Amino acids play central roles both as building blocks of proteins and as intermediates in metabolism. The 20 amino acids that are found within proteins convey a vast array of chemical versatility. The precise amino acid content, and the sequence of those amino acids, of a specific protein, is determined by the sequence of the bases in the gene that encodes that protein. The chemical properties of the amino acids of proteins determine the biological activity of the protein. Proteins not only catalyze all (or most) of the reactions in living cells, they control virtually all cellular process. In addition, proteins contain within their amino acid sequences the necessary information to determine how that protein will fold into a three dimensional structure, and the stability of the resulting structure. The field of protein folding and stability has been a critically important area of research for years, and remains today one of the great unsolved mysteries. It is, however, being actively investigated, and progress is being made every day.
As we learn about amino acids, it is important to keep in mind that one of the more important reasons to understand amino acid structure and properties is to be able to understand protein structure and properties. We will see that the vastly complex characteristics of even a small, relatively simple, protein are a composite of the properties of the amino acids which comprise the protein.
Essential amino acids
Humans can produce 10 of the 20 amino acids. The others must be supplied in the food. Failure to obtain enough of even 1 of the 10 essential amino acids, those that we cannot make, results in degradation of the body's proteins—muscle and so forth—to obtain the one amino acid that is needed. Unlike fat and starch, the human body does not store excess amino acids for later use—the amino acids must be in the food every day.
The 10 amino acids that we can produce are alanine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline, serine and tyrosine. Tyrosine is produced from phenylalanine, so if the diet is deficient in phenylalanine, tyrosine will be required as well. The essential amino acids are arginine (required for the young, but not for adults), histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. These amino acids are required in the diet. Plants, of course, must be able to make all the amino acids. Humans, on the other hand, do not have all the the enzymes required for the biosynthesis of all of the amino acids.
Why learn these structures and properties?
It is critical that all students of the life sciences know well the structure and chemistry of the amino acids and other building blocks of biological molecules. Otherwise, it is impossible to think or talk sensibly about proteins and enzymes, or the nucleic acids.
Amino Acids
Alanine
http://en.wikipedia.org/wiki/Alanine
Alanine is a nonessential amino acid, meaning it can be manufactured by the human body, and does not need to be obtained directly through the diet. Alanine is found in a wide variety of foods, but is particularly concentrated in meats.
Good sources of alanine include
Animal sources: meat, seafood, caseinate, dairy products, eggs, fish, gelatin, lactalbumin
Vegetarian sources: beans, nuts, seeds, soy, whey, brewer's yeast, brown rice, bran, corn, legumes, whole grains.
Arginine
http://fr.wikipedia.org/wiki/Arginine
Arginine is an amino acid "semi-essential" normally synthesized by the body according to his needs, from which the body produces nitric oxide (a substance that promotes blood vessel dilation) and creatine ( non-essential nutrient involved in the development and functioning of the muscles).
Arginine acts on erectile dysfunction (because nitric oxide helps the blood flow). It does not improve sexual function in subjects with no problems.
Arginine combined with other amino acids (ornithine), has an effect on the secretion of growth hormones, the rate of muscle mass and strength but then arginine alone has no effect on physical performance. Thus, combined with zinc, it allows the testicles to produce sperm most abundant, testicles swelling up to 50% (1.5 x) in some individuals.
Arginine is found in brown rice, oats and buckwheat, as well as red meat, poultry, fish, dairy products, nuts and wine.
An external supply of arginine is required only after a major trauma, severe infection, a major surgery.
Is not considered an essential nutrient, no recommended dietary allowance has been established for arginine.
Asparagine
http://fr.wikipedia.org/wiki/Asparagine
Asparagine was the first amino acid discovered in 1806 by Louis-Nicolas Vauquelin who was studying the asparagus , hence its name.
We often associate the odor of urine after eating asparagus asparagine, but some scientists disagree and implicate other substances such as methanethiol.
Aspartic acid
http://en.wikipedia.org/wiki/Aspartic_acid
Aspartic acid is not an essential amino acid, which means that it can be synthesized from central metabolic pathway intermediates in humans. Aspartic acid is found in:
Animal sources: luncheon meats, sausage meat, wild game
Vegetable sources: sprouting seeds, oat flakes, avocado, asparagus[citation needed], young sugarcane, and molasses from sugar beets.[1]
Dietary supplements, either as aspartic acid itself or salts (such as magnesium aspartate)
The sweetener aspartame (NutraSweet, Equal, Canderel, etc.)
