L-cysteinium

Base Information

• Chemical Name: L-cysteinium
• CAS No.: 52-90-4
• Molecular Formula: C3H7NO2S
• Molecular Weight: 121.16
• Hs Code.: 29309012
• NCI Thesaurus Code: C29609
• Nikkaji Number: J3.302.195J,J3.302.196H
• RXCUI: 3024
• Wikidata: Q27114944
• Wikipedia: Cysteine
• Mol file: 52-90-4.mol

Synonyms:L-cysteinium;cysteine;L-cysteine cation;L-cysteinium(1+);CHEBI:32445;(1R)-1-carboxy-2-mercaptoethanaminium;(1R)-1-carboxy-2-sulfanylethanaminium;Q27114944

Chemical Property of L-cysteinium

Chemical Property:

• Appearance/Colour: white crystalline powder
• Melting Point: 220 °C
• Refractive Index: 8.8 ° (C=8, 1mol/L HCl)
• Boiling Point: 293.9 °C at 760 mmHg
• PKA: 1.92(at 25℃)
• Flash Point: 131.5°C
• PSA: 102.12000
• Density: 1.334 g/cm³
• LogP: 0.02840
• Storage Temp.: Store at RT.
• Sensitive.: Air Sensitive
• Solubility.: H2O: 25 mg/mL
• Water Solubility.: 280 g/L (25 ºC)
• XLogP3: -2.5
• Hydrogen Bond Donor Count: 3
• Hydrogen Bond Acceptor Count: 3
• Rotatable Bond Count: 2
• Exact Mass: 122.02757467
• Heavy Atom Count: 7
• Complexity: 75.3

Purity/Quality:

99.9% ^*data from raw suppliers

L-Cysteine ^*data from reagent suppliers

Safty Information:

• Pictogram(s): Xi,Xn
• Hazard Codes: Xn,Xi
• Statements: 22-36/37/38-20/21/22
• Safety Statements: 36-37/39-26-24/25

MSDS Files:

SDS file from LookChem

Total 1 MSDS from other Authors

Useful:

• Chemical Classes: Biological Agents -> Amino Acids and Derivatives
• Canonical SMILES: C(C(C(=O)O)[NH3+])S
• Isomeric SMILES: C([C@@H](C(=O)O)[NH3+])S
• Recent ClinicalTrials: Effects of Dietary Amino Acids on Serum and Macrophage Atherogenicity
• description: L-Cysteine is one of the 20 natural amino acids and, besides methionine,the only one which contains sulfur. It is a thiol-containing non-essential amino acid that is oxidized to form Cystine. It is a non-essential sulfur-containing amino acid in humans, related to cystine, Cysteine is important for protein synthesis, detoxification, and diverse metabolic functions. Found in beta-keratin, the main protein in nails, skin, and hair, Cysteine is important in collagen production, as well as skin elasticity and texture. Also required in the manufacture of amino acid taurine, Cysteine is a component of the antioxidant glutathione, and plays a role in the metabolism of essential biochemicals such as coenzyme A, heparin, and biotin. L-cysteine hydrochloride is used in the baking industry as dough conditioner. Specially, it breaks the disulfide bonds of gluten, which lowers the viscosity of the dough. It is then easier to work with and increases the elasticity of the dough, helping it to rise during baking. L-cysteine is available through many dietary sources, primarily animal protein. Eggs and dairy products also contain significant levels of l-cysteine. Vegetable sources of l-cysteine include broccoli, Brussels sprouts, garlic, granola, sprouted lentils, oats, onions and peppers. The commercial extraction of l-cysteine typically uses human hair, due to its high concentration of this amino acid. Other commercial sources include hog hair and poultry feathers. L-cysteine may also be synthesized in a process that involves fermentation by a variety of E. coli.
• Uses: L-cysteine can be used as bread improver, nutritional supplements, antioxidants and color fixative. It can also be applied for curing acrylonitrile and aromatic acid poisoning, preventing radiation damage and treating bronchitis and phlegm. L-cysteine can absorb alcohol and convert it into acetaldehyde to alleviate a hangover. L-cysteine can be used for the treatment of eczema, urticaria, freckles and other skin diseases. And its series products are widely used in medicine, food and cosmetics industry L-cysteine can be used for biochemical research and as the antidote for hepatitis, liver poisoning, radiopharmaceutical poisoning, antimony poisoning, etc. L-cysteine is mainly used for medicine, cosmetics, biochemical research and so on. It can be used in the bread material to accelerate the formation of gluten and to promote fermenting and depanning, as well as to prevent aging. It can be used in natural fruit juices to prevent oxidation of vitamin C and to prevent fruit juice from becoming brown. The product has detoxification effect and can be used for curing acrylonitrile poisoning and aromatic acidosis. This product also has the role of preventing the human body from radiation damage. It can be used as bronchitis drugs, especially as phlegm drugs (mostly in the form of acetyl L-cysteine methyl ester salt). In cosmetics, it is mainly used as cosmetic water, perm solution, anti-sun cream and other skin care. L-cysteine can be used as the receptor agonists of NMDA glutamate. L-Cysteine is a non-essential amino acid that can be synthesized by the human body under normal physiological conditions if a sufficient quantity of methionine is available. L-Cysteine is commonly used as a precursor in the food and pharmaceutical industries. L-Cysteine is used as a processing aid for baking, as an additive in cigarettes, as well as in the preparation of meat flavours. It is used in foods to prevent oxygen from destroying vitamin c and is used in doughs to reduce mixing time.
• Description: Cysteine (abbreviated as Cys or C) is an α-amino acid with the chemical formula HO2CCH(NH2)CH2SH. It is a semi - essential amino acid, which means that it can be biosynthesized in humans. The thiol side chain in cysteine often participates in enzymatic reactions, serving as a nucleophile. The thiol is susceptible to oxidization to give the disulfide derivative cystine, which serves an important structural role in many proteins. When used as a food additive, it has the E number E920.
• Biological Functions: The cysteine thiol group is nucleophilic and easily oxidized. The reactivity is enhanced when the thiol is ionized, and cysteine residues in proteins have pKa values close to neutrality, so are often in their reactive thiolate form in the cell. 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. 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 .

