Author Topic: L-cysteine in bodybuilding  (Read 4999 times)

Offline Sergio

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L-cysteine in bodybuilding
« on: March 10, 2013, 08:44:03 PM »
From:  http://www.livestrong.com/article/424637-what-is-l-cysteine/

Bodybuilders may develop compromised immune systems due to over-performing strenuous endurance exercise. L-cysteine may offer a boost to help those body builders fight off the effects over-training. L-cysteine is a natural precursor to taurine, which is important to build lean muscle mass. It is for this reason body builders will choose to supplement with L-cysteine. The idea is that by loading additional amounts of L-cysteine, your body will naturally turn it into taurine, which will increase the lean muscle mass.

From: http://www.bodybuilding.com/fun/southfacts_cysteine.htm

L-cysteine is a conditionally sensitive, sulfur bearing, amino acid present in protein.

L-cysteine is a conditionally essential because it can be made endogenously in sufficient quantities under normal circumstances, but it may have to be exogenously supplemented if physical demands on the body (from physical exercise, stress or sickness) become too great.

From: http://www.bodybuilding.com/store/cysteine.html

USE L-CYSTEINE TO SUPPORT YOUR MUSCLE BUILDING GOALS*
L-cysteine is an amino acid that comes from protein sources. It's non-essential, which means that your body can make enough L-cysteine on its own or from other nutrients and amino acids. But, if you get a lot of exercise or you're an athlete, you may need extra L-cysteine support to continue to push yourself towards your fitness peak.*

Good sources of L-cysteine are: chicken, turkey, pork, dairy products, eggs, egg whites, garlic, onions and broccoli.

Offline Sergio

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Re: L-cysteine in bodybuilding
« Reply #1 on: March 10, 2013, 08:49:43 PM »
What does L-cisteine controls in the human body?

From: http://en.wikipedia.org/wiki/Cysteine

Because of its high reactivity, the thiol group of cysteine has numerous biological functions:

Precursor to the antioxidant glutathione

Due to the ability of thiols to undergo redox reactions, cysteine has antioxidant properties. Cysteine's antioxidant properties are typically expressed in the tripeptide glutathione, which occurs in humans as well as other organisms. The systemic availability of oral glutathione (GSH) is negligible; so it must be biosynthesized from its constituent amino acids, cysteine, glycine, and glutamic acid. Glutamic acid and glycine are readily available in most Western diets, but the availability of cysteine can be the limiting substrate.[citation needed]

Precursor to iron-sulfur clusters

Cysteine is an important source of sulfide in human metabolism. The sulfide in iron-sulfur clusters and in nitrogenase is extracted from cysteine, which is converted to alanine in the process.

Metal ion binding

Beyond the iron-sulfur proteins, many other metal cofactors in enzymes are bound to the thiolate substituent of cysteinyl residues. Examples include zinc in zinc fingers and alcohol dehydrogenase, copper in the blue copper proteins, iron in cytochrome P450, and nickel in the [NiFe]-hydrogenases.  The thiol group also has a high affinity for heavy metals, so that proteins containing cysteine, such as metallothionein, will bind metals such as mercury, lead, and cadmium tightly.

Roles in protein structure

In the translation of messenger RNA molecules to produce polypeptides, cysteine is coded for by the UGU and UGC codons.

Cysteine has traditionally been considered to be a hydrophilic amino acid, based largely on the chemical parallel between its thiol group and the hydroxyl groups in the side-chains of other polar amino acids. However, the cysteine side chain has been shown to stabilize hydrophobic interactions in micelles to a greater degree than the side chain in the non-polar amino acid glycine, and the polar amino acid serine. In a statistical analysis of the frequency with which amino acids appear in different chemical environments in the structures of proteins, free cysteine residues were found to associate with hydrophobic regions of proteins. Their hydrophobic tendency was equivalent to that of known non-polar amino acids such as methionine and tyrosine, and was much greater than that of known polar amino acids such as serine and threonine.  Hydrophobicity scales, which rank amino acids from most hydrophobic to most hydrophilic, consistently place cysteine towards the hydrophobic end of the spectrum, even when they are based on methods that are not influenced by the tendency of cysteines to form disulfide bonds in proteins. Therefore, cysteine is now often grouped among the hydrophobic amino acids,   though it is sometimes also classified as slightly polar, or polar.

While free cysteine residues do occur in proteins, most are covalently bonded to other cysteine residues to form disulfide bonds. Disulfide bonds play an important role in the folding and stability of some proteins, usually proteins secreted to the extracellular medium.[20] Since most cellular compartments are reducing environments, disulfide bonds are generally unstable in the cytosol with some exceptions as noted below.



Figure 2: Cystine (shown here in its neutral form), two cysteines bound together by a disulfide bond.
Disulfide bonds in proteins are formed by oxidation of the thiol groups of cysteine residues. The other sulfur-containing amino acid, methionine, cannot form disulfide bonds. More aggressive oxidants convert cysteine to the corresponding sulfinic acid and sulfonic acid. Cysteine residues play a valuable role by crosslinking proteins, which increases the rigidity of proteins and also functions to confer proteolytic resistance (since protein export is a costly process, minimizing its necessity is advantageous). Inside the cell, disulfide bridges between cysteine residues within a polypeptide support the protein's tertiary structure. Insulin is an example of a protein with cystine crosslinking, wherein two separate peptide chains are connected by a pair of disulfide bonds.

Protein disulfide isomerases catalyze the proper formation of disulfide bonds; the cell transfers dehydroascorbic acid to the endoplasmic reticulum, which oxidises the environment. In this environment, cysteines are, in general, oxidized to cystine and are no longer functional as a nucleophiles.

Aside from its oxidation to cystine, cysteine participates in numerous posttranslational modifications. The nucleophilic thiol group allows cysteine to conjugate to other groups, e.g., in prenylation. Ubiquitin ligases transfer ubiquitin to its pendant, proteins, and caspases, which engage in proteolysis in the apoptotic cycle. Inteins often function with the help of a catalytic cysteine. These roles are typically limited to the intracellular milieu, where the environment is reducing, and cysteine is not oxidized to cystine.