deamination - sayali jagtap.pdf
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This document summarizes different pathways for deamination of amino acids. It discusses oxidative deamination, which involves the liberation of ammonia from amino acids coupled with oxidation. This can occur via glutamate dehydrogenase or amino acid oxidases. It also discusses non-oxidative deamination of serine and threonine via the enzymes serine dehydratase and threonine dehydratase. Deamination pathways play important roles in amino acid catabolism and the regulation of nitrogen and amino acid levels.
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Transamination & Deamination
The document summarizes amino acid metabolism through transamination and deamination. It discusses:
1) Transamination is the transfer of an amino group from an amino acid to a ketoacid, catalyzed by transaminases and involving the cofactor PLP. This converts the amino acid to a keto acid.
2) Most amino acids then undergo oxidative deamination through a coupled reaction of transamination and oxidative deamination. This releases ammonia for urea synthesis.
3) Glutamate acts as a collection center for amino groups and undergoes oxidative deamination by glutamate dehydrogenase in the liver mitochondria to liberate ammonia.
GENERAL REACTIONS OF AMINO ACIDS vnd.ms-powerpoint&rendition=1-5.ppt
i. Transamination is the exchange of the alpha amino group between one alpha amino acid and another alpha keto acid, forming a new alpha amino acid. This reaction helps synthesize non-essential amino acids and interconvert amino acids.
ii. The amino group is removed from most amino acids through a coupled reaction of transamination and oxidative deamination. This releases ammonia, which is detoxified in the liver by conversion to urea.
iii. Only liver mitochondria contain the enzyme glutamate dehydrogenase, which finally deaminates glutamate produced from other amino acids, releasing ammonia. This pathway allows for the deamination of all amino acids.
METABOLISM OF PROTEINS AND AMINO ACIDS
Protein metabolism denotes the various biochemical processes responsible for the synthesis of proteins and amino acids (anabolism), and the breakdown of proteins by catabolism. ... In humans, non-essential amino acids are synthesized from intermediates in major metabolic pathways such as the Citric Acid Cycle.
Amino acid metabolism...................
The document summarizes amino acid metabolism. Key points:
1. Amino acids undergo transamination and deamination to generate ammonia for urea synthesis and produce keto acids that can be used for energy, glucose synthesis, or fat/ketone body formation.
2. Transamination involves transferring amino groups between amino acids and keto acids using transaminases. This redistributes amino groups and produces non-essential amino acids.
3. Glutamate is a central amino acid that receives amino groups via transamination and releases ammonia via oxidative deamination by glutamate dehydrogenase, linking amino acid and TCA cycle metabolism.
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.
amino acids
The document discusses amino acids, which are molecules that contain an amine group, a carboxylic acid group, and a side chain. There are 22 standard amino acids that are incorporated into proteins, as well as non-standard amino acids. Amino acids join together to form peptides or longer protein chains. Methods for synthesizing alpha-amino acids include amination reactions, Gabriel synthesis, Strecker synthesis, resolution of racemic mixtures, and the Petasis reaction. Amino acids undergo various reactions including esterification, acylation, and the ninhydrin reaction.
8402594 pm.ppt metabolism of amino acids
PLP (pyridoxal phosphate) is the active coenzyme form of vitamin B6. It acts as a cofactor for many transamination and decarboxylation reactions involved in amino acid metabolism.
A deficiency of PLP can cause microcytic hypochromic anemia because it impairs the metabolism of the amino acid glycine. Glycine is required as a precursor for the synthesis of heme, which is the iron-containing prosthetic group of hemoglobin. Without sufficient heme production, red blood cell maturation is disrupted, resulting in microcytic (small) and hypochromic (pale) red blood cells characteristic of iron-deficiency anemia. So in summary, PLP deficiency leads to impaired gly
TRANSAMINATION
This document discusses amino acid metabolism, including:
- Transamination is one of the central reactions, where an amino group is transferred between amino acids via alpha-keto acids using aminotransferase enzymes and pyridoxal phosphate as a cofactor.
- The liver, kidneys, and muscles play key roles in amino acid metabolism. The liver catalyzes the catabolism of most amino acids and incorporates nitrogen into urea for excretion.
- There are specific transaminases for different amino acids, such as aspartate transaminase and alanine transaminase, which transfer amino groups between specific amino acids and alpha-ketoglutarate.
