The principle sources of protein are pulses, cereals, peas, beans and nuts and principle animal sources are milk and its products, meat, fish, liver, eggs etc.
Primarily proteins are hydrolyzed from polypeptides to dipeptides and then finally they are converted in amino acids and absorbed in gut.
Digestion of proteins begins in stomach and happens at different levels in GI tract by help of different digestive enzymes.
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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.
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Protein metabolism is a complex process involving protein turnover, nitrogen balance, amino acid pools, and the interconversion and catabolism of amino acids. Protein turnover occurs as proteins are constantly degraded and resynthesized at a rate of 150-300g/day in adults. Nitrogen balance measures nitrogen intake versus losses and can be positive, negative, or in equilibrium. The amino acid pool contains free amino acids distributed throughout body fluids. Amino acids undergo transamination, where the amino group is transferred between amino acids and keto acids, and oxidative deamination, where the amino group is removed as ammonia. Ammonia is metabolized through the urea cycle in the liver to form urea for excretion, or
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Amino acid metabolism
- 2. AMINO ACID METABOLISM BY MUHAMMAD HASEEB TARIQ
- 3. PROTEINS Proteins are formed of repeating units of Amino acids. Half of the body protein (collagen) is present in supportive tissue. Other half is present Intracellularly.
- 4. GENERAL CLASSIFICATION Amino Acids are classified in 3 categories: • Essential (Can’t be synthesized in body) • Non-Essential (Can be synthesized in body) • Semi-Essential Total amino acids are 20. Essential amino acids are 10.
- 5. AMINO ACID POOL Body contains 100g of protein present freely inside the body. This is amino acid pool. Amino acids of pool are in dynamic state. These participate in different metabolic reactions occurring in the body. CONTENTS: 50% of the pool is formed of : • Glutamate • Glutamine. 10% of pool is formed of Essential amino acids.
- 6. SOURCES: • Protein turnover • Ingestion PROTEIN TURNOVER: The amount of protein degraded and synthesized constantly in the body is called as protein turnover (300-400g).
- 7. Factors: • Ubiquitin tags a protein and increase its degradation. • Amino acid sequence of Proline , Glutamine , Serine and Threonine increases the degradation. Above factors are responsible for affecting Protein turnover.
- 8. INGESTION: • 30-50g protein is daily lost. • RDA for proteins is 1g/kg body weight/day. • Excess amino acids are not stored in body.
- 9. GENRAL ASPECTS OF AMINO ACID METABOLISM Amino acids undergo 2 steps along metabolism. These are: • Transamination • Deamination
- 10. TRANSAMINATION Definition: The transfer of an amino group (-NH2 ) from an amino acid to a keto acid is known as Transamination.
- 11. Features: • The reaction is catalysed by transaminases. • All reactions require PLP derivative of B6. • No free NH3 is liberated, just transfer occurs.
- 12. • Excess amino acids are diverted to generate energy. • Nitrogen is finally concentrated in Glutamate. • Only Glutamate undergoes oxidative deamination to liberate ammonia. • Serum transaminases can be used for diagnostic and prognostic purposes.
- 13. MECHANISM OF TRANSAMINATION PING PONG BI BI MODEL:
- 14. • Amino group is transferred to Pyridoxal phosphate converting it to Pyridoxamine phosphate. • Amino group is transferred to a keto acid converting Pyridoxamine phosphate to Pyridoxal phosphate. • During the reactions there is formation of Schiff base.
- 16. DEAMINATION Definition: The removal of amino group as NH3 is called as Deamination. Mostly it occurs in: • Liver • Kidneys
- 17. Deamination is of 2 types: • Oxidative deamination (coupled with oxidation) • Non-oxidative deamination
- 18. OXIDATIVE DEAMINATION Glutamate acts as a collection centre for amino groups. Deamination requires enzyme Glutamate Dehydrogenase (GDH). It is inhibited by ATP, GTP and allosterically activated by ADP, GDP. Amino acid oxidases can also cause deamination. GDH: Zn containing enzyme. 6 identical subunits. Molecular wt. 56000 each.
- 19. EFFECT OF PROTEIN RICH MEAL: After ingestion of protein rich meal glutamate level is increased, which leads to increased levels of NH3 in body.
- 20. AMINO ACID OXIDASES: These are flavo proteins, possessing FMN and FAD. Activity of L-amino acid oxidases is low than D-amino acid oxidases. Hydrogen peroxide is produced in these reactions which is then acted upon by Catalase.
- 21. NON-OXIDATIVE DEAMINATION Following enzymes cause it : • Dehydratase (acts on Serine, Threonine , Homoserine) • Desulfhydrases (acts on Cystein , Homocystein) • Histidase (acts on histidine)
- 22. THANK YOU!