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1. Introduction 2. Synthesis of Amino acids: An Overview 3. Regulation by Feedback Inhibition 4. Significance of Amino Acids
Amino acids serve as the building blocks for proteins. In addition, they are the starting points for the synthesis of many important cellular molecules including vitamins and nucleotides. Amino acids are classified into two categories according to their availability: Essential amino acids – Those amino acids are obtained by the organisms through dietary sources Nonessential amino acids – Those acids that are synthesized by mammals. The basic twenty amino acids can be divided into two groups of amino acids each having ten. Ten are essential and the other ten are nonessential. Yet, this classification is not accurate, since there is an overlap between the two groups. • Nonessential amino acids include Alanine, Asparagine, Aspartate, Glutamate, Glutamine, Glycine, Cysteine, Serine, Proline and Tyrosine.
Tyrosine is is synthesized by the hydroxylation of phenylalanine which is an essential amino acid. Hence it is indeed included under essential amino acids. In animals, the essential amino acids methionine supplies the sulfhydryl group of cysteine and hence it can also be considered essential. • Essential amino acids include Arginine, Histidine, Lycine, Leucine, Isoleucine, Phenylalanine, Mehionine, Tryptophan, Valine and Threonine.
In mammals, Arginine is synthesized during the urea cycle, but most of it is hydrolyzed to urea and ornithine. As a result, sufficient arginine cannot be synthesized to meet the metabolic needs of infants and children and hence it is classified as an essential amino acid.
In the studies done on lower microorganisms like bacteria, it is revealed that they would rather use amino acids already available in their environment than synthesizing them from the scratch. It is based upon two important facts • • A significant amount of energy is necessary to create the enzymes for the pathway. Some of the reactions in amino acid biosynthetic pathway are highly energy consuming and the cell needs to feed this great energy input.
The amino acids synthesis pathways can be grouped into a number of consistent systems. Some of those systems share common mechanisms while some are characterized by the use of common enzymes that have the ability to synthesize more than one amino acid. Such systems can be classified into simple reactions, branch chain amino acids, aromatic amino acids, threonine/lysine, serine/glycine, and unique pathways. The three systems of ‘aromatic amino acids’, ‘threonine/lysine’ and ‘serine/glycine pathways’ possess a common beginning and then diverge to form the amino acid of interest. Each of these pathways begins with a central metabolite or some other molecules which are results of the major metabolic reactions inside the cell. This way of utilizing the common compounds instead of synthesizing them from scratch helps the cell to save energy. This also leads to gene conservation as only very few enzymes are needed to code for the pathways. Thus synthesis of amino acids is very critical for the survival of a cell. If the amino acids are synthesized from the scratch, then the genes that code for ‘amino acid synthesis enzymes’ and the ‘enzymes’ themselves are under tight control and are allowed to be turned on only when they are absolutely needed.
2. Synthesis of Amino acids: An Overview
Synthesis of Essential Amino Acids The synthetic pathways for the essential amino acids in lower organisms like plants and microorganisms are generally more complicated when compared to the pathways for nonessential amino acid synthesis. In addition to this, they are specific to particular species and makes use of the common metabolic precursors. Based upon the common precursors, essential amino acids can be grouped into 4 "families" as follows: Aspartate Family: lysine, threonine, methionine Pyruvate Family: leucine, isoleucine, valine Aromatic Family: phenylalanine, Tyrosine, Tryptophan Histidine
The amino acids synthesis pathways can be classified into simple reactions, serine/glycine, threonine/lysine, branch chain amino acids, aromatic amino acids, and unique pathways. Simple Reactions (Synthesis of nonessential amino acids) Almost in all the cases, the nonessential amino acids like alanine, aspartate, glutamate, glutamine, and asparagine and can be simply synthesized by a single step reactions from central metabolites. As they are simple in structure and also their synthesis is uncomplicated, these systems of synthesizing pathways are termed as ‘simple reactions’. All of the nonessential amino acids are synthesized from intermediates of major metabolic pathways. An exception to this is tyrosine since its immediate precursor phenylalanine is an essential amino acid. Transamination of α- ketoacids: The carbon skeletons of these amino acids are definite to their corresponding α ketoacids. Thus, it is possible to synthesize any of the nonessential amino acids directly by transaminating that amino acids to its corresponding α - ketoacid. In this case, the ketoacid should exist as a common intermediate. An amino group is transferred from an amino acid to α - carbon of a ketoacid, which is catalyzed by an aminotransferase is termed as a "transamination reaction". Three very common α – ketoacids can be transaminated to their corresponding amino acid in a single step reaction. Alanine synthesis: Several pathways can be followed for this synthesis and the most likely used is formation of alanine by transamination from glutamate onto pyruvate. Pyruvate (glycolytic end product) → alanine
A transamination using valine instead of glutamate is also feasible. Aspartate synthesis: Aspartate is synthesized by the transfer of an ammonia group from glutamate to oxaloacetate. Oxaloacetate (citric acid cycle intermediate) → aspartate Glutamate synthesis: Glutamate can be easily synthesized by the addition of ammonia to α - ketoglutarate. α - ketoglutarate (citric acid cycle intermediate) → glutamate Asparagine synthesis: Asparagine is made either by adding ammonia directly to aspartate or through transamination from glutamine.