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Transamination & Deamination
The document summarizes amino acid metabolism through transamination and deamination. It discusses:
1) Transamination is the transfer of an amino group from an amino acid to a ketoacid, catalyzed by transaminases and involving the cofactor PLP. This converts the amino acid to a keto acid.
2) Most amino acids then undergo oxidative deamination through a coupled reaction of transamination and oxidative deamination. This releases ammonia for urea synthesis.
3) Glutamate acts as a collection center for amino groups and undergoes oxidative deamination by glutamate dehydrogenase in the liver mitochondria to liberate ammonia.
GENERAL REACTIONS OF AMINO ACIDS vnd.ms-powerpoint&rendition=1-5.ppt
i. Transamination is the exchange of the alpha amino group between one alpha amino acid and another alpha keto acid, forming a new alpha amino acid. This reaction helps synthesize non-essential amino acids and interconvert amino acids.
ii. The amino group is removed from most amino acids through a coupled reaction of transamination and oxidative deamination. This releases ammonia, which is detoxified in the liver by conversion to urea.
iii. Only liver mitochondria contain the enzyme glutamate dehydrogenase, which finally deaminates glutamate produced from other amino acids, releasing ammonia. This pathway allows for the deamination of all amino acids.
METABOLISM OF PROTEINS AND AMINO ACIDS
Protein metabolism denotes the various biochemical processes responsible for the synthesis of proteins and amino acids (anabolism), and the breakdown of proteins by catabolism. ... In humans, non-essential amino acids are synthesized from intermediates in major metabolic pathways such as the Citric Acid Cycle.
Amino acid metabolism...................
The document summarizes amino acid metabolism. Key points:
1. Amino acids undergo transamination and deamination to generate ammonia for urea synthesis and produce keto acids that can be used for energy, glucose synthesis, or fat/ketone body formation.
2. Transamination involves transferring amino groups between amino acids and keto acids using transaminases. This redistributes amino groups and produces non-essential amino acids.
3. Glutamate is a central amino acid that receives amino groups via transamination and releases ammonia via oxidative deamination by glutamate dehydrogenase, linking amino acid and TCA cycle metabolism.
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.
amino acids
The document discusses amino acids, which are molecules that contain an amine group, a carboxylic acid group, and a side chain. There are 22 standard amino acids that are incorporated into proteins, as well as non-standard amino acids. Amino acids join together to form peptides or longer protein chains. Methods for synthesizing alpha-amino acids include amination reactions, Gabriel synthesis, Strecker synthesis, resolution of racemic mixtures, and the Petasis reaction. Amino acids undergo various reactions including esterification, acylation, and the ninhydrin reaction.
8402594 pm.ppt metabolism of amino acids
PLP (pyridoxal phosphate) is the active coenzyme form of vitamin B6. It acts as a cofactor for many transamination and decarboxylation reactions involved in amino acid metabolism.
A deficiency of PLP can cause microcytic hypochromic anemia because it impairs the metabolism of the amino acid glycine. Glycine is required as a precursor for the synthesis of heme, which is the iron-containing prosthetic group of hemoglobin. Without sufficient heme production, red blood cell maturation is disrupted, resulting in microcytic (small) and hypochromic (pale) red blood cells characteristic of iron-deficiency anemia. So in summary, PLP deficiency leads to impaired gly
TRANSAMINATION
This document discusses amino acid metabolism, including:
- Transamination is one of the central reactions, where an amino group is transferred between amino acids via alpha-keto acids using aminotransferase enzymes and pyridoxal phosphate as a cofactor.
- The liver, kidneys, and muscles play key roles in amino acid metabolism. The liver catalyzes the catabolism of most amino acids and incorporates nitrogen into urea for excretion.
- There are specific transaminases for different amino acids, such as aspartate transaminase and alanine transaminase, which transfer amino groups between specific amino acids and alpha-ketoglutarate.
3.TRANSAMINATION.pptx
This document discusses the metabolism of amino acids. It begins by outlining common reactions like transamination and deamination that amino acids undergo to release ammonia. Transamination involves the transfer of amino groups between amino acids and keto acids, allowing for interconversion. Deamination results in the liberation of ammonia, which is used to synthesize urea via the urea cycle in the liver. The carbon skeletons of amino acids are converted to keto acids that can be used for energy production, glucose synthesis, or formation of fats/ketone bodies. The document then goes into more detail about specific processes involved in amino acid metabolism, including transamination, deamination, decarboxylation, the urea cycle,
CC 8 SEM 4 AMINO ACID METABOLISM.pdf Shilpa Dutta
The document discusses amino acid metabolism. It covers:
1) Transamination is the transfer of an amino group between amino acids and keto acids using pyridoxal phosphate as a cofactor. This reaction converts non-essential amino acids and diverts excess amino acids to energy production.