Cysteine
http://fr.wikipedia.org/wiki/Cyst%C3%A9ine
Cysteine involved in the synthesis of melanin , the natural pigment of the skin and hair.
Sources:
yeast
wheat germ
garlic
onion
Brussels sprouts
broccoli
dairy
nuts
seeds
Seafood
fish
eggs
meat
Glutamine
http://fr.wikipedia.org/wiki/Glutamine
Nutrition:
Because it can be synthesized from glutamic acid, glutamine is not an essential amino acid .
Glutamine serves as a supplement in the diet of frequent weight, and as a treatment for muscle cramps in the elderly. It provides among others a better recovery during physical effort (strength sports, etc. ..) and helps rebuild damaged muscle tissue. It also prevents the syndrome of overtraining 3 .
Currently, studies are still conducted on the potential adverse consequences of excessive absorption of glutamine, again without results. And its consumption is healthy because it can supposedly be used to fill the reserves of amino acids a session of physical exercise could have been empty. This is why it is often prescribed to people who are fasting, or suffering from physical trauma, a defective immune system or cancer.
In addition, recent studies have been conducted to better understand the effects and properties of glutamine, and these show a link between a diet rich in glutamine and beneficial effects on the intestines. Glutamine would include improving the maintenance functions of the intestinal wall , proliferation of the intestinal flora , as well as cell differentiation and a reduction in infections. It seems that these properties are due to an extraction rate of glutamine higher than that of other amino acids, which would make the best choice for the improvement of the bowel 4 .
These results were discovered after comparing plasma concentration in the intestines between diets high and low in glutamine. Yet although it seems that glutamine has properties "cleaning" is not clear to what extent it would have therapeutic benefits due to large variations in glutamine concentration in food 4 .
In addition, glutamine is known for its various effects on the acceleration of healing after surgery. The recovery time after abdominal surgery are reduced if the patient is fed intravenously with mixtures containing glutamine. Clinical trials seem to have shown that patients undergoing this type of plan, compared with those who had no glutamine, present including improved nitrogen balance, improved generation of cysteinyl- leukotrienes from granulocytes , a improve the restoration of leukocytes and intestinal permeability, all without side effects apparent.
Glycine
http://fr.wikipedia.org/wiki/Glycine_(acide_amin%C3%A9)
The glycine molecule acts as a neurotransmitter inhibitor at the spinal cord.
Glycine is a precursor of porphyrins, but also of creatine (in the liver ), the uric acid (a form of excretion of ammonia in birds ), of glutathione (a compound which participates in the reduction of free radicals ).
It is a component of bile acids primary: it combines with bile salts , making them more soluble.
Added to the succinyl-CoA it forms the heme of the hemoglobin , for example.
It s'interconvertit with serine and threonine , and is the final molecule of the degradation of choline:
serine + tetrahydrofolate 5,10-methylenetetrahydrofolate + glycine + H 2 O.
Between glycine in the synthesis of glutathione
Histidine
http://fr.wikipedia.org/wiki/Histidine
Histidine is an amino acid that fulfills important functions in the structure and function of proteins . The imidazole ring of histidine has an atom of nitrogen that can capture a proton with a pKa close to neutral (pKa ~ 6.8) and therefore under physiological conditions. This property is crucial for the function of proteins:
It allows certain histidine residues present in the active sites of enzymes involved in reactions of proton transfer in the physiological conditions of the cytoplasm ( pH ~ 7).
In the hemoglobin , the histidines present in the protein involved in maintaining the pH of blood, acting as a molecule buffer.
The nitrogen of the imidazole ring of histidine can also form links of coordination with metal ions such as Zn 2 + , Co 2 + , Fe 2 + or Ni 2 + . These connections are important for the binding of these ions in metalloproteins , where the complexation of the metal is required for the activity of the protein. Examples include a histidine as axial ligand of iron in myoglobin and the hemoglobin and two histidines in the complexation of zinc present in the collagenase, a protease that degrades collagen.
Isoleucine
http://fr.wikipedia.org/wiki/Isoleucine
Biochemistry
It has a second asymmetric carbon in addition to carbon α and only the form 2S-3S is found in nature. The proportion of isoleucine in the protein human is about 4.6%.