In this reaction, AMP is used instead of ADP which helps to release more energy which is required to drive the synthesis. Glutamine synthesis: Glutamine is made by the addition of another ammonia molecule to glutamate.
These five are the basic reactions and the rest of the simple reactions employ transamination from glutamate or glutamine to a central metabolite in order to construct the required amino acid. Asparagine and glutamine are in fact the products resulted from the amidations of aspartate and glutamate, respectively. Hence, asparagines, glutamine, and the remaining nonessential amino acids are not directly the result of transamination of α ketoacids as these are not common intermediates of the other pathways. Even, the carbon skeletons of all of these can be traced back to a α - ketoacid. Aspartate is transaminated to asparagine in an ATP-dependent reaction catalyzed by asparagine synthetase. Here glutamine swerves as the amino group donor.
The synthesis of glutamine is a two-step reaction. Step 1: Glutamate is first "activated" to a α - glutamylphosphate intermediate Step 2: Phosphate group is displaced by NH3. Hence, it can be understood that Synthesis of asparagine is fundamentally coupled to that of glutamine Glutamine, being a storage form of NH3 acts as the amino group donor in the formation of numerous biosynthetic products Serine/glycine metabolic pathways Biosynthesis of serine and glycine constitute a major metabolic pathway. This pathway has a significant role in the formation of other amino acids and nucleic acids. Serine/Glycine metabolic pathway is an exergonic pathway in which energy is produced in the form of reduced NADH and does not require any energy input. The glycolytic intermediate, 3-phosphoglycerate, is the principal molecule which participates in this pathway and is converted to serine, cysteine and glycine.
Synthesis of serine: Step 1: Oxidation of 3-phosphoglycerate to form 3-phosphohydroxy pyruvate and NADH. Step 2: Formation of 3-phosphoserine by means of a transamination reaction with glutamate (donates the amino group) and serine is formed consequently by the removal of the phosphate.
Synthesis of Glycine: Glycine generation is done by the removal of methyl group from serine. Serine is converted to glycine as follows
serine hydroxymethyltransferase Serine + THF ⎯⎯⎯⎯⎯⎯⎯⎯⎯ →
glycine + N5,N10 -methylene-THF
Glycine is also formed in a condensation reaction of N5,N10 -methylene-THF as given in the following:
N5,N10 -methylene-THF + CO2 + NH4+ Synthesis of Cysteine:
glycine synthase + NADH ⎯⎯⎯⎯⎯⎯⎯→
Cysteine is synthesized from serine and homocysteine which is a breakdown product of methionine. Serine + homocysteine → cystathionine + H2O cystathionine + H2O → α-ketobutyrate + cysteine + NH3 Threonine/lysine metabolic pathyways Synthesis of threonine and lysine is basically a shared pathway Energy input includes one ATP and two NADPH + H+. Lysine, threonine and methionine belong to the Aspartate family. The first committed step for the synthesis of Lys, Met and Thr is the phosphorylation of aspartate into aspartyl-β-phosphate, catalyzed by aspartokinase: The bacterium E.coli has 3 isozymes of aspartokinase and those will respond differently to each of the 3 amino acids, considering the situations of enzyme inhibition and feedback inhibition. The pathway from aspartate to lysine included 10 steps. The pathway from aspartate to threonine has 5 steps The pathway from aspartate to methionine has 7 steps Synthesis of Threonine: Threonine biosynthesis constitutes three major steps. Step 1: Conversion of oxaloacetate into aspartate semialdehyde is the initial step of this pathway. Step 2: Homoserine is yielded by a second reduction with NADPH + H+. Step 3: The so formed homoserine is phosphorylated into homoserine phosphate by ATP and finally it is converted into threonine. Synthesis of Lysine: A general pathway is widely studied even the lysine pathways follows different reactions in different species of bacteria. Lysine synthesis involves Addition of pyruvate to aspartate semialdehyde Use of a CoA intermediate which may be either acetyl CoA or succinyl-CoA Addition of an amino group from glutamate.