2) Glutamate undergoes oxidative deamination to liberate ammonia for urea synthesis. Urea synthesis involves carbamoyl phosphate synthase I catalyzing the first step.
3) Methionine is activated to form S-adenosylmethionine, which donates methyl groups in transmethylation reactions like cysteine synthesis from homocysteine and serine.
Amines 2
1. The document discusses the nomenclature, physical properties, structure, basicity, and reactions of primary, secondary, and tertiary amines. It covers topics such as IUPAC nomenclature, hydrogen bonding abilities, inversion of chiral amines, relative basicities, and reactions including oxidation, diazotization, and coupling reactions.
2. Amines can undergo a variety of reactions due to the lone pair on the nitrogen atom, including acting as a base or nucleophile. Reactions covered include oxidation, diazotization with nitrous acid, coupling reactions, and eliminations.
3. The document provides examples of amine syntheses such as reductive amination and
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Fate of Glucogenic and Ketogenic amino acid
Amino acid are the currency of of nitrogen and protein economy of the host, hence they are used in many pathways beyond protein synthesis, including energy production and neurotransmitter synthesis.
All amino acid are comprised of an amino group and a carbon skeleton. During metabolism these two parts are separated as they have different ‘fates’
Of the liberated amino acid approximately 75% are utilized while remainder serve as precursors for important biological compound and those not utilized are degraded to amphibolic intermediates
The pathway of amino acid catabolism is quite similar in most organism
Deamination and transamination
This document discusses deamination and transamination processes in the liver and other tissues. Deamination is the removal of amino groups from amino acids, producing ammonia (NH3). There are two types - oxidative deamination which is coupled to other reactions, and non-oxidative deamination which directly produces NH3. Transamination is the transfer of amino groups between amino acids and keto acids, catalyzed by transaminase enzymes using pyridoxal phosphate as a cofactor. This allows for interconversion and redistribution of amino acids as well as the production of ketone bodies from amino acids for energy production. Both deamination and transamination play important roles in amino acid catabolism and anabolism.
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.
Protein and amino acids metabolism in the body
This document summarizes protein metabolism and the catabolism of amino acids. It discusses nitrogen balance, amino acid pools, and the three main stages of amino acid catabolism. The first stage involves the removal of the alpha-amino group via transamination or deamination. The second stage is the disposal of ammonia in the liver via the urea cycle. The third stage is the breakdown of the remaining carbon skeleton via the citric acid cycle. Key processes like transamination, deamination, the urea cycle, and the fates of various carbon skeletons are explained in detail. Metabolic disorders and regulation of the urea cycle are also summarized.
Ammonia metabolism
Ammonia is produced through the metabolism of amino acids and nitrogenous compounds and exists as NH4+ ions at physiological pH. It is transported and stored as glutamine, which can be converted back to ammonia and glutamate. The liver plays a key role in ammonia disposal through the urea cycle, where ammonia and aspartate are converted to urea and fumarate in a 5-step process. Elevated ammonia is toxic and can cause neurological issues if not properly eliminated as urea through the kidneys. Genetic defects in the urea cycle can lead to hyperammonemia.
خصائص الاحماض الامينية
This document discusses the properties and characteristics of amino acids. It covers their ionic properties, isoelectric points, optical activity, solubility, UV absorption, and various chemical reactions including esterification, acylation, alkylation, reactions with carbonyl compounds, and reactions involving functional groups like cysteine and methionine. It notes that amino acids are important in developing flavors and aromas in foods during high-temperature cooking methods like frying and baking.
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Chemistry of amino acids
Amino acids are the building blocks of proteins. There are 20 standard amino acids that make up proteins. Amino acids have a general structure that includes an amino group, a carboxyl group, and a side chain. They can be classified based on their structure, side chain properties, nutritional requirements, and metabolic fate. Common properties of amino acids include being crystalline solids, existing as zwitterions with an isoelectric point, and having chirality with L and D isomers. Amino acids undergo various reactions due to their amino, carboxyl, and side chain groups.
