454-29-5

Usage

Biochem/physiol Actions

Homocysteine is a sulfhydryl-containing amino acid, synthesized from methionine. It is a non-essential, non-proteinogenic amino acid. It is an important determinant of the methylation cycle and is present in the plasma in four forms. An abnormally high level of homocysteine leads to hyperhomocysteinemia and also promotes atherosclerosis.

Purification Methods

Purify it as for the L-isomer. [Allen & Steinmann J Am Chem Soc 74 3932 1952, and references for the L-isomer above, Beilstein 4 IV 3189.]

InChI:InChI=1/C4H9NO2S/c5-3(1-2-8)4(6)7/h3,8H,1-2,5H2,(H,6,7)/t3-/m1/s1

Upstream product

• 462-10-2 DL-homocystine 
• 1017-76-1 S-benzyl homocysteine 
• 6038-19-3 3-aminodihydrothiophen-2(3H)-one hydrochloride 
• 59-51-8 DL-methionine 
• 187878-81-5 S-nitroso-homocysteine 
• 1192-20-7 2-aminobutyrolactone 
• 10593-85-8 DL-homocysteine thiolactone 
• 348-67-4 D-methionine 
• 700-63-0 (R)-phenylglycine amide 
• 147331-82-6 (R)-1,3-thiazane-4-carboxylic acid 
• 6027-15-2 D-homocystine 
• 2867-15-4 (2S,2'S)-2-amino-4-(2'-amino-2'-carboxyethylsulfanyl)butanoic acid 

Downstream Products

• 60175-95-3 1,3-thiazane-4-carboxylic acid 
• 100795-85-5 N-benzoyl-S-cyanomethyl-homocysteine 
• 99855-86-4 S-benzoyl-DL-homocysteine 
• 348-67-4 D-methionine 
• 462-10-2 DL-homocystine 
• 59-51-8 DL-methionine 
• 2598-44-9 S-(2-hydroxyethyl)-D,L-homocysteine 
• 88096-03-1 S-γ-Carboxypropylhomocystein 
• 7689-60-3 S-benzyl-L-homocysteine 
• 1007126-73-9 N-Benzyl-2-(2-oxo-tetrahydro-thiophen-3-ylamino)-4-phenyl-butyramide 
• 1007126-74-0 N-Benzyl-2-cyclopropyl-2-(2-oxo-tetrahydro-thiophen-3-ylamino)-acetamide 
• 1007126-72-8 3-Methyl-2-(2-oxo-tetrahydro-thiophen-3-ylamino)-N-(2,4,6-trimethyl-phenyl)-butyramide 
• 2906-60-7 5,6-dithia-decanedioic acid 
• 1160162-67-3 (RS)-2-amino-4-[(3-carboxypropyl)disulfanyl]butanoic acid 

Relevant academic research and scientific papers

New thiazane and thiazolidine PNA monomers: Synthesis, incorporation into PNAs and hybridization studies

New constrained PNA monomers containing a substituted thiazolidine or a thiazane ring were synthesized and incorporated in the center of a 9-mer homothymine PNA. The PNA/DNA hybrids stability was studied by UV-melting experiments which showed that the presence of the modified unit destabilizes the PNA/DNA triplexes.

A quantitative method for the assessment of homocysteine thiolactonase enzyme activity

This assay elucidates an accurate, simple, and precise protocol to quantify the activity of homocysteine thiolactonase (HTase). To establish HTase activity, the enzyme samples were incubated with a 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES) buffer, which contained suitable concentrations of the homocysteine thiolactone as a substrate. To stop the enzyme's reaction, the CUPRAC reagent (Cu(Nc)22+) was added after a suitable incubation time. The reduction of Cu(II)-neocuproine complex (Cu(Nc)22+) to highly coloured Cu(I)-neocuproine complex (Cu(Nc)2+) by the produced homocysteine was quantified spectrophotometrically at 450 nm (CUPRAC method). The increase in the absorbance of the coloured Cu(I)-neocuproine complex (Cu(Nc)2+) was correlated directly to the activity of HTase. ANOVA analysis was utilised to validate the new method against homocysteine thiolactonase activity using the H+ ions liberating method in matched samples. In conclusion, according to the obtained correlation coefficient (0.9995) from the comparison of the current method with the reference method, the current method is effective in assay HTase activity with high reliability.

An Organodiselenide with Dual Mimic Function of Sulfhydryl Oxidases and Glutathione Peroxidases: Aerial Oxidation of Organothiols to Organodisulfides

A novel organodiselenide, which mimics sulfhydryl oxidases and glutathione peroxidase (GPx) enzymes for oxidation of thiols by oxygen and hydrogen peroxide, respectively, into disulfides has been presented. The developed catalyst oxidizes an array of organothiols into respective disulfides in practical yields by using aerial O2 to avoid any reagents/additives, base, and light source. The synthesized diselenide also catalyzes the reduction of hydrogen peroxide into water by following the GPx enzymatic catalytic cycle with a reduction rate of 49.65 ± 3.7 μM·min-1.