Either the succinyl or acetyl group added from CoA serves as a blocking group by protecting the amino group from attack during transamination by glutamate. NADPH + H+ are required for reduction process in the second step of the pathway. Synthesis of methionine: In the major pathway which includes the synthesis of this group of 3 amino acids threonine, lysine and methionine, the important step in which homocysteine is converted to methionine is catalyzed by the enzyme methionine synthase. During this reaction, homocysteine is methylated to methionine, and the C1 donor is N5methyl-THF. Here occurs the transfer of a methyl group from N5-methyl-THF to homocysteine and so the enzyme catalyzing it is also termed as homocysteine methyltransferase. Here, the catalyzing enzyme is methionine synthase rather than the normal synthatases. The reaction involved here is a condensation reaction where ATP or any other nucleoside triphosphate (NTP) is not used as an energy source. In a synthetase enzyme, NTP is required as an energy source. Regulation of these three pathways occurs at the two branch points: 1. β-Aspartate-semialdehyde (by the feedback inhibition of homoserine and lysine) 2. Homoserine (by the feedback inhibition of threonine and methionine) Branch chain amino acids (Synthesis of Essential Amino Acids) Pyruvate family of the essential amino acids includes leucine, isoleucine and valine. All these three are the "branched chain" amino acids. They are able to be grouped under a single category since they all originate from the pyruvate carbon skeleton. The first step of the pathway is common to all the three amino acids: Pyruvate + TPP
⎯acetolactate synthase → ⎯ ⎯ ⎯ ⎯⎯
The central carbon atom in hydroxyethyl-TPP is a carbanion and it is stabilized by resonance forms. • • If this pathway leads to the formation of valine and isoleucine, then hydroxyethyl-TPP needs to react with another pyruvate to form αacetolactate. In case, if this pathway leads to the formation of isoleucine, it needs to react with α-ketobutyrate.
The intermediates the isoleucine pathway and the valine pathway are so similar since common enzymes catalyze four steps of each pathway.
The difference between the isoleucine pathway and the valine pathway is the substitution of an ethyl group instead of a methyl group to the α-carbon of the intermediates. Here the branch point lies at α-ketoisovalerate through which, in one direction leads to valine and, in the other, to leucine. Synthesis of Leucine: Biosynthesis of leucine involves the following steps: Initial step starts from the last intermediate of valine synthesis, αketoisovalerate. In the first step, Acetyl-CoA is used to add an acetyl group to the molecule. Electrons are transferred to NAD+ and one carbon is lost in the form of CO2 at the fourth step of the pathway. In the final step, the amine from glutamate is added to a-ketoisocaproate to form leucine. Isoleucine synthesis begins with threonine, which undergoes deamination to form αketobutyrate. Following this step, it involves a 4 step synthesis which requires one NADPH + H+ for the synthesis of each amino acid. The final step in the formation of each of these amino acids involves transamination reaction from glutamate to the corresponding α-ketoacid of each of the 3 branched-chain amino acids. Aromatic amino acids (Synthesis of Essential Amino Acids) Aromatic family of the essential amino acids includes tryptophan, phenylalanine and tyrosine. Synthesis of the aromatic amino acids begins with the synthesis of chorismate which is an important intermediate for many biosynthetic pathways. Erythrose 4-phosphate and Phosphoenol pyruvate serve as beginning substrates for this pathway. One NADPH + H+ needs to be fed and one ATP is extracted for every molecule of chorismate formed. Chorismate formation: The glycolytic intermediate Phosphoenolpyruvate (PEP), and a pentose-phosphate pathway intermediate erythrose-4-phosphate undergoes condensation reaction and results in the formation of 2-keto-3-deoxyarabinoheptulosonate-7-phosphate and inorganic phosphate.
This condensation reaction is catalyzed by the enzyme ‘synthase’. Finally the condensation product is cyclized to form chorismate.