Amino acid metabolism 1.pdf
The document summarizes amino acid metabolism. It discusses how proteins are broken down into individual amino acids, which then undergo various reactions like transamination and deamination. Transamination involves transferring the amino group from an amino acid to a keto acid. Deamination removes the amino group as ammonia. The carbon skeleton is used for energy production, glucose synthesis, or fat/ketone body formation. Ammonia is converted to urea in the urea cycle in the liver to allow excretion. Deficiencies in urea cycle enzymes can cause metabolic disorders.
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Transamination, deamination, and decarboxylation are the three main reactions in amino acid metabolism. Transamination involves transferring the amino group from an amino acid to α-ketoglutarate, catalyzed by a transaminase, forming a new amino acid (usually glutamate) and α-keto acid. Glutamate can then donate its amino group for biosynthesis or have its amino group removed by oxidative deamination via glutamate dehydrogenase into α-ketoglutarate and ammonium, providing α-ketoglutarate for further transamination reactions. This process funnels amino nitrogen into glutamate and ultimately results in its removal as ammonium, a form excreted from the body.
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.
transamination.pptx
1. Transamination is the transfer of an amino group from one amino acid to another, catalyzed by transaminase enzymes. This allows for the interconversion of amino acids.
2. Glutamate acts as a major amino group acceptor in transamination reactions. The amino group is transferred from an amino acid to α-ketoglutarate to form glutamate, and from glutamate to oxaloacetate to form aspartate.
3. Transamination requires pyridoxal phosphate as a cofactor and allows for the redistribution of amino groups and production of nonessential amino acids from essential ones. It is a reversible process that occurs in two stages involving the transfer of the amino group to and
PM.pptx
Transamination is the transfer of amino groups between amino acids and alpha-keto acids, catalyzed by transaminases using pyridoxal phosphate as a cofactor. The liver is the main site of transamination, which makes amino groups available for disposal as ammonia. Ammonia is produced through deamination, either oxidative or non-oxidative, and is toxic, so the first line of defense is trapping it as glutamine for transport to the liver. In the liver, glutamate dehydrogenase catalyzes deamination of glutamate to ammonia and alpha-ketoglutarate. Finally, urea is formed and excreted to dispose of ammonia non-toxically.
Chapters 18 , 22 - Biochemistry
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Class 4 reactions of 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.
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.
Amino acid metabolism_digestion & absorption.pdf
(1) Protein digestion involves proteolytic enzymes that break proteins into smaller peptides and amino acids in the stomach and small intestine. (2) Amino acids are absorbed into the bloodstream and transported to tissues via three main mechanisms. (3) Within cells, amino acids undergo various reactions including transamination, oxidative and non-oxidative deamination, and transmethylation and trans-sulfuration. (4) Ammonia is a byproduct of amino acid metabolism and is shuttled to the liver where it is converted to urea to be excreted.
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This document discusses the metabolism of amino acids. It begins by outlining common reactions like transamination and deamination that amino acids undergo to release ammonia. Transamination involves the transfer of amino groups between amino acids and keto acids, allowing for interconversion. Deamination results in the liberation of ammonia, which is used to synthesize urea via the urea cycle in the liver. The carbon skeletons of amino acids are converted to keto acids that can be used for energy production, glucose synthesis, or formation of fats/ketone bodies. The document then goes into more detail about specific processes involved in amino acid metabolism, including transamination, deamination, decarboxylation, the urea cycle,
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1) Transamination is the transfer of an amino group between amino acids and keto acids using pyridoxal phosphate as a cofactor. This reaction converts non-essential amino acids and diverts excess amino acids to energy production.
2) Glutamate undergoes oxidative deamination to liberate ammonia for urea synthesis. Urea synthesis involves carbamoyl phosphate synthase I catalyzing the first step.
3) Methionine is activated to form S-adenosylmethionine, which donates methyl groups in transmethylation reactions like cysteine synthesis from homocysteine and serine.
Amines 2
1. The document discusses the nomenclature, physical properties, structure, basicity, and reactions of primary, secondary, and tertiary amines. It covers topics such as IUPAC nomenclature, hydrogen bonding abilities, inversion of chiral amines, relative basicities, and reactions including oxidation, diazotization, and coupling reactions.
2. Amines can undergo a variety of reactions due to the lone pair on the nitrogen atom, including acting as a base or nucleophile. Reactions covered include oxidation, diazotization with nitrous acid, coupling reactions, and eliminations.
