Cau Tao Cua Cac Loai Amino Acid 1 | Amino Acid | Biosynthesis

Alanine - The second simplest amino acid, but used the most in Hydroxyproline - Important amino acid used

in structural proteins proteins. like collagen. beta-Alanine - The only naturally occurring beta amino acid. Isoleucine - Hydrophobic amino acid used almost exclusively in protein and enzyme construction. Arginine - Amino acid often used at the active sites of enzymes. Leucine - Another hydrophobic amino acid used almost exclusively in protein and enzyme construction. Asparagine - Amide derivative of aspartic acid. Lysine Aspartic Acid - Important intermediate in the citric acid cycle.- An essential amino acid with a positive charge on the aliphatic side chain. Carnitine - Unusual amino acid that carries fatty acids into Methionine - An essential amino acid that helps initiate protein mitochondria. synthesis. Citrulline - An amino acid that works to detoxify and eliminate Ornithine - Critical member of the amino acids in the urea cycle. unwanted ammonia. Phenylalanine - Most common aromatic amino acid found in Cysteine - Thiol containing amino acid involved in active sites proteins. and protein tertiary structure determination. Proline Cystine - Oxidation product of cysteine that holds proteins - Cyclic aliphatic amino acid used in the synthesis of collagen. together. Serine gamma-Aminobutyric Acid - Decarboxylated amino acid that - Amino acid alcohol found in the active site of serine proteases. helps you chill out. Glutamic Acid - Negatively charged amino acid foundTaurine - Mercaptan-containing amino acid that is involved in bile on the acid biochemistry. surface of proteins. Threonine Glutamine - The only amino acid with the ability to easily cross - Amino acid alcohol involved in porphyrin metabolism. the barrier between blood and brain tissue. Tryptophan - Aromatic amino acid used the least frequently in Glutathione - Small peptide that helps dump free radicals. proteins. Glycine - Simplest amino acid that also acts as a neurotransmitter antagonist. Tyrosine - Hydroxyphenyl amino acid that is used to build neurotransmitters and hormones.

Histidine - Amino acid responsible for histamine biosynthesis. Valine - Hydrophobic aliphatic amino acid used to hold proteins together. Cysteine C (Cys) Chemical Properties: Sulfur-containing (Sulfur containing group) Physical Properties: Polar (uncharged)

Cysteine is one of two sulfur-containing amino acids; the other is methionine. Cysteine differs from serine in a single atom-- the sulfur of the thiol replaces the oxygen of the alcohol. The amino acids are, however, much more different in their physical and chemical properties than their similarity might suggest. Consider, for example, the differences between H2O and H2S. The hydrogen bonding propensity of water is well known and is responsible for many of its remarkable features. Under similar conditions of temperature and pressure, however, H2S is a gas as a consequence of its weak H-bonding propensity. Furthermore, the proton of the thiol of cysteine is much more acid than the hydroxylic proton of serine, making the nucleophilic thiol(ate) much more reactive than the hydroxyl of serine. Cysteine also plays a key role in stabilizing extracellular proteins. Cysteine can react with itself to form an oxidized dimer by formation of a disulfide bond. The environment within a cell is too strongly reducing for disulfides to form, but in the extracellular environment, disulfides can form and play a key role in stabilizing many such proteins, such as the digestive enzymes of the small intestine. Cysteine and methionine are the only sulfur-containing amino acids.

Asparagine N (Asn) Chemical Properties: Physical Properties: Neutral Polar (uncharged) (Amides of acidic amino acids R-group) Asparagine is the amide of aspartic acid. The amide group does not carry a formal charge under any biologically relevant pH conditions. The amide is rather easily hydrolyzed, converting asparagine to aspartic acid. This process is thought to be one of the factors related to the molecular basis of aging. Asparagine has a high propensity to hydrogen bond, since the amide group can accept two and donate two hydrogen bonds. It is found on the surface as well as buried within proteins. Asparagine is a common site for attachment of carbohydrates in glycoproteins.