From this chorismate formation, the branching of pathway starts. It ends up in the production of tryptophan at one branch end, and tyrosine and phenylalanine are formed at the other end. Glutamine serves as the amino group donor to chorismate and ends up in the formation of anthranilate at the tryptophan branch. Indole is the immediate precursor of tryptophan and the indole ring forms the characterizing feature of the tryptophan structure. Here serine is the donor of the amino group to indole and forms tryptophan. Another branch which leads towards tyrosine and phenylalanine formation has one more branch point at prephenate. The single difference between the resulting two amino acids is that the para carbon of the benzene ring of tyrosine is hydroxylated. In fact, in case of mammals, phenylalanine is directly hydroxylated to tyrosine, and the enzyme phenylalanine hydroxylase catalyses the reaction. Synthesis of Tryptophan Synthesis of Trytophan is complex and it involves five steps starting from chorismate formation.
Step 1: Glutamate donates an amine group in the first step of the pathway and pyruvate is lost from chorismate. Step 2, 3 4, and 5: In these steps, a ribose sugar is added and this finally contributes to the formation of a 5 membered ring of tryptophan. Step 6: Another phosphoenol pyruvate molecule is added to the growing molecule. Step 7: The last step of this pathway involves serine where it donates the carbon amino group of tryptophan. Energy is contributed to this process in the form of hydrolysis of pyrophosphate. This hydrolysis reaction serves to drive the addition of the ribose sugar in the second step of the reaction. Synthesis of Phenylalanine Conversion of chorismate into phenylpyruvate happens in two steps and phenylalanine is synthesized by a transamination reaction with glutamate. No energy input is required for these conversion reactions. Synthesis of Tyrosine Tyrosine is made by a similar transamination reaction as in the case of phenylalanine synthesis. Synthesis of tyrosine is very similar to the synthesis of phenylalanine, but the reactions are carried out by different enzymes under different regulatory control. NADH is created in the formation of 4-hydroxyphenylpyruvate. Active amines from tyrosine: Some very important physiologically active amines are derived from tyrosine, and these are L-DOPA, dopamine, norepinephrine and epinephrine. The pathway from tyrosine to norepinephrine is shown below:
Tyrosin e hyroxylase Tyro sin e ⎯⎯⎯⎯⎯⎯⎯ Dihydroxyphenylalanine ⎯⎯ Melanin → →
Aromatic a min o acid decarboxylase Dihydroxyphenylalanine ⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯ Dopa min e →
dopamaine β − hydroxylase Dopa min e ⎯⎯⎯⎯⎯⎯⎯⎯→ Norepinephrine
The formation of epinephrine from norepinephrine involves the transfer of the highly reactive methyl group of S-adenosylmethionine to norepinephrine:
phenylethanola min e N − methyltransferase Norepinephrine ⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯⎯→ Epinephrine ⎯
Unique pathways Proline, Ornithine and Arginine, all the three amino acids are derived from Glutamate and have unique pathways for their formation.
Overall view: First step involves phosphorylation of glutamate by ATP with the enzyme α-glutamyl kinase. This reaction is followed by the reduction to glutamate-5-semialdehyde and this spontaneously cyclizes into an internal Schiff base without the action of any enzyme. Semialdehyde formation also requires the presence of either NADP or NADPH. Yet, this semialdehyde serves as the branch point. One branch leads to proline while the other branch leads to ornithine and arginine. Glutamate-5-semialdehyde undergoes transamination to form ornithine and glutamate serves as the amino group donor. Ornithine is a urea cycle intermediate and it is converted into arginine through the urea cycle. Glutamate is converted to the physiologically active amine, α-aminobutyric acid (GABA) which is the major inhibitory neurotransmitter in the brain:
glutamate decarboxylase Glutamate ⎯⎯ ⎯ ⎯ ⎯ ⎯⎯→ GABA
cysteine, methionine ( essential amino acid - aspartate family) , proline, histidine and arginine These amino acids are said to follow unique pathways since they are abnormal from the other amino acids in the following two ways: The structure of the amino acid may be different enough than the other normal amino acids. Sulfur may be involved in the synthesis of these amino acids. Also, specific enzymes are involved in every step of the pathway. Cysteine Synthesis of cysteine is a two step reaction. • Serine and acetyl-CoA combine to form O-acetylserine. • Cysteine is formed by adding sulfide from sulfur assimilation to Oacetylserine. Thus sulfate assimilation envelops the pathway for cysteine synthesis. Methionine Methionine is synthesized from oxaloacetate.
