Organic Molecule – Lysine.

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Lysine is one of the twenty amino acids that make up natural proteins. Eleven of these amino acids can be made by the human body from other amino acids, while the remaining nine cannot be synthesized by the body they must be derived nutritionally from protein intake – these are the “essential amino acids”. Lysine is one of nine essential amino acids and therefore an important molecule as proteins are made up of a melange of most of the amino acids. Formed in plants, algae, and fungi by two distinct biosynthetic pathways (see Figures 1 and 2) it helps maintain growth, lean body mass, tissue repair and the body’s store of nitrogen.

Lysine is a polar molecule that has a net positive charge at physiological pH values making it one of the three basic (with respect to charge) amino acids. It therefore mostly prefers to substitute for the other positively charged amino acid arginine, though in some circumstances it will also tolerate a change to other polar amino acids. Lysine frequently plays an important role in structure. It can be considered to be somewhat amphipathic as the part of the side chain nearest to the backbone is long, carbon containing and hydrophobic, whereas the end of the side chain is positively charged.

Due to this lysine is located where part of the side-chain is buried, and only the charged portion is on the outside of the protein. However, this is by no means always the case, as lysine is often positioned on the outside of proteins. Lysine is also frequently involved in salt-bridges, where they pair with a negatively charged amino acids (such as aspartate, shown below) to create stabilizing hydrogen bonds, that can be important for protein stability. Furthermore lysine contains a positively charged amino on its side-chain that is sometimes involved in forming hydrogen bonds with negatively charged non-protein atoms.

This polar amino acid is commonly found on the surfaces of proteins and enzymes, and sometimes appears in the active or binding site. Lysine is an amino acid released in the hydrolysis of many common proteins but present in small amounts or lacking in certain plant proteins; for example gliadin from wheat or zein from corn (maize).

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Good sources of lysine are foods rich in protein including meat (specifically red meat, pork, and poultry), dairy products such as cheese (particularly parmesan), certain fish (such as cod and sardines), nuts, eggs, soybeans (particularly tofu, isolated soy protein, and defatted soybean flour), lentils and spinach. Lysine is incorporated into proteins at the rate of 7 percent on a molar basis compared to the other amino acids.

Like all amino acids, lysine functions as a building platform for proteins, and thus key in the production of disease fighting antibodies, numerous enzymes, and hormones. It insures the adequate absorption of calcium; ...

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