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zoo assignment.pptx
Fate of Glucogenic and Ketogenic amino acid
Amino acid are the currency of of nitrogen and protein economy of the host, hence they are used in many pathways beyond protein synthesis, including energy production and neurotransmitter synthesis.
All amino acid are comprised of an amino group and a carbon skeleton. During metabolism these two parts are separated as they have different ‘fates’
Of the liberated amino acid approximately 75% are utilized while remainder serve as precursors for important biological compound and those not utilized are degraded to amphibolic intermediates
The pathway of amino acid catabolism is quite similar in most organism
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This document discusses deamination and transamination processes in the liver and other tissues. Deamination is the removal of amino groups from amino acids, producing ammonia (NH3). There are two types - oxidative deamination which is coupled to other reactions, and non-oxidative deamination which directly produces NH3. Transamination is the transfer of amino groups between amino acids and keto acids, catalyzed by transaminase enzymes using pyridoxal phosphate as a cofactor. This allows for interconversion and redistribution of amino acids as well as the production of ketone bodies from amino acids for energy production. Both deamination and transamination play important roles in amino acid catabolism and anabolism.
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.
Protein and amino acids metabolism in the body
This document summarizes protein metabolism and the catabolism of amino acids. It discusses nitrogen balance, amino acid pools, and the three main stages of amino acid catabolism. The first stage involves the removal of the alpha-amino group via transamination or deamination. The second stage is the disposal of ammonia in the liver via the urea cycle. The third stage is the breakdown of the remaining carbon skeleton via the citric acid cycle. Key processes like transamination, deamination, the urea cycle, and the fates of various carbon skeletons are explained in detail. Metabolic disorders and regulation of the urea cycle are also summarized.
Ammonia metabolism
Ammonia is produced through the metabolism of amino acids and nitrogenous compounds and exists as NH4+ ions at physiological pH. It is transported and stored as glutamine, which can be converted back to ammonia and glutamate. The liver plays a key role in ammonia disposal through the urea cycle, where ammonia and aspartate are converted to urea and fumarate in a 5-step process. Elevated ammonia is toxic and can cause neurological issues if not properly eliminated as urea through the kidneys. Genetic defects in the urea cycle can lead to hyperammonemia.
خصائص الاحماض الامينية
This document discusses the properties and characteristics of amino acids. It covers their ionic properties, isoelectric points, optical activity, solubility, UV absorption, and various chemical reactions including esterification, acylation, alkylation, reactions with carbonyl compounds, and reactions involving functional groups like cysteine and methionine. It notes that amino acids are important in developing flavors and aromas in foods during high-temperature cooking methods like frying and baking.
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Amino acid metabolism 1.pdf
The document summarizes amino acid metabolism. It discusses how proteins are broken down into individual amino acids, which then undergo various reactions like transamination and deamination. Transamination involves transferring the amino group from an amino acid to a keto acid. Deamination removes the amino group as ammonia. The carbon skeleton is used for energy production, glucose synthesis, or fat/ketone body formation. Ammonia is converted to urea in the urea cycle in the liver to allow excretion. Deficiencies in urea cycle enzymes can cause metabolic disorders.
13315997.ppt
Transamination, deamination, and decarboxylation are the three main reactions in amino acid metabolism. Transamination involves transferring the amino group from an amino acid to α-ketoglutarate, catalyzed by a transaminase, forming a new amino acid (usually glutamate) and α-keto acid. Glutamate can then donate its amino group for biosynthesis or have its amino group removed by oxidative deamination via glutamate dehydrogenase into α-ketoglutarate and ammonium, providing α-ketoglutarate for further transamination reactions. This process funnels amino nitrogen into glutamate and ultimately results in its removal as ammonium, a form excreted from the body.
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.
transamination.pptx
1. Transamination is the transfer of an amino group from one amino acid to another, catalyzed by transaminase enzymes. This allows for the interconversion of amino acids.
2. Glutamate acts as a major amino group acceptor in transamination reactions. The amino group is transferred from an amino acid to α-ketoglutarate to form glutamate, and from glutamate to oxaloacetate to form aspartate.