Alanine A (Ala) Chemical Properties: Physical Properties: Aliphatic Nonpolar (Aliphatic R-group) Alanine is a hydrophobic molecule. It is ambivalent, meaning that it can be inside or outside of the protein molecule. The α carbon of alanine is optically active; in proteins, only the L-isomer is found. Note that alanine is the α-amino acid analog of the α-keto acid pyruvate, an intermediate in sugar metabolism. Alanine and pyruvate are interchangeable by a transamination reaction.

Interchangeable with Pyruvate

Arginine R (Arg) Chemical Properties: Basic (Basic R-group) Physical Properties: Polar (positively charged)

Arginine, an essential amino acid, has a positively charged guanidino group. Arginine is well designed to bind the phosphate anion, and is often found in the active centers of proteins that bind phosphorylated substrates. As a cation, arginine, as well as lysine, plays a role in maintaining the overall charge balance of a protein. Arginine also plays an important role in nitrogen metabolism. In the urea cycle, the enzyme arginase cleaves (hydrolyzes) the guanidinium group to yield urea and the L-amino acid ornithine. Ornithine is lysine with one fewer methylene groups in the side chain. L-ornithine is not normally found in proteins. There are 6 codons in the genetic code for arginine, yet, although this large a number of codons is normally associated with a high frequency of the particular amino acid in proteins, arginine is one of the least frequent amino acids. The discrepancy between the frequency of the amino acid in proteins and the number of codons is greater for arginine than for any other amino acid.

Aspartic Acid D (Asp) Chemical Properties: Physical Properties:

Acidic (Acidic R-group and their amides)

Polar (charged)

Aspartic acid is one of two acidic amino acids. Aspartic acid and glutamic acid play important roles as general acids in enzyme active centers, as well as in maintaining the solubility and ionic character of proteins. Proteins in the serum are critical to maintaining the pH balance in the body; it is largely the charged amino acids that are involved in the buffering properties of proteins. Aspartic acid is alanine with one of the β hydrogens replaced by a carboxylic acid group. The pKa of the β carboxyl group of aspartic acid in a polypeptide is about 4.0 Note that aspartic acid has an α-keto homolog, oxaloacetate, just as pyruvate is the α-keto homolog of alanine. Aspartic acid and oxaloacetate are interconvertable by a simple transamination reaction, just as alanine and pyruvate are interconvertible. Oxaloacetate is one of the intermediates of the Krebs cycle.

Aspartic acid and oxaloacetate are interconvertable by a simple transamination reaction

Glutamic Acid E (Glu) Chemical Properties: Acidic (Acidic R-group and their amides) Glutamic acid has one additional methylene group in its side chain than does aspartic acid. The side chain carboxyl of Physical Properties: Polar (charged)

aspartic acid is referred to as the β carboxyl group, while that of glutamic acid is referred to as the γ carboxyl group. The pKa of the γ carboxyl group for glutamic acid in a polypeptide is about 4.3, significantly higher than that of aspartic acid. This is due to the inductive effect of the additional methylene group. In some proteins, due to a vitamin K dependent carboxylase, some glutamic acids will be dicarboxylic acids, referred to as γ carboxyglutamic acid, that form tight binding sites for calcium ion.

Top Glutamic acid is interconvertible by transamination withα-ketoglutarate Glutamic acid and α-ketoglutarate, an intermediate in the Krebs cycle, are interconvertible by transamination. Glutamic acid can therefore enter the Krebs cycle for energy metabolism, and be converted by the enzyme glutamine synthetase into glutamine, which is one of the key players in nitrogen metabolism.

Biosynthesis of Proline Note also that glutamic acid is easily converted into proline. First, the γ carboxyl group is reduced to the aldehyde, yielding glutamate semialdehyde. The aldehyde then reacts with the α-amino group, eliminating water as it forms the Schiff base. In a second reduction step, the Schiff base is reduced, yielding proline.

Glutamine Q (Gln) Chemical Properties: Neutral (Amides of acidic amino acids R-group) Physical Properties: Polar (uncharged)

Glutamine is the amide of glutamic acid, and is uncharged under all biological conditions. The additional single methylene group in the side chain relative to asparagine allows glutamine in the free form or as the Nterminus of proteins to spontaneously cyclize and deamidate yielding the six-membered ring structure pyrrolidone carboxylic acid, which is found at the N-terminus of many immunoglobulin polypeptides. This causes obvious difficulties with amino acid sequence determination.

