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Amino Acids Pool Catabolic Pathways of Amino Acids 1- Transamination

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Amino Acids Pool Catabolic Pathways of Amino Acids 1- Transamination 1 Amino acids pool The amount of free amino acids distributed throughout the body is called amino acid pool. Plasma level for most amino acids varies widely throughout the day. It ranges between 4 –8 mg/dl. It tends to increase in the fed state and tends to decrease in the post absorptive state. Sources of amino acid pool 1.Dietary protein 2.Breakdown of tissue proteins 3.Biosynthesis of nonessential amino acids Fate of amino acid pool 1.Biosynthesis of structural proteins e.g. tissue proteins 2.Biosynthesis of functional proteins e.g. haemoglobin, myoglobin, protein hormones and enzymes 3- Biosynthesis of small peptides of biological importance e.g. glutathione, endorphins and enkephalins 4- Biosynthesis of non protein nitrogenous compounds (NPN) as urea, uric acid, creatine, creatinine and ammonia 5- Catabolism of amino acids to give ammonia and α-keto acids. Ammonia is transformed mainly into urea The α-keto acids that remain after removal of ammonia from amino acids are called the carbon skeleton. Catabolic pathways of amino acids 1.Transamination 2.Deamination 3.Transamidination 4.Transamidation 5.Decarboxylation 1- Transamination Transamination means transfer of amino group from α-amino acid to α-keto acid with formation of a new α-amino acid and a new α-keto acid. The liver is the main site for transamination. All amino acids can be transaminated except lysine, threonine, proline and hydroxy proline. All transamination reactions are reversible. It is catalyzed by aminotransferases (transaminases). It needs pyridoxal phosphate as a coenzyme. 2 α-amino acid α-keto acid Transaminase a new α-keto acid a new α-amino acid Role of pyridoxal phosphate in transamination Pyridoxal phosphate acts as an intermediate carrier for amino group Pyridoxal phosphate accepts the amino group from amino acid to form pyridoxamine phosphate, which in turn gives the amino group to α-keto acid α-amino acid Pyridoxal phosphate a new α-amino acid CHO NH NH 2 2 HO CH2 O P R COOH R COOH CH H3C 1 CH N Transaminases CH2-NH2 O O HO CH2 O P R COOH R1 C COOH C H3C N α -keto acid Pyridoxamine phosphate a new α-keto acid Examples of transaminases A. Alanine transaminase B. Aspartate transaminase C. Glutamate transaminase A. Alanine transaminase (ALT) • It is also called glutamic pyruvic transaminase (GPT). • It catalyzes the transfer of amino group from glutamic acid to pyruvic acid to form alanine and α-ketoglutaric acid. • It also catalyzes the reverse reaction. • It needs pyridoxal phosphate as a coenzyme. • It is present in the cytoplasm of liver cells. 3 Alanine Pyridoxal phosphate Glutamic acid COOH CHO HC NH2 NH 2 CH2 HO CH2 O P CH CH COOH CH 3 H3C 2 N COOH ALT (GPT) COOH O CH2-NH2 C O CH3 C COOH HO CH2 O P CH2 H3C N CH2 COOH Py ruvic acid Pyridoxamine phosphate α-ketoglutaric acid B. Aspartate transaminase (AST) • It is also called glutamic oxalacetic transaminase (GOT) • It catalyzes the transfer of amino group from glutamic acid to oxalacetic acid to form aspartic acid and α-ketoglutaric acid • It also catalyzes the reverse reaction • It needs pyridoxal phosphate as a coenzyme • It is present in liver, heart and skeletal muscle cells. • It is present in both cytoplasm and mitochondria Pyridoxal phosphate Glutamic acid Aspartic acid COOH HC NH2 CHO COOH CH2 HO CH O 2 P HC NH2 CH2 H3C N CH 2 COOH COOH AST (GOT) COOH COOH CH2-NH2 C O C O CH2 HO CH2 O P CH2 H3C CH2 N COOH COOH Oxalacetic acid Pyridoxamine phosphate α-ketoglutaric acid 4 C. Glutamate transaminase • It catalyzes the transfer of amino group from any amino acid (except lysine, threonine, proline and hydroxy proline) to α-ketoglutaric acid to form glutamic acid and the corresponding α-keto acid • It also catalyzes the reverse reaction • It needs pyridoxal phosphate as a coenzyme • It is widely distributed in all tissues Glutamic acid α- Amino acid Pyridoxal phosphate COOH HC NH CHO 2 CH NH 2 2 HO CH2 O P CH2 COOH H C R CH 3 N COOH Glutamate transaminase COOH CH2-NH2 O C O HO CH2 O P CH R C COOH 2 H C 3 CH N 2 α- Keto acid Pyridoxamine phosphate COOH α-ketoglutaric acid Clinical significance of serum transaminases Transaminases are intracellular enzymes. Their levels in blood plasma are low under normal conditions. ALT (GPT) is present mainly in the cytoplasm of liver cells. AST (GOT) is present in both cytoplasm and mitochondria in liver, heart and skeletal muscles. Any damage to these organs will increase the level of transaminases in blood In liver diseases, there is