3. Transamination requires pyridoxal phosphate as a cofactor and allows for the redistribution of amino groups and production of nonessential amino acids from essential ones. It is a reversible process that occurs in two stages involving the transfer of the amino group to and
PM.pptx
Transamination is the transfer of amino groups between amino acids and alpha-keto acids, catalyzed by transaminases using pyridoxal phosphate as a cofactor. The liver is the main site of transamination, which makes amino groups available for disposal as ammonia. Ammonia is produced through deamination, either oxidative or non-oxidative, and is toxic, so the first line of defense is trapping it as glutamine for transport to the liver. In the liver, glutamate dehydrogenase catalyzes deamination of glutamate to ammonia and alpha-ketoglutarate. Finally, urea is formed and excreted to dispose of ammonia non-toxically.
Chapters 18 , 22 - Biochemistry
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18 : Amino acid oxidation and production of urea
22: nitrogen Assimilation
Class 4 reactions of 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.
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.
Amino acid metabolism_digestion & absorption.pdf
(1) Protein digestion involves proteolytic enzymes that break proteins into smaller peptides and amino acids in the stomach and small intestine. (2) Amino acids are absorbed into the bloodstream and transported to tissues via three main mechanisms. (3) Within cells, amino acids undergo various reactions including transamination, oxidative and non-oxidative deamination, and transmethylation and trans-sulfuration. (4) Ammonia is a byproduct of amino acid metabolism and is shuttled to the liver where it is converted to urea to be excreted.
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Presentation given at the official farewell of Prof Ken Gillet at Wageningen on 13 June 2024
Anti-Universe And Emergent Gravity and the Dark Universe
Recent theoretical progress indicates that spacetime and gravity emerge together from the entanglement structure of an underlying microscopic theory. These ideas are best understood in Anti-de Sitter space, where they rely on the area law for entanglement entropy. The extension to de Sitter space requires taking into account the entropy and temperature associated with the cosmological horizon. Using insights from string theory, black hole physics and quantum information theory we argue that the positive dark energy leads to a thermal volume law contribution to the entropy that overtakes the area law precisely at the cosmological horizon. Due to the competition between area and volume law entanglement the microscopic de Sitter states do not thermalise at sub-Hubble scales: they exhibit memory effects in the form of an entropy displacement caused by matter. The emergent laws of gravity contain an additional ‘dark’ gravitational force describing the ‘elastic’ response due to the entropy displacement. We derive an estimate of the strength of this extra force in terms of the baryonic mass, Newton’s constant and the Hubble acceleration scale a0 = cH0, and provide evidence for the fact that this additional ‘dark gravity force’ explains the observed phenomena in galaxies and clusters currently attributed to dark matter.
Quality assurance B.pharm 6th semester BP606T UNIT 5
Warehousing
Good warehousing practices
Material management
11.1 Role of physical biological in deterioration of grains.pdf
Storagedeteriorationisanyformoflossinquantityandqualityofbio-materials.
Themajorcausesofdeteriorationinstorage
•Physical
•Biological
•Mechanical
•Chemical
Storageonlypreservesquality.Itneverimprovesquality.
Itisadvisabletostartstoragewithqualityfoodproduct.Productwithinitialpoorqualityquicklydepreciates
MICROBIAL INTERACTION PPT/ MICROBIAL INTERACTION AND THEIR TYPES // PLANT MIC...
MICROBIAL INTERACTION PPT/ MICROBIAL INTERACTION AND THEIR TYPES // PLANT MIC...ABHISHEK SONI NIMT INSTITUTE OF MEDICAL AND PARAMEDCIAL SCIENCES , GOVT PG COLLEGE NOIDA
Microbial interaction
Microorganisms interacts with each other and can be physically associated with another organisms in a variety of ways.
One organism can be located on the surface of another organism as an ectobiont or located within another organism as endobiont.
Microbial interaction may be positive such as mutualism, proto-cooperation, commensalism or may be negative such as parasitism, predation or competition
Types of microbial interaction
Positive interaction: mutualism, proto-cooperation, commensalism
Negative interaction: Ammensalism (antagonism), parasitism, predation, competition
I. Mutualism:
It is defined as the relationship in which each organism in interaction gets benefits from association. It is an obligatory relationship in which mutualist and host are metabolically dependent on each other.
Mutualistic relationship is very specific where one member of association cannot be replaced by another species.
Mutualism require close physical contact between interacting organisms.
Relationship of mutualism allows organisms to exist in habitat that could not occupied by either species alone.
Mutualistic relationship between organisms allows them to act as a single organism.
Examples of mutualism:
i. Lichens:
Lichens are excellent example of mutualism.