Glycine G (Gly)

Chemical Properties: Aliphatic (Aliphatic R-group)

Physical Properties: Nonpolar

Glycine is the smallest of the amino acids. It is ambivalent, meaning that it can be inside or outside of the protein molecule. In aqueous solution at or near neutral pH, glycine will exist predominantly as the zwitterion The isoelectric point or isoelectric pH of glycine will be centered between the pKas of the two ionizable groups, the amino group and the carboxylic acid group. In estimating the pKa of a functional group, it is important to consider the molecule as a whole. For example, glycine is a derivative of acetic acid, and the pKa of acetic acid is well known. Alternatively, glycine could be considered a derivative of aminoethane.

Histidine H (His) Chemical Properties: Basic (Basic group) Physical Properties: Polar (positively charged)

Histidine, an essential amino acid, has as a positively charged imidazole functional group. The imidazole makes it a common participant in enzyme catalyzed reactions. The unprotonated imidazole is nucleophilic and can serve as a general base, while the protonated form can serve as a general acid. The residue can also serve a role in stabilizing the folded structures of proteins.

Isoleucine I (Ile) Chemical Properties: Aliphatic (Aliphatic R-group) Physical Properties: Nonpolar

Isoleucine, an essential amino acid, is one of the three amino acids having branched hydrocarbon side chains. It is usually interchangeable with leucine and occasionally with valine in proteins. The side chains of these amino acids are not reactive and therefore not involved in any covalent chemistry in enzyme active centers. However, these residues are critically important for ligand binding to proteins, and play central roles in protein stability. Note also that the β carbon of isoleucine is optically active, just as the β carbon of threonine. These two amino acids, isoleucine and threonine, have in common the fact that they have two chiral centers.

Leucine L (Leu)

Chemical Properties: Aliphatic (Aliphatic R-group)

Physical Properties: Nonpolar

Leucine, an essential amino acid, is one of the three amino acid with a branched hydrocarbon side chain. It has one additional methylene group in its side chain compared with valine. Like valine, leucine is hydrophobic and generally buried in folded proteins.

Lysine K (Lys) Chemical Properties: Basic (Basic R-group) Physical Properties: Polar (positively charged)

Lysine. an essential amino acid, has a positively charged ε-amino group (a primary amine). Lysine is basically alanine with a propylamine substituent on theβcarbon. The ε-amino group has a significantly higher pKa (about 10.5 in polypeptides) than does the α-amino group. The amino group is highly reactive and often participates in a reactions at the active centers of enzymes. Proteins only have one α amino group, but numerous ε amino groups. However, the higher pKa renders the lysyl side chains effectively less nucleophilic. Specific environmental effects in enzyme active centers can lower the pKa of the lysyl side chain such that it becomes reactive. Note that the side chain has three methylene groups, so that even though the terminal amino group will be charged under physiological conditions, the side chain does have significant hydrophobic character. Lysines are often found buried with only theεamino group exposed to solvent.

Methionine M (Met) Chemical Properties: Sulfur-containing (Sulfur containing group) Methionine, an essential amino acid, is one of the two sulfur-containing amino acids. The side chain is quite hydrophobic and methionine is usually found buried within proteins. Unlike cysteine, the sulfur of methionine is not highly nucleophilic, although it will react with some electrophilic centers. It is generally not a participant in the covalent chemistry that occurs in the active centers of enzymes. The chemical linkage of the sulfur in methionine is a thiol ether. Compare this terminology with that of the oxygen containing ethers. The sulfur of methionine, as with that of cysteine, is prone to oxidation. The first step, yielding methionine sulfoxide, can be reversed by standard thiol containing reducing agents. The second step yields methionine sulfone, and is effectively irreversible. It is thought that oxidation of the sulfur in a specific methionine of the elastase inhibitor in human lung tissue by agents in cigarette smoke is one of the causes of smoking-induced emphysema. Methionine as the free amino acid plays several important roles in metabolism. It can react to form S-AdenosylL-Methionine (SAM) which servers at a methyl donor in reactions. Methionine and cysteine are the only sulfur-containing amino acids. Physical Properties: Non polar (hydrophobic)