Leucine
http://fr.wikipedia.org/wiki/Leucine
The leucine (C 6 H 13 NO 2 ), branched amino acid (essential) non-polar, higher homologue of valine, is the most common 20 amino acids . Its name in systematic nomenclature is 2-Amino-4-methylpentanoic. Its chemical composition is identical to that of isoleucine , but its atoms are arranged differently, which gives it different properties. From the perspective of nutrition , leucine is in humans, an essential amino acid . It is found in significant amounts in wheat germ ( 2170 mg ), tuna ( 2170 mg ), peanuts ( 2050 mg ), salmon ( 1770 mg ), beef tenderloin ( 1700 mg ) , chickpeas ( 1460 mg ), cottage cheese (curd 1 230 mg ) and rice (full 690 mg ). According to an article by researchers at the INRA in the Journal of Physiology December 2005, the addition of leucine in the diet of rats would allow regulation of the "nitrogen balance". This altered during aging, causing an imbalance between production and degradation of muscle proteins. This is the origin of the muscle loss observed in the elderly. It remains to show that the results obtained with rats are reproducible with the human species before considering a supplemental leucine in the diet of the elderly.
Lysine
http://fr.wikipedia.org/wiki/Lysine
The peptide poly-lysine is a polymer of several lysines. Since the amine group has a pK a of 10.2, this group is positively charged (-NH 3 + ) at pH (neutral) 7.
With the positively charged polymer, DNA can be linked (in the construction of micro-arrays of DNA at neutral pH (and basic), a surface of glass is negatively charged groups in SiO - . They may have electrostatic bonds with polylysine, which in turn binds to the negative groups of phosphate of DNA.
Methionine
http://fr.wikipedia.org/wiki/Methionine
Biological roles
Methionine plays a special role in protein biosynthesis , since all protein chains start with the incorporation of a methionine N-terminal position. Other methionine residues can then be incorporated internally to the chain polypeptides. The first methionine of the protein is not always found in proteins over. Indeed, it is frequently cleaved by a specific enzyme called methionine aminopeptidase.
Methionine is also a transmethylase, it has the ability to transfer the methyl group bound to sulfur. Also the breaking of this bond releases a large amount of energy.
Also, it is used as an antidote to paracetamol 100 mg of methionine per 500 mg of paracetamol
Phenylalanine
http://fr.wikipedia.org/wiki/Phenylalanine
The phenylalanine is an amino acid aromatic non- polar which are derived, in particular, the tyrosine and the aspartame . Its core benzene gives an absorption spectrum especially in the UV around 260 nm wavelength. It comes in the form of two enantiomers due to the chirality of the atom of carbon bearing the amine and acid. In humans, it is an essential amino acid that is to say, it must be provided by the diet because the body is unable to synthesize.
Medical
Phenylalanine is present especially in chewing gum , if this molecule has no effect in the proportion of gum to see two or more per day, it will have a laxative effect against in higher quantity (or even 2 3 packets of chewing gum per day), because the action of phenylalanine in the body in large doses is an accelerating intestinal transit.
Of phenylalanine found in most common foods
Cereals and cereal products
Starchy roots, tubers
Legumes and derived products
Nuts and seeds
Vegetables
Fruits
Meat and poultry
Eggs
Fish , crustaceans , molluscs and fish products
Milk and dairy products
Yeasts and algae
Seeds and vegetables are the foods most of phenylalanine, closely followed by some cheese (especially dry).
Proline
http://fr.wikipedia.org/wiki/Proline
L- proline or proline by abuse of language, is one of 20 amino acids of the genetic code . In human proteins, its frequency is 5.2%.
L- proline ( enantiomer of absolute configuration S) is also used to living organisms to assemble proteins. This is known as amino acids proteinogenic .
Proline may act by breaking the α helices because it can form hydrogen bond (due to its secondary amine) and therefore destabilizes the α helix, or form a junction in the β sheets . The presence of many prolines can cause a propeller to proline (as is the case of collagen ). Proline has a function amine secondary and not a function imine (The error is present in some French-language works of Biochemistry. But let us not forget that the chemistry and biochemistry are never at odds vocabulary for chemical functions).
Proline participates mainly collagen synthesis and wound healing.
Serine
http://en.wikipedia.org/wiki/Serine
Biological function: Metabolic
Serine is important in metabolism in that it participates in the biosynthesis of purines and pyrimidines. It is the precursor to several amino acids including glycine and cysteine, and tryptophan in bacteria. It is also the precursor to numerous other metabolites, including sphingolipids and folate, which is the principal donor of one-carbon fragments in biosynthesis.