They are the association of specific fungi and certain genus of algae. In lichen, fungal partner is called mycobiont and algal partner is called
II. Syntrophism:
It is an association in which the growth of one organism either depends on or improved by the substrate provided by another organism.
In syntrophism both organism in association gets benefits.
Compound A
Utilized by population 1
Compound B
Utilized by population 2
Compound C
utilized by both Population 1+2
Products
In this theoretical example of syntrophism, population 1 is able to utilize and metabolize compound A, forming compound B but cannot metabolize beyond compound B without co-operation of population 2. Population 2is unable to utilize compound A but it can metabolize compound B forming compound C. Then both population 1 and 2 are able to carry out metabolic reaction which leads to formation of end product that neither population could produce alone.
Examples of syntrophism:
i. Methanogenic ecosystem in sludge digester
Methane produced by methanogenic bacteria depends upon interspecies hydrogen transfer by other fermentative bacteria.
Anaerobic fermentative bacteria generate CO2 and H2 utilizing carbohydrates which is then utilized by methanogenic bacteria (Methanobacter) to produce methane.
ii. Lactobacillus arobinosus and Enterococcus faecalis:
In the minimal media, Lactobacillus arobinosus and Enterococcus faecalis are able to grow together but not alone.
The synergistic relationship between E. faecalis and L. arobinosus occurs in which E. faecalis require folic acid
Holsinger, Bruce W. - Music, body and desire in medieval culture [2001].pdf
Music and Medieval History
Mechanisms and Applications of Antiviral Neutralizing Antibodies - Creative B...
Neutralizing antibodies, pivotal in immune defense, specifically bind and inhibit viral pathogens, thereby playing a crucial role in protecting against and mitigating infectious diseases. In this slide, we will introduce what antibodies and neutralizing antibodies are, the production and regulation of neutralizing antibodies, their mechanisms of action, classification and applications, as well as the challenges they face.
Discovery of An Apparent Red, High-Velocity Type Ia Supernova at 𝐳 = 2.9 wi...
We present the JWST discovery of SN 2023adsy, a transient object located in a host galaxy JADES-GS
+
53.13485
−
27.82088
with a host spectroscopic redshift of
2.903
±
0.007
. The transient was identified in deep James Webb Space Telescope (JWST)/NIRCam imaging from the JWST Advanced Deep Extragalactic Survey (JADES) program. Photometric and spectroscopic followup with NIRCam and NIRSpec, respectively, confirm the redshift and yield UV-NIR light-curve, NIR color, and spectroscopic information all consistent with a Type Ia classification. Despite its classification as a likely SN Ia, SN 2023adsy is both fairly red (
�
(
�
−
�
)
∼
0.9
) despite a host galaxy with low-extinction and has a high Ca II velocity (
19
,
000
±
2
,
000
km/s) compared to the general population of SNe Ia. While these characteristics are consistent with some Ca-rich SNe Ia, particularly SN 2016hnk, SN 2023adsy is intrinsically brighter than the low-
�
Ca-rich population. Although such an object is too red for any low-
�
cosmological sample, we apply a fiducial standardization approach to SN 2023adsy and find that the SN 2023adsy luminosity distance measurement is in excellent agreement (
≲
1
�
) with
Λ
CDM. Therefore unlike low-
�
Ca-rich SNe Ia, SN 2023adsy is standardizable and gives no indication that SN Ia standardized luminosities change significantly with redshift. A larger sample of distant SNe Ia is required to determine if SN Ia population characteristics at high-
�
truly diverge from their low-
�
counterparts, and to confirm that standardized luminosities nevertheless remain constant with redshift.
(June 12, 2024) Webinar: Development of PET theranostics targeting the molecu...
(June 12, 2024) Webinar: Development of PET theranostics targeting the molecu...Scintica Instrumentation
Targeting Hsp90 and its pathogen Orthologs with Tethered Inhibitors as a Diagnostic and Therapeutic Strategy for cancer and infectious diseases with Dr. Timothy Haystead.Alternate Wetting and Drying - Climate Smart Agriculture
Alternate Wetting and Drying - Climate Smart AgricultureInternational Food Policy Research Institute- South Asia Office
PPT on Alternate Wetting and Drying presented at the three-day 'Training and Validation Workshop on Modules of Climate Smart Agriculture (CSA) Technologies in South Asia' workshop on April 22, 2024. Recently uploaded (20)
Sexuality - Issues, Attitude and Behaviour - Applied Social Psychology - Psyc...