Phenylalanine F (Phe) Chemical Properties: Aromatic (Aromatic R-group) Physical Properties: Nonpolar

As the name suggests, phenylalanine, an essential amino acid, is a derivative of alanine with a phenyl substituent on the β carbon. Phenylalanine is quite hydrophobic and even the free amino acid is not very soluble in water. It is an interesting point of history that Marshall Nirenberg and Phil Leder in their earliest experiments were studying the translation of the synthetic message polyU, which encodes polyphenylalanine. It was a happy coincidence that the product was insoluble. At the time, they did not know that UUU encodes Phe, but soon after the precipitate formed in their translation mix, they did, and they were on the way to unraveling the genetic code, and the Nobel prize. Due to its hydrophobicity, phenylalanine is nearly always found buried within a protein. The π electrons of the phenyl ring can stack with other aromatic systems and often do within folded proteins, adding to the stability of the structure.

Proline P (Pro) Chemical Properties: Physical Properties:

Cyclic Biosynthesis of Proline Proline shares many properties with the aliphatic group.

Nonpolar

Proline is formally NOT an amino acid, but an imino acid. Nonetheless, it is called an amino acid. The primary amine on the α carbon of glutamate semialdehyde forms a Schiff base with the aldehyde which is then reduced, yielding proline. When proline is in a peptide bond, it does not have a hydrogen on the α amino group, so it cannot donate a hydrogen bond to stabilize an α helix or a β sheet. It is often said, inaccurately, that proline cannot exist in an α helix. When proline is found in an α helix, the helix will have a slight bend due to the lack of the hydrogen bond. Proline is often found at the end of α helix or in turns or loops. Unlike other amino acids which exist almost exclusively in the trans- form in polypeptides, proline can exist in the cis-configuration in peptides. The cis and trans forms are nearly isoenergetic. The cis/trans isomerization can play an important role in the folding of proteins and will be discussed more in that context. Proline is the only cyclic amino acid.

Serine S (Ser) Chemical Properties: Non-aromatic hydroxyl (Hydroxyl group) Serine differs from alanine in that one of the methylenic hydrogens is replaced by a hydroxyl group. Serine is one of two hydroxyl amino acids. Both are commonly considered to by hydrophilic due to the hydrogen bonding capacity of the hydroxyl group. Physical Properties: Polar (uncharged)

Threonine T (Thr)

Chemical Properties: Non-aromatic hydroxyl

Physical Properties: Polar (uncharged)

(Hydroxyl group) Threonine, an essential amino acid, is a hydrophilic molecule. Threonine is an other hydroxyl-containing amino acid. It differs from serine by having a methyl substituent in place of one of the hydrogens on the β carbon and it differs from valine by replacement of a methyl substituent with a hydroxyl group. Note that both the α and β carbons of threonine are optically active.

Differs from serine

Differs from valine

Tryptophan W (Trp)

Chemical Properties: Aromatic (Aromatic R-group)

Physical Properties: Nonpolar

Tryptophan, an essential amino acid, is the largest of the amino acids. It is also a derivative of alanine, having an indole substituent on the β carbon. The indole functional group absorbs strongly in the near ultraviolet part of the spectrum. The indole nitrogen can hydrogen bond donate, and as a result, tryptophan, or at least the nitrogen, is often in contact with solvent in folded proteins.

Tyrosine Y (Tyr) Chemical Properties: Aromatic (Aromatic group & Hydroxyl group) Physical Properties: Nonpolar

Tyrosine, an essential amino acid, is also an aromatic amino acid and is derived from phenylalanine by hydroxylation in the para position. While tyrosine is hydrophobic, it is significantly more soluble that is phenylalanine. The phenolic hydroxyl of tyrosine is significantly more acidic than are the aliphatic hydroxyls of either serine or threonine, having a pKa of about 9.8 in polypeptides. As with all ionizable groups, the precise pKa will depend to a major degree upon the environment within the protein. Tyrosines that are on the surface of a protein will generally have a lower pKa than those that are buried within a protein; ionization yielding the phenolate anion would be exceedingly unstable in the hydrophobic interior of a protein. Tyrosine absorbs ultraviolet radiation and contributes to the absorbance spectra of proteins. The absorbance spectrum of tyrosine will be shown later; the extinction of tyrosine is only about 1/5 that of tryptophan at 280 nm, which is the primary contributor to the UV absorbance of proteins depending upon the number of residues of each in the protein.