Technology Process of L-cysteinium

There total 189 articles about L-cysteinium which guide to synthetic route it. The literature collected by LookChem mainly comes from the sharing of users and the free literature resources found by Internet computing technology. We keep the original model of the professional version of literature to make it easier and faster for users to retrieve and use. At the same time, we analyze and calculate the most feasible synthesis route with the highest yield for your reference as below:

synthetic route:

Reference yield: 94.0%

L-cystine (56-89-3) → L-Cysteine (52-90-4) + L-Cysteic acid (498-40-8,3024-83-7)

Guidance literature:

With hydrogenchloride; sulfuric acid; hydrogen bromide; In water; at 45 ℃; electrolysis (graphite sheets, i = 0.5 A/cm²);

DOI:10.1016/S0040-4020(01)87076-9

Reference yield: 21.0%

H-Cys(Acm)(O)-OH (75893-05-9) → L-Cysteine (52-90-4) + L-Cysteic acid (498-40-8,3024-83-7) + L-cystine (56-89-3) + S-acetamidomethyl-L-cysteine (19647-70-2)

Guidance literature:

With ammonia; sodium; for 0.00277778h; Product distribution;

Reference yield:

N,N'-di-p-nitrocarbobenzoxy-L-cystine (95107-90-7) → L-Cysteine (52-90-4) + N-(4-methylphenyl)hydroxylamine (623-10-9)

Guidance literature:

Hydrogenation;

DOI:10.1017/S1092852900008580

upstream raw materials:

cysteine disulfide

L-cystine

sodium cyanide

N,S-diacetyl-cysteine

Downstream raw materials:

(RS)-2-amino-3-<(2-chloroethyl)sulfanyl>propanoic acid hydrochloride

S-(2-carboxyethyl)-L-cysteine

S,S'-trans-cinnamylidene-di-L-cysteine

S-(1,1,2-trichlorovinyl)-L-cysteine

Refernces

• 1、 Hattori, Ryota,Matsushita-Morita, Mayumi,Marui, Junichiro,Tada, Sawaki,Suzuki, Satoshi,Furukawa, Ikuyo,Yamagata, Youhei,Amano, Hitoshi,Ishida, Hiroki,Takeuchi, Michio,Kusumoto, Ken-Ichi. "Characterization of an aspergillus oryzae cysteinyl dipeptidase expressed in escherichia coli". . p. 159 - 161. Retrieved 2011.
• 2、 Zervas,Photaki,Phocas. "Note on S-trityl-L-cystein". . p. 3332 - 3333. Retrieved 1968.
• 3、 Márquez, Vanina E.,Arias, Diego G.,Chiribao, Maria L.,Faral-Tello, Paula,Robello, Carlos,Iglesias, Alberto A.,Guerrero, Sergio A.. "Redox metabolism in Trypanosoma cruzi. Biochemical characterization of dithiol glutaredoxin dependent cellular pathways". . p. 56 - 67. Retrieved 2014.
• 4、 Gebauer-Fuelnegg. "-". . p. 4610. Retrieved 1930.
• 5、 Shiraiwa, Tadashi,Tazoh, Hirohide,Sunami, Michio,Sado, Yujin,Kurokawa, Hidemoto. "Racemic Structure and Optical Resolution by Preferential Crystallization of DL-Cysteine Salts of Substituted Benzenesulfonic Acids". . p. 3985 - 3990. Retrieved 1987.
• 6、 Arai, Gorou,Sugaya, Toshiaki,Sakamoto, Mika,Yasumori, Iwao. "Electrochemical Studies of Poly(mercaptohydroquinone) and Poly(mercapto-p-benzoquinone) Films Prepared by Electrochemical Polymerization. VI. Electroreduction of L-Cystine on Thiolates Fixed in the Polymer Film". . p. 594 - 596. Retrieved 1992.
• 7、 Hill, David T.,Isab, Anvarhusein A.,Griswold, Don E.,Dimartino, Michael J.,Matz, Elizabeth D.,Figueroa, Angel L.,Wawro, Joyce E.,Debrosse, Charles,Reiff, William M.,Elder, Richard C.,Jones, Benjamin,Webb, James W.,Shaw, C. Frank. "Seleno-auranofin (Et3PAuSe-tagl): Synthesis, spectroscopic (EXAFS, 197Au Moessbauer, 31P, 1H, 13C, and 77Se NMR, ESI-MS) characterization, biological activity, and rapid serum albumin-induced triethylphosphine oxide generation". . p. 7663 - 7675. Retrieved 2010.
• 8、 -. "MODIFIED INTERLEUKIN-7 PROTEINS AND USES THEREOF". . . Retrieved 2021/10/22.
• 9、 Bridoux, Maxime,Ceccarelli, Cecilia,Shalayel, Ibrahim,Vallée, Yannick,Vazart, Fanny,Youssef-Saliba, Sparta. "Cysteine Chemistry in Connection with Abiogenesis". supporting information. . Retrieved 2020/05/18.