Sexuality - Issues, Attitude and Behaviour - Applied Social Psychology - Psyc...
Evidence of Jet Activity from the Secondary Black Hole in the OJ 287 Binary S...
Evidence of Jet Activity from the Secondary Black Hole in the OJ 287 Binary S...
Farming systems analysis: what have we learnt?.pptx
Farming systems analysis: what have we learnt?.pptx
Clinical periodontology and implant dentistry 2003.pdf
Clinical periodontology and implant dentistry 2003.pdf
Anti-Universe And Emergent Gravity and the Dark Universe
Anti-Universe And Emergent Gravity and the Dark Universe
Quality assurance B.pharm 6th semester BP606T UNIT 5
Quality assurance B.pharm 6th semester BP606T UNIT 5
11.1 Role of physical biological in deterioration of grains.pdf
11.1 Role of physical biological in deterioration of grains.pdf
MICROBIAL INTERACTION PPT/ MICROBIAL INTERACTION AND THEIR TYPES // PLANT MIC...
MICROBIAL INTERACTION PPT/ MICROBIAL INTERACTION AND THEIR TYPES // PLANT MIC...
Holsinger, Bruce W. - Music, body and desire in medieval culture [2001].pdf
Holsinger, Bruce W. - Music, body and desire in medieval culture [2001].pdf
Mechanisms and Applications of Antiviral Neutralizing Antibodies - Creative B...
Mechanisms and Applications of Antiviral Neutralizing Antibodies - Creative B...
Immunotherapy presentation from clinical immunology
Immunotherapy presentation from clinical immunology
Discovery of An Apparent Red, High-Velocity Type Ia Supernova at 𝐳 = 2.9 wi...
Discovery of An Apparent Red, High-Velocity Type Ia Supernova at 𝐳 = 2.9 wi...
(June 12, 2024) Webinar: Development of PET theranostics targeting the molecu...
(June 12, 2024) Webinar: Development of PET theranostics targeting the molecu...
Alternate Wetting and Drying - Climate Smart Agriculture
Alternate Wetting and Drying - Climate Smart Agriculture
deamination - sayali jagtap.pdf
- 1. DEAMINATION OF AMINO ACID Name – sayali Jagtap Roll no - 40
- 3. OXIDATIVE DEAMINATION • The liberation of free ammonia from amino group of amino acids,when coupled with oxidation known as oxidative deamination. • Site- mostly in liver and kidney
- 4. OXIDATIVE DEAMINATION BY GLUTAMATE DEHYDROGENASE • The alpha amino group of most amino acid are ultimately transferred to alpha ketoglutarate by transamination forming L-glutamate. • The L-glutamate undergoes oxidative deamination by the action of L –glutamate dehydrogenase to liberate ammonia. • It also requires NAD or NADP as an oxidizing agent. • Thus,net removal of alpha amino groups to ammonia requires the combined action of glutamate transaminase and glutamate dehydrogenase.
- 6. Metabolic significance • It is a reversible reaction . • Catabolically ,it channels nitrogen from glutamate to ammonia . • Anabolically it catalyzes animation of alpha ketoglutarate by free ammonia to form glutamate. • Regulation of glutamate dehydrogenase activity.
- 7. OXIDATIVE DEAMINATION BY AMINOACID OXIDASES • Oxidative deamination occur by both L-and D-amino acid OXIDASES. • Site – occur in kidney and liver. • Amino acid oxidases uses FMN or FAD as coenzyme • This coenzyme oxidize amino acids to an alpha imino acid .alpha imino acid is an unstable compound which decomposes to the corresponding alpha keto acid with release of ammonium ion . • In this reaction oxygen is reduced to hydrogen peroxide , which is later decomposed by catalase .
- 9. METABOLIC SIGNIFICANCE • L-amino acid oxidase plays minor role in amino acid catabolism. • Activity of D-amino acid oxidase is than that of L- amino acid oxidase • D-amino acid present in diet are metabolized by D – amino acid oxidase in liver.
- 10. NON-OXIDATIVE DEAMINATION BY AMINOACID DEHYDRATASE • The alpha amino groups of serine and threonine can be directly deaminated into ammonium ion,this are hydroxy amino acid . • Direct deamination,without oxidation • These direct deamination is catalyzed by serine dehydratase and threonine dehydratase in which pyridoxal phosphate (PLP) is the coenzyme .