Valine V (Val) Chemical Properties: Physical Properties: Aliphatic Nonpolar (Aliphatic R-group) Valine, an essential amino acid, is hydrophobic, and as expected, is usually found in the interior of proteins. Valine differs from threonine by replacement of the hydroxyl group with a methyl substituent. Valine is often referred to as one of the amino acids with hydrocarbon side chains, or as a branched chain amino acid. Note that valine and threonine are of roughly the same shape and volume. It is difficult even in a high resolution structure of a protein to distinguish valine from threonine.

Differs from threonine

Alanine is a non-essential amino acid that is involved in the metabolism of tryptophan and the vitamin pyridoxine. The alpha-carbon in alanine is substituted with a levorotatory (l)-methyl group, making it one of the simplest amino acids with respect to molecular structure. This amino acid is one of the most widely used in protein construction, averaging about 9 percent of average protein composition on a per-mole basis when compared with the other amino acids. Alanine has little therapeutic role in humans, although it has been demonstrated to display a cholesterol-reducing effect in rats This is the only naturally occurring beta amino acid, however this biochemical is not used in the biosynthesis of any major proteins or enzymes. Structurally, the IUPAC name for beta-alanine would be 3(or beta- ) aminopropionic acid. It is a component of the naturally occurring peptides carnosine and anserine and also of pantothenic acid (vitamin B-5) which itself is a component of coenzyme A. Under normal conditions, beta-alanine is metabolized into acetic acid. Arginine is a complex amino acid that is often found at the active (or catalytic) site in proteins and enzymes due to its amine-containing side chain. Although arginine is considered an essential amino acid (it must be obtained through the diet), this is true only during the juvenile period in humans. Arginine is incorporated in proteins at about a 4.7 percent on a per-mole basis when compared to the other amino acids. Natural sources of arginine are brown rice, nuts, popcorn, raisins, and whole-wheat products. Asparagine, the beta-amido derivative of aspartic acid, is considered a non-essential amino acid. This amino acid plays an important role in the biosynthesis of glycoproteins and is also essential to the synthesis of a large number of other proteins. On a per-mole basis, asparagine is incorporated into proteins and enzymes at a rate of 4.4 percent with respect to the other amino acids. Aspartic acid is one of two amino acids (the other is glutamic acid) that has a negatively charged carboxylate group on the side chain. This gives aspartic acid an overall negative charge at physiological hydrogen ion concentrations (approximately pH 7.3). Although aspartic acid is considered a non-essential amino acid, it plays a paramount role in metabolism during construction of other amino acids and biochemicals in the citric acid cycle. Among the biochemicals that are synthesized from aspartic acid are asparagine, arginine, lysine, methionine, threonine, isoleucine, and several nucleotides. The major biochemical function of carnitine is to act as a trans-membrane carrier of fatty acids to the interior of mitochondria. Carnitine is not used in the biosynthesis of proteins or enzymes and has an unusual structure compared to the classical amino acids. It is synthesized naturally from the amino acids methionine and lysine, but good external sources of carnitine are milk products and meats