Novel synthetic method of DL-homocysteinethiolactone hydrochloride

The invention discloses a novel synthetic method of DL-homocysteinethiolactone hydrochloride. According to the novel synthetic method, DL-methionine and metallic sodium are subjected to reduction reaction, an obtained reduction product is subjected to desalting, and is subjected to condensation de-watering in the presence of dilute hydrochloric acid so as to obtain the DL-homocysteinethiolactone hydrochloride. DL-homocysteine is obtained via one-step synthesis from methionine, and DL-homocysteinethiolactone hydrochloride is obtained via condensation of DL-homocysteine under acid conditions, so that a re-reduction process of conversion of DL-methionine into DL-homocysteine in the prior art is avoided, reaction steps are reduced, harsh high temperature reaction conditions are avoided, release of hypertoxic gas and production of a large amount of high-salt waste water are reduced, three waste discharge is reduced, and a large amount of energy consumption is reduced; and in addition, the medium used in the novel synthetic method can be recycled, and cost is reduced. The novel synthetic method is capable of satisfying green and environment-friendly technology requirements; operation is simple; preparation is convenient; cost is low; and the novel synthetic method is suitable for industrialized large scale production.

Reaction of hydrogen sulfide with disulfide and Sulfenic acid to form the strongly Nucleophilic Persulfide

Background: Hydrogen sulfide (H2S) modulates physiological processes in mammals. Results: The reactivity of H2S toward disulfides (RSSR) and albumin sulfenic acid (RSOH) to form persulfides (RSSH) was assessed. Conclusion: H2S is less reactive than thiols. Persulfides have enhanced nucleophilicity. Significance: This kinetic study helps rationalize the contribution of the reactions with oxidized thiol derivatives toH2S biology.

Immunomodulatory peptides

The invention relates to peptides derivatized with a hydrophilic polymer which, in some embodiments, bind to human FcRn and inhibit binding of the Fc portion of an IgG to an FcRn, thereby modulating serum IgG levels. The disclosed compositions and methods may be used in some embodiments, for example, in treating autoimmune diseases and inflammatory disorders. The invention also relates, in further embodiments, to methods of using and methods of making the peptides of the invention.

A green and expedient synthesis of enantiopure diketopiperazines via enzymatic resolution of unnatural amino acids

Dipeptides comprising a d-phenylglycyl moiety coupled to the l-enantiomer of 2-amino butyric acid, norvaline, norleucine, and homocysteine were successfully synthesized from d-phenylglycine amide and the racemate of the corresponding unnatural amino acid.

METHOD FOR PREPARING AN AMINO ACID FROM 2 AMINOBUTYROLACTONE

The invention relates to a method for preparing an amino acid, or its salts, from 2-aminobutyrolactone (2ABL), said amino acid fitting the formula I, XCH2CH2CHNH2COOH, wherein X is such that X? represents a nucleophilic ion, according to which N-carboxylation of 2-aminobutyrolactone (2ABL) is achieved with carbon dioxide, and the thereby obtained 2ABL carbamate is reactive with an XH reagent or its salts.

Protein thiocarboxylate-dependent methionine biosynthesis in Wolinella succinogenes

Thiocarboxylated proteins are important intermediates in a variety of biochemical sulfide transfer reactions. Here we identify a protein thiocarboxylate-dependent methionine biosynthetic pathway in Wolinella succinogenes. In this pathway, the carboxy terminal alanine of a novel sulfur transfer protein, HcyS-Ala, is removed in a reaction catalyzed by a metalloprotease, HcyD. HcyF, an ATP-utilizing enzyme, catalyzes the adenylation of HcyS. HcyS acyl-adenylate then undergoes nucleophilic substitution by bisulfide produced by Sir to give the HcyS thiocarboxylate. This adds to O-acetylhomoserine to give HcyS-homocysteine in a PLP-dependent reaction catalyzed by MetY. HcyD-mediated hydrolysis liberates homocysteine. A final methylation completes the biosynthesis. The biosynthetic gene cluster also encodes the enzymes involved in the conversion of sulfate to sulfide suggesting that sulfate is the sulfur source for protein thiocarboxylate formation in this system.

Inhibitors of autoinducer transporters

The present invention relates to the discovery of the lsr operon, the genes therein, and the polypeptides encoded by these genes. The present invention also includes strains with altered expression levels of the polypeptides encoded by the genes and the lsr operon relative to wild type cells. In some embodiments, the strains express a transporter that transports an autoinducer into the cell at a level higher than that of wild type cells. The present invention also includes methods for identifying compounds that modulate the transport of the autoinducer into cells.