Oxaloacetate is first converted into homoserine in the threonine biosynthetic pathway which involves the participation of Succinyl-CoA and donation of a sulfur group to the molecule by cysteine. Homoserine then possess sulfur attached to the end in next two steps and finally methionine is formed by the addition of a methyl group. The donor of the methyl group (R) is a methyl carrier in the cell, N5, N10-Methylene terahydropteroyl. Proline Starting with glutamate, proline synthesis involves a four step process. One ATP and two NADPH + H+ is used per molecule of proline. Histidine Histidine synthesis is long and complicated. Its pathway is intertwined with the purine nucleic acid biosynthesis. The pathway seems to be universal in all organisms able to synthesize histidine. Histidine Biosynthesis involves the molecule 5-phosphoribosyl - α - pyrophosphate (PRPP). PRPP is a significant molecule involved in the synthesis of purines and pyrimidines. The first five steps of the pathway take ribose from phosphoribosyl pyrophosphate (PRPP) and transform it into Imadiazoleglycerol phosphate. In the first step of histidine synthesis, PRPP condenses with ATP to form a purine, N1-5'phosphoribosyl ATP. This reaction is driven by the subsequent hydrolysis of the pyrophosphate that condenses out. Glutamine again plays a role as an amino group donor and results in the formation of 5aminoamidazole-4-carboximide ribonucleotide (ACAIR). ACAIR is an intermediate in purine biosynthesis. Once the formation of imadiazole ring is done, glutamate donates the α-amino group and newly forms an amine. This amine is then oxidized into histidine in the last step of the pathway. Energy is needed in the form of ATP and pyrophosphate which is lost from phosphoribosyl pyrophosphate. Ultimately ATP helps to drive the reaction. Significance: Histidine is peculiar in a way that its biosynthesis is intrinsically linked to the pathways of nucleotide formation. • Imidazole ring of histidine makes it a nucleophile and a good acid/base catalyzer and it is often found in enzyme active sites.
Transition to protein catalysis from RNA catalysis occurred at the origin of histidine biosynthesis.
Synthesis of histamine: Histamine is the physiologically active amine formed from Histidine.
Arginine Starting with the amino acid glutamate, synthesis of arginine is an eight step process. Two ATP and one NADPH + H+ are utilized to synthesize each arginine molecule.
3. Regulation by Feedback Inhibition
Particular amino acids serve as the building blocks for normal plant growth and development. The amino acid synthesis inhibitors like the sulfonylureas and imidazolinones act on a specific enzyme to prevent the production of such particular amino acids, thus acting as the herbicides. Amino acid derivatives also come under this type of herbicides. The main plant enzyme known as acetolactate synthase (ALS) is inhibited by the action of sulfonylureas and imidazolinone herbicides, thus preventing the production of three essential branch-chain amino acids.
The action of amino acid derivative herbicides is by inhibiting the production of three essential aromatic amino acids by restraining another key plant enzyme, known as SEPSP synthase. Regulation of nitrogen metabolism: The regulation of glutamine synthetase has been studied in the bacterium E.Coli and it is composed of 12 identical subunits. Glutamine synthetase is the enzyme which is responsible for the amidation of glutamate, and plays a central role in the regulation of nitrogen metabolism. The oxidative deamination of glutamate by glutamate dehydrogenase results in the production of NH3 and α-ketoglutarate. The α-ketoglutarate produced is then available for accepting amino groups in other transamination reactions. If ammonia, the other product of this reaction starts accumulates, its concentration increases and is highly toxic. In order to keep the level of NH3 in a controlled range, a rising level of α-ketoglutarate activates glutamine synthetase, thus increasing the production of glutamine, which donates its amino group in various other reactions. This enzyme activity is controlled by nine allosteric feedback inhibitors. Out of them, six are end products of pathways involving glutamine. They are histidine, tryptophan, carbamoyl phosphate glucosamine-6-phosphate, AMP, and CTP. The other three effectors out of nine are alanine, serine and glycine, which carry information regarding the cellular nitrogen level. The enzyme is also regulated by adenylylation of a Tyr residue and this results in an increase sensitivity to the cumulative feedback inhibition by the above nine effectors. Adenylyltransferase is the enzyme which catalyzes both the adenylylation and deadenylylation of E. coli glutamine synthetase. This specific enzyme is complexed with a tetrameric regulatory protein, PII. Regulation of the adenylylation and its reverse occurs at the level of PII, depending upon the uridylylation of another Tyr residue, located on PII. When PII is uridylylated, glutamine synthetase is deadenylylated. Also the reverse occurs when UMP is covalently attached to the Tyr residue of PII. Level of uridylylation is consecutively regulated by the activities of the two enzymes, uridylyltransferase and uridylyl-removing enzyme; both are present on the same protein. Uridylyltransferase is activated by α -ketoglutarate and ATP, while it is inhibited by glutamine and Pi. Thus the regulation of bacterial glutamine synthetase is precisely sensitive to the level of the cell's nitrogen metabolites.