Citrulline exists primarily in the liver, where it is heavily involved in the urea cycle to detoxify and excrete ammonia. This unusual amino acid is formed in the urea cycle by the addition of carbon dioxide and ammonia to ornithine. Next, it is combined with aspartic acid to form arginosuccinic acid, which later is metabolized into the amino acid arginine. Citrulline is not a component of any major proteins or enzymes. Cysteine is only incorporated into proteins at the rate of 2.8 percent relative to the other amino acids, but the unique thiol side chain of this amino acid is often heavily involved in the threedimensional stability of proteins and enzymes. The side chain is also often involved in the chemistry occurring at the active sites of many enzymes. Cysteine is also critical to the metabolism of a number of essential biochemicals including coenzyme A, heparin, biotin, lipoic acid, and glutathione. Cystine is the product of an oxidation between the thiol side chains of two cysteine amino acids. As such, cystine is not considered one of the 20 amino acids. This oxidation product is found in abundance in a variety of proteins such as hair keratin, insulin, the digestive enzymes chromotrypsinogen A, papain, and trypsinogen where it is heavily involved in stabilizing the tertiary structure of these macromolecules. gamma-Aminobutyric acid (GABA) is the product of a biochemical decarboxylation reaction of glutamic acid by the vitamin pyridoxal. GABA serves as a inhibitory neurotransmitter to block the transmission of an impulse from one cell to another in the central nervous system. Medically, GABA has been used to treat both epilepsy and hypertension where it is thought to induce tranquility in individuals who have a high activity of manic behavior and acute agitation Glutamic acid is biosynthesized from a number of amino acids including ornithine and arginine. When aminated, glutamic acid forms the important amino acid glutamine. Because it has a carboxylic acid moiety on the side chain, glutamic acid is one of only two amino acids (the other being aspartic acid) that has a net negative charge at physiological pH. This negative charge makes glutamic acid a very polar molecule and it is usually found on the outside of proteins and enzymes where it is free to interact with the aqueous intracellular surroundings. On a molar basis, glutamic acid is incorporated into proteins at a rate of 6.2 percent compared to the other amino acids. Glutamine is one of the twenty amino acids generally present in animal proteins. A monoamide of glutamic acid, the biochemical is also a component of many plants and was first isolated from beet juice in 1883. Glutamine was not isolated as a component from a protein, however, until 1932 and was first chemically produced the following year. The substance plays an important role in the cellular metabolism of animals and is the only amino acid with the ability to easily cross the barrier between blood and brain tissue. Combined, glutamine and glutamic acid are responsible for the vast majority of the amino nitrogen located in the brain, and are of central importance in the regulation of bodily ammonia levels. Though it is readily synthesized naturally within the body, glutamine is popularly sold as a nutritional supplement for athletes. Glutathione is actually a tripeptide made up the amino acids gamma-glutamic acid, cysteine, and glycine. The primary biological function of glutathione is to act as a non-enzymatic reducing agent to help keep cysteine thiol side chains in a reduced state on the surface of proteins. Glutathione is also used to prevent oxidative stress in most cells and helps to trap free radicals that can damage DNA and RNA. There is a direct correlation with the speed of aging and the reduction of glutathione concentrations in intracellular fluids. As individuals grow older, glutathione levels drop, and the ability to detoxify free radicals decreases Glycine is the simplest amino acid and is the only amino acid that is not optically active (it has no stereoisomers). This amino acid is essential for the biosynthesis of nucleic acids as well as of bile