an increase in both serum ALT (SGPT) and AST (SGOT) levels. In acute liver diseases, e.g. acute viral hepatitis, the increase is more in SGPT In chronic liver diseases, e.g. liver cirrhosis the increase is more in SGOT. In heart diseases, e.g. myocardial infarction, there is an increase in SGOT only. In skeletal muscle diseases, e.g. myasthenia gravis, there is an increase in SGOT only. 3- Deamination Deamination means the removal of amino group from α-amino acid in the form of ammonia with formation of α-keto acid The liver and kidney are the main sites for deamination Deamination may be oxidative or non-oxidative 5 A. Oxidative deamination It is catalyzed by one of the following enzymes: 1- L-amino acid oxidases 2- D-amino acid oxidases 3- Glutamate dehydrogenase B. Non-oxidative deamination It is catalyzed by one of the following enzymes: 1- Dehydratases 2- Desulfhydrases A. Oxidative deamination 1- L amino acid oxidase • This enzyme is present in the liver and kidney. Its activity is low. • It is an aerobic dehydrogenase that needs FMN as a coenzyme. • It deaminates most of the naturally occurring L-amino acids L-amino acid oxidase L-amino acid oxidase O R COOH R COOH CH C R C COOH NH2 NH FMN FMNH2 H2 O NH3 L-amino acid α -imino acid α-keto acid 2- D amino acid oxidase • D- amino acids are present in plants and bacterial cell wall. • They are not used in protein biosynthesis in humans and animals. • D-amino acids are deaminated by D-amino acid oxidase resulting in ammonia and α-keto acids. • D-amino acid oxidase is present in the liver. • It is an aerobic dehydrogenase. • It needs FAD as a coenzyme. NH2 D-amino acid oxidase NH D-amino acid oxidase O R CH COOH R CH COOH R C COOH H2O NH3 FAD FADH2 D-amino acid α-imino acid α-keto acid 6 3-Glutamate dehydrogenase • This enzyme is present in most tissues • It is present both in cytoplasm and mitochondria • Its activity is high • It is an anaerobic dehydrogenase • It needs NAD or NADP as a coenzyme • It deaminates glutamic acid resulting in α-ketoglutaric acid and ammonia COOH COOH COOH HC NH2 C NH C O Glutamate dehydrogenase Glutamate dehydrogenase CH2 CH2 CH2 CH 2 CH2 CH2 H2O NH NAD NADH+H+ 3 COOH COOH COOH Glutamic acid α-iminoglutaric acid α-ketoglutaric acid B.Non-oxidative deamination 1-Dehydratase This enzyme deaminates amino acids containing hydroxyl group e.g. serine, homoserine and threonine. It needs pyridoxal phosphate as coenzyme. OH NH2 Serine dehydratase NH Serine dehydratase O CH2 CH COOH CH3 C COOH CH3 C COOH PLP H O NH H2O 2 3 Serine α-imino acid Pyruvic acid 2-Desulfhydrase This enzyme deaminates sulpher containing amino aids e.g. cysteine and cystine. It needs pyridoxal phosphate as a coenzyme. SH NH2 Desulfhydrase NH Desulfhydrase O CH CH COOH CH C COOH CH C COOH 2 3 3 PLP H2S H2O NH3 Cysteine α-imino acid Pyruvic acid 7 Most of the naturally occurring α–amino acids are catabolized by transamination with α– ketoglutaric acid followed by deamination of the produced glutamic acid, a condition called transdeamination α-ketoglutaric acid α -Amino acid COOH Ammonia C O NH 2 CH NH3 2 R CH COOH CH2 COOH Transaminases COOH Glutamate O dehydrogenase HC NH2 R C COOH CH2 CH 2 COOH Keto acid Glutamic acid α- 3-Transamidination Transamidination means the transfer of amidine group from a donor molecule to an acceptor molecule It is catalyzed by transamidinase enzyme An example of transmidination reaction is the transfer of amidine group from arginine (donor) to glycine (acceptor) in creatine biosynthesis NH2 HN C NH2 NH CH2 CH 2 CH 2 NH 2 CH Transamidinase HN 2 C + CH2 H2NCH 2 COOH + CH2 HN CH2 COOH HC NH2 HC NH 2 Glycine COOH COOH Guanidoacetic acid Arginine Ornithine 8 4-Transamidation Transamidation means transfer of amide group nitrogen from a donor molecule to an acceptor molecule It is catalyzed by transamidase enzyme Examples of transmidation reaction include: 1- Transfer of amide nitrogen from glutamine (donor) to fructose (acceptor) to form glucosamine 2-Amide group nitrogen of glutamine is the source of N3 and N9 in purine bases Glucosamine biosynthesis CH2OH CH2OH COOH COOH HC NH2 C O HC NH2 HC NH2 HOC H HO C H CH2 CH2 + + H C OH H C OH CH CH2 2 H C OH H C OH CO NH COOH 2 CH2 OH CH2 OH Glutamine Fructose Glutamic acid Glucosamine 5-Decarboxylation Decarboxylation means removal of CO2 from amino acid with formation of corresponding amines It is catalyzed by decarboxylase enzyme It needs pyridoxal phosphate as a coenzyme Examples of decarboxylation reaction include: 1. Decarboxylation of histidine to form histamine 2. Decarboxylation of tyrosine to form tyramine NH Decarboxylase 2 R CH COOH R CH2 NH2 PLP CO 2 Amine α -amino acid .
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