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	Maca has 19 of 20 Amino Acids AMINO ACIDS Amino Acids - Proteins are made of combination of amino acids and in the process of digestion each protein is split up by the enzymes which act upon it into the several amino-acids of which it is formed, as it is only when in this state that protein can be utilized by the tissues of the body. A great number of amino acids are formed as the result of protein digestion and these form a pool (the amino acid pool) from which the cells of the body draw the protein they need. Actually only 9 of these amino-acids are essential for the growth and repair of body tissues. Examples : acetyl-l-carnitine , agmatine sulphate , alanine (d,l,dl) , aspartame ,beta-alanine , creatine citrate , creatine monohydrate,creatine phosphate disodium salt, creatine pyruvate, dirnethylglycine, dl-allo-threonine, d-mannose, gaba , lycine, homo-l-cystein, inosine, l-5-hydroxytryptophan, l-asparagine, l-aspartic acid, l-carnitine (base, hci, tartrat, orotate), l-carnosine, l-cystein (base, mono/anhydrous hci),l-cystine, l-glutamine, l-hydroxyproline, l-isoleucine, l-leucine, l-pyroglutamic acid, l-tyrosine, l-valine, n-acetyl-glycine, n-acetyl-l-cysteine, phenylalanine (d,l,dl), proline (d,l,dl), sarcosine, selenomethionine ,s-phenyl-l-cysteine, threonine (d,l,dl), tyramine etc. Amino Acid Remarks Alanine NE-MACA Very abundant, very versatile. More stiff than glycine, but small enough to pose only small steric limits for the protein conformation. It behaves fairly neutrally, can be located in both hydrophilic regions on the protein outside and the hydrophobic areas inside. Cysteine NE The sulfur atom binds readily to heavy metal ions. Under oxidizing conditions, two cysteines can join together by a disulfide bond to form the amino acid cystine. When cystines are part of a protein, insulin for example, this enforces tertiary structure and makes the protein more resistant to unfolding and denaturation; disulphide bridges are therefore common in proteins that have to function in harsh environments, digestive enzymes (e.g., pepsin and chymotrypsin), structural proteins (e.g., keratin), and proteins too small to hold their shape on their own (eg. insulin). Aspartate NE-MACA Behaves similarly to glutamic acid. Carries a hydrophilic acidic group with strong negative charge. Usually is located on the outer surface of the protein, making it water-soluble. Binds to positively-charged molecules and ions, often used in enzymes to fix the metal ion. When located inside of the protein, aspartate and glutamate are usually paired with arginine and lysine. Glutamate NE-MACA Behaves similar to aspartic acid. Has longer, slightly more flexible side chain. Phenylalanine E-MACA Essential for humans. Phenylalanine, tyrosine, and tryptophan contain large rigid aromatic group on the side chain. These are the biggest amino acids. Like isoleucine, leucine and valine, these are hydrophobic and tend to orient towards the interior of the folded protein molecule. Glycine NE-MACA Because of the two hydrogen atoms at the a carbon, glycine is not optically active. It is the smallest amino acid, rotates easily, adds flexibility to the protein chain. It is able to fit into the tightest spaces, e.g., the triple helix of collagen. As too much flexibility is usually not desired, as a structural component it is less common than alanine. Histidine E-MACA In even slightly acidic conditions protonation of the nitrogen occurs, changing the properties of histidine and the polypeptide as a whole. It is used by many proteins as a regulatory mechanism, changing the conformation and behavior of the polypeptide in acidic regions such as the late endosome or lysosome, enforcing conformation change in enzymes. However only a few histidines are needed for this, so it is comparatively scarce. Isoleucine E-MACA Essential for humans. Isoleucine, leucine and valine have large aliphatic hydrophobic side chains. Their molecules are rigid, and their mutual hydrophobic interactions are important for the correct folding of proteins, as these chains tend to be located inside of the protein molecule. Lysine E-MACA Essential for humans. Behaves similarly to arginine. Contains a long flexible side-chain with a positively-charged end. The flexibility of the chain makes lysine and arginine suitable for binding to molecules with many negative charges on their surfaces. E.g., DNA-binding proteins have their active regions rich with arginine and lysine. The strong charge makes these two amino acids prone to be located on the outer hydrophilic surfaces of the proteins; when they are found inside, they are usually paired with a corresponding negatively-charged amino acid, e.g., aspartate or glutamate. Leucine E-MACA Essential for humans. Behaves similar to isoleucine and valine. See isoleucine. Methionine E-MACA Essential for humans. Always the first amino acid to be incorporated into a protein; sometimes removed after translation. Like cysteine, contains sulfur, but with a methyl group instead of hydrogen. This methyl group can be activated, and is used in many reactions where a new carbon atom is being added to another molecule.   Asparagine Similar to aspartic acid. Asn contains an amide group where Asp has a carboxyl.   Proline NE-MACA Contains an unusual ring to the N-end amine group, which forces the CO-NH amide sequence into a fixed conformation. Can disrupt protein folding structures like a helix or ß sheet, forcing the desired kink in the protein chain. Common in collagen, where it often undergoes a posttranslational modification to hydroxyproline. Uncommon elsewhere. Glutamine E-MACA Similar to glutamic acid. Gln contains an amide group where Glu has a carboxyl. Used in proteins and as a storage for ammonia. Arginine E-MACA Functionally similar to lysine. Serine NE-MACA Serine and threonine have a short group ended with a hydroxyl group. Its hydrogen is easy to remove, so serine and threonine often act as hydrogen donors in enzymes. Both are very hydrophilic, therefore the outer regions of soluble proteins tend to be rich with them. Threonine E-MACA Essential for humans. Behaves similarly to serine. Valine E-MACA Essential for humans. Behaves similarly to isoleucine and leucine. See isoleucine. Tryptophan E-MACA Essential for humans. Behaves similarly to phenylalanine and tyrosine (see phenylalanine). Precursor of serotonin. Tyrosine NE-MACA Behaves similarly to phenylalanine and tryptophan (see phenylalanine). Precursor of melanin, epinephrine, and thyroid hormones. Retrieved from "http://en.wikipedia.org/wiki/List_of_standard_amino_acids"

 

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