acids, porphyrins, creatine phosphate, and other amino acids. On a molar basis, glycine is the second most common amino acid found in proteins and enzymes being incorporated at the rate of 7.5 percent compared to the other amino acids. Glycine is also similar to gamma-aminobutyric acid and glutamic acid in the ability to inhibit neurotransmitter signals in the central nervous system. Histidine is one of the basic (with reference to pH) amino acids due to its aromatic nitrogenheterocyclic imidazole side chain. This amino acid is biochemically metabolized into the neurotransmitter histamine and the set of genes that produce the enzymes responsible for histidine biosynthesis are controlled by the well-studied histidine operon. The disruption of histidine biosynthesis in bacteria is the basis for the famous Ames test, used to determine the mutagenability of various chemicals. Histidine is incorporated into proteins and enzymes at a molar percentage of 2.1 compared to the other amino acids. Hydroxyproline is derived from the amino acid proline and is used almost exclusively in structural proteins including collagen, connective tissue in mammals, and in plant cell walls. An unusual feature of this amino acid is that it is not incorporated into collagen during biosynthesis at the ribosome, but is formed from proline by a posttranslational modification by an enzymatic hydroxylation reaction. Non-hydroxylated collagen is commonly termed pro-collagen. Isoleucine is a member of the aliphatic side-chain amino acid family that is composed of extremely hydrophobic biochemicals that are found principally in the interior of proteins and enzymes. Like several other members of this family (valine and leucine), isoleucine is an essential amino acid that is not synthesized by mammalian tissues. Another feature of this class of amino acids is that they appear to have no other significant biological role than incorporation into proteins and enzymes, where their main purpose is to help dictate the tertiary structure of the macromolecules. Isoleucine is incorporated into proteins at a molar rate of 4.6 percent when compared to the other amino acids. Leucine, like its cousins isoleucine and valine, is a hydrophobic amino acid that is found as a structural element on the interior of proteins and enzymes. There appears to be no other significant metabolic role for these amino acids, but they are essential and because they are not synthesized by mammalian tissues, must be taken in the diet. Leucine ties glycine for the position of second most common amino acid found in proteins with a concentration of 7.5 percent on a molar basis compared to the other amino acids. Lysine is an essential amino acid that has a net positive charge at physiological pH values making it one of the three basic (with respect to charge) amino acids. This polar amino acid is commonly found on the surfaces of proteins and enzymes, and sometimes appears in the active site. Sources of lysine include meats, fish, poultry, and dairy products. Lysine is incorporated into proteins at the rate of 7 percent on a molar basis compared to the other amino acids Methionine is an important amino acid that helps to initiate translation of messenger RNA by being the first amino acid incorporated into the N-terminal position of all proteins. This sulfurcontaining amino acid is also the source of sulfur for cysteine in animals and man. In that regard, methionine is considered an essential amino acid whereas cysteine is not, so cysteine is nonessential only as long as the diet contains adaquate amounts of methionine. The terminal methyl group of the methionine side chain often participates in biochemical methyl transfer reactions making methionine a member of the "methyl donor" class of biochemicals. On a molar basis, methionine is incorporated into proteins and enzymes at the rate of 1.7 percent, but this is partially due to posttranslational protein-modifying events that often occur where methionine and several other N-terminal amino acids are removed from the protein.

Ornithine plays an important role in the urea cycle and is the precursor of the amino acids citrulline, glutamic acid, and proline. Another primary role of ornithine is being an intermediate in arginine biosynthesis, although this is due to its participation in the urea cycle (responsible for the production of urea). Ornithine is not directly incorporated into proteins and enzymes and does not have a codon in the genetic code. Phenylalanine is an essential amino acid that is also one of the aromatic amino acids that exhibit ultraviolet radiation absorption properties with a large extinction coefficient. This characteristic is often used as an analytical tool to quantify the amount of protein in a sample. Phenylalanine plays a key role in the biosynthesis of other amino acids and some neurotransmitters. It is the most commonly found aromatic amino acid in proteins and enzymes with a molar ratio of 3.5 percent compared to the other amino acids, about double the amount of any other aromatic amino acid Proline is one of the cyclic aliphatic amino acids that is a major component of the protein collagen, the connective tissue structure that binds and supports all other tissues. Proline is synthesized from glutamic acid prior to its incorporation into pro-collagen during messenger RNA translation. After the pro-collagen protein is synthesized, it is converted by posttranslational modification into hydroxyproline. On a molar basis proline is incorporated into protein at a rate of 4.2 percent with respect to other amino acids The methyl side chain of serine contains a hydroxy group making this one of two amino acids that are also alcohols. Serine plays a major role in a variety of biosynthetic pathways including those involving pyrimidines, purines, creatine, and porphyrins. Serine is also found at the active site in an important class of enzymes termed "serine proteases" that include trypsin and chymotrypsin. These enzymes catalyze the hydrolysis of peptide bonds in polypeptides and proteins, a major function in the digestive process. On a molar basis, serine is incorporated into proteins at a rate of 7.1 percent compared to the other amino acids. Taurine is a non-essential sulfur-containing amino acid that functions with glycine and gammaaminobutyric acid as a neuroinhibitory transmitter. While taurine does not have a genetic codon and is not incorporated into proteins and enzymes, it does play an important role in bile acid metabolism. Taurine is incorporated into one of the most abundant bile acids, chenodeoxychloic acid where it serves to emulsify dietary lipids in the intestine, promoting digestion. Threonine is another alcohol-containing amino acid that can not be produced by metabolism and must be taken in the diet. This amino acid plays an important role along with glycine and serine in porphyrin metabolism. Threonine is incorporated into proteins and enzymes at a molar rate of 6 percent compared to the other amino acids Tryptophan is an essential amino acid that must be obtained from the diet. The unusual indole side chain of tryptophan is also the nucleus of the important neurotransmitter serotonin, which is biosynthesized from tryptophan. The aromatic portion of tryptophan also serves as an ultraviolet marker for detection of this amino acid either separately, or incorporated into proteins and enzymes, via ultraviolet spectrophotometry. Tryptophan is incorporated into proteins and enzymes at the molar rate of 1.1 percent compared to other amino acids making it the rarest amino acid found in proteins. Tyrosine is metabolically synthesized from phenylalanine to become the para-hydroxy derivative of that important amino acid. This hydroxylated amino acid participates in the synthesis of many important biochemicals including the thyroid hormones, the melanin biological pigments, and the catecholamines, an important class of biological regulators. Tyrosine is incorporated into proteins and enzymes at the molar rate of 3.5 percent with respect to the other amino acids.