4. Significance of Amino Acids
Amino acids serve as the precursors of proteins, nucleotide bases and other nitrogenous compounds. Proteins are single unbranched chain made of amino acid monomers. The exclusive shape of proteins is a result of the non covalent interactions between regions in the linear sequence of amino acids. Conformation of proteins refers to the proper arrangement of its three dimensional structure. This conformation determines the function the protein needs to serve. The three-dimensional structure is derived from the amino acid sequence and hence amino acids serve a significant role in the building and efficient functioning of body. Inside the intestine the proteins in the diet are digested and amino acids are produced. These amino acids are transported through out the body to serve the various cellular requirements. Hydrolysis of arginine results in urea formation, along with the regeneration of ornithine. Some of the deficiencies in the enzymes of urea cycle can be avoided by the supplementation of arginine in the diet. Phenylketonuria is the best known hereditary errors of amino acid metabolism. The carriers of phenylketonuria possess a reduced level of phenylalanine hydroxylase which results in buildup of phenylalanine. This phenylalanine is consequently transaminated to phenylpyruvate and excreted in the urine, the diseased condition called as "phenylketonuria". It quickly leads to severe mental retardation if not treated soon after birth with a low phenylalanine diet to prevent irreversible brain damage. Deficiency in Tyrosinase enzyme results in Albinism, a diseasae characterized with the absence of pigmentation.
Points to remember:
• Amino acids are classified into two categories as essential amino acids which are obtained by the organisms through dietary sources and nonessential amino acids that are synthesized by mammals. • Amino acids synthesis pathways can be grouped into a number of consistent systems such as simple reactions, branch chain amino acids, aromatic amino acids, threonine/lysine, serine/glycine, and unique pathways. • The three systems of ‘aromatic amino acids’, ‘threonine/lysine’ and ‘serine/glycine pathways’ possess a common beginning and then diverge to form the amino acid of interest.
Based upon the common precursors, essential amino acids can be grouped into 4 "families" as Aspartate Family: lysine, threonine, methionine, Pyruvate Family: leucine, isoleucine, valine, Aromatic Family: phenylalanine, Tyrosine, Tryptophan and Histidine.
An amino group is transferred from an amino acid to α -carbon of a ketoacid, which is catalyzed by an aminotransferase is termed as a "transamination reaction".
• • • • • • • • • • •
Alanine synthesis is by the transamination from glutamate onto pyruvate. Aspartate is synthesized by the transfer of an ammonia group from glutamate to oxaloacetate. Glutamate can be synthesized by the addition of ammonia to α - ketoglutarate. Asparagine is made either by adding ammonia directly to aspartate or through transamination from glutamine. Glutamine is made by the addition of another ammonia molecule to glutamate. Serine/Glycine metabolic pathway is an exergonic pathway in which energy is produced in the form of reduced NADH and does not require any energy input. Glycine generation is done by the removal of methyl group from serine. Cysteine is synthesized from serine and homocysteine which is a breakdown product of methionine. Synthesis of the aromatic amino acids begins with the synthesis of chorismate which is an important intermediate for many biosynthetic pathways. Proline, Ornithine and Arginine, all the three amino acids are derived from Glutamate and have unique pathways for their formation. Histidine Biosynthesis involves the molecule 5-phosphoribosyl α pyrophosphate (PRPP). PRPP is a significant molecule involved in the synthesis of purines and pyrimidines.
Amino acid synthesis inhibitors are sulfonylureas and imidazolinones which act on a specific enzyme to prevent the production of particular amino acids, thus acting as the herbicides.
Amino acid derivatives herbicides inhibit the production of three essential aromatic amino acids by restraining another key plant enzyme, known as SEPSP synthase.
Amino acids serve as the precursors of proteins, nucleotide bases and other nitrogenous compounds. Phenylketonuria is the best known hereditary errors of amino acid metabolism and characterized with a reduced level of phenylalanine hydroxylase which results in buildup of phenylalanine.
Deficiency in Tyrosinase enzyme results in Albinism, a disease characterized with the absence of pigmentation.
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