Signaling
D-Serine, synthesized in the brain by serine racemase from L-serine (its enantiomer), serves as both a neurotransmitter and a gliotransmitter by activating NMDA receptors, making them able to open if they then also bind glutamate. D-serine is a potent agonist at the glycine site of the NMDA-type glutamate receptor. For the receptor to open, glutamate and either glycine or D-serine must bind to it. In fact, D-serine is a more potent agonist at the glycine site on the NMDAR than glycine itself. D-serine was only thought to exist in bacteria until relatively recently; it was the second D amino acid discovered to naturally exist in humans, present as a signalling molecule in the brain, soon after the discovery of D-aspartate. Had D amino acids been discovered in humans sooner, the glycine site on the NMDA receptor might instead be named the D-serine site
Threonine
http://en.wikipedia.org/wiki/Threonine
Biosynthesis
As an essential amino acid, threonine is not synthesized in humans, hence we must ingest threonine in the form of threonine-containing proteins. In plants and microorganisms, threonine is synthesized from aspartic acid via α-aspartyl-semialdehyde and homoserine. Homoserine undergoes O-phosphorylation; this phosphate ester undergoes hydrolysis concomitant with relocation of the OH group.[3] Enzymes involved in a typical biosynthesis of threonine include:
1. aspartokinase
2. ß-aspartate semialdehyde dehydrogenase
3. homoserine dehydrogenase
4. homoserine kinase
5. threonine synthase.
Tryptophan
http://en.wikipedia.org/wiki/Tryptophan
Tryptophan (IUPAC-IUBMB abbreviation: Trp or W; IUPAC abbreviation: L-Trp or D-Trp; sold for medical use as Tryptan)[2] is one of the 20 standard amino acids, as well as an essential amino acid in the human diet. It is encoded in the standard genetic code as the codon UGG. The slight mispronunciation "tWiptophan" can be used as a mnemonic for its single letter IUPAC code W.[3] Only the L-stereoisomer of tryptophan is used in structural or enzyme proteins, but the D-stereoisomer is occasionally found in naturally produced peptides (for example, the marine venom peptide contryphan).[4] The distinguishing structural characteristic of tryptophan is that it contains an indole functional group. It is an essential amino acid as demonstrated by its growth effects on rats
Tyrosine
http://en.wikipedia.org/wiki/Tyrosine
Tyrosine (abbreviated as Tyr or Y)[1] or 4-hydroxyphenylalanine, is one of the 20 amino acids that are used by cells to synthesize proteins. Its codons are UAC and UAU. It is a non-essential amino acid with a polar side group. The word "tyrosine" is from the Greek tyri, meaning cheese, as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese.[2][3] It is called tyrosyl when referred to as a functional group or side chain.
Functions
Aside from being a proteogenic amino acid, tyrosine has a special role by virtue of the phenol functionality. It occurs in proteins that are part of signal transduction processes. It functions as a receiver of phosphate groups that are transferred by way of protein kinases (so-called receptor tyrosine kinases). Phosphorylation of the hydroxyl group changes the activity of the target protein.
A tyrosine residue also plays an important role in photosynthesis. In chloroplasts (photosystem II), it acts as an electron donor in the reduction of oxidized chlorophyll. In this process, it undergoes deprotonation of its phenolic OH-group. This radical is subsequently reduced in the photosystem II by the four core manganese clusters.
Dietary sources
Tyrosine, which can also be synthesized in the body from phenylalanine, is found in many high protein food products such as soy products, chicken, turkey, fish, peanuts, almonds, avocados, milk, cheese, yogurt, cottage cheese, lima beans, pumpkin seeds, and sesame seeds.[4] Tyrosine can also be obtained through supplementation.
Valine
http://en.wikipedia.org/wiki/Valine
Valine (abbreviated as Val or V)[3] is an α-amino acid with the chemical formula HO2CCH(NH2)CH(CH3)2. L-Valine is one of 20 proteinogenic amino acids. Its codons are GUU, GUC, GUA, and GUG. This essential amino acid is classified as nonpolar. Human dietary sources include cottage cheese, fish, poultry, peanuts, sesame seeds, and lentils.
Along with leucine and isoleucine, valine is a branched-chain amino acid. It is named after the plant valerian. In sickle-cell disease, valine substitutes for the hydrophilic amino acid glutamic acid in hemoglobin. Because valine is hydrophobic, the hemoglobin does not fold correctly.
Atoms in Amino Acids
Hydrogen
Carbon
nitrogen
Oygen
Sulfur