Valine is an aliphatic amino acid that is closely related to leucine and isoleucine both in structure and function. These amino acids are extremely hydrophobic and are almost always found in the interior of proteins. They are also seldom useful in routine biochemical reactions, but are relegated to the duty of determining the three-dimensional structure of proteins due to their hydrophobic nature. They are also essential amino acids and must be obtained in the diet. Important sources of valine include soy flour, cottage cheese, fish, meats, and vegetables. Valine is incorporated into proteins and enzymes at the molar rate of 6.9 percent when compared to the other amino acids. SU HINH THANH AMINO ACID Mô phỏng các đám bụi và nước thời hệ mặt trời mới hình thành, hai nhóm nghiên cứu độc lập đều giật mình khi phát hiện các axit amin - một trong những "viên gạch cơ bản" của ngôi nhà sự sống. Đây là bằng chứng cho thấy, sự sống có thể đã xuất hiện bên ngoài rồi mới nhập cư vào trái đất. Axit amin đóng vai trò quan trọng trong các phản ứng hóa học, khiến các protein và enzyme hoạt động được. Trong một thí nghiệm, nhà hóa học Đức Uwe Meierhenrich cùng các cộng sự Pháp và Hà Lan đã dựng lại quá trình xảy ra ở những đám mây bụi và khí cách đây 4,6 triệu năm - thời điểm hệ mặt trời đang hình thành. Trong một bình chân không, người ta bơm vào một hỗn hợp nước + CO2 + amoniac + methanol lên bề mặt một tấm hợp kim nhôm lạnh. Dưới tác dụng của tia cực tím, hỗn hợp đó đã tạo thành đám bọt khói mờ trên bề mặt nhôm. Thoạt tiên Meierhenrich muốn làm thí nghiệm này để thử chất lượng vật liệu nhôm cho tàu thăm dò sao chổi Rossetta. Tuy nhiên, điều bất ngờ đã xảy ra khi các nhà khoa học hâm nóng đám bọt bám trên bề mặt tấm nhôm. Khi đó, đã xuất hiện 16 axit amin. Trong số này có 4 axit amin của cơ thể người. Cùng lúc, nhóm nghiên cứu của Max Bernstein ở Trung tâm nghiên cứu Ames của NASA (Mỹ) cũng đạt được kết quả tương tự. Nhóm này cũng dùng tia cực tím tác động vào một hỗn hợp bụi băng (tương tự như bụi băng trong vũ trụ). Kết quả, họ đã Axit amin là một tạo ra 3 axit amin: glycine, alanine và serine. viên gạch cơ bản của ngôi nhà sự Thực ra, người ta từng tìm thấy axit amin ở một số thiên thạch giàu carbon. Tuy nhiên, sống. các nhà khoa học lại giải thích rằng các axit amin hình thành khi thiên thạch rơi vào khí quyển trái đất. "Từ 50 năm nay, khoa học cho rằng axit amin chỉ có mặt trên hành tinh của chúng ta", Meierhenrich nói. "Nhưng bây giờ thì ta biết rằng axit amin có thể xuất hiện mọi nơi trong vũ trụ. Rõ ràng, sự sống trên trái đất có liên hệ mật thiết đến khoảng không bên ngoài"

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