462-10-2

Usage

Uses

Used in Pharmaceutical Industry:
DL-Homocystine is used as a precursor in the synthesis of potential antitumor agents for its ability to inhibit L-asparagine. This makes it a valuable component in the development of cancer treatments.
Used in Clinical Research:
There is growing clinical evidence that elevated homocysteine levels are associated with an increased risk of venous and arterial thrombosis. As a result, DL-Homocystine plays a significant role in research aimed at understanding and managing these conditions.

Purification Methods

dl-Homocystine crystallises in platelets from water with 1H2O and m 258-260o(dec), all operations should be carried out under N2. [Sudo J Chem Soc Jpn (Pure Chem Sect) 79 81, 86, 87 1958, Beilstein 4 IV 3199.]

Upstream product

• 454-29-5 2-amino-4-mercaptobutyric acid 
• 59-51-8 DL-methionine 
• 1910-42-5 paraquat dichloride 
• 187878-81-5 S-nitroso-homocysteine 
• 1192-20-7 2-aminobutyrolactone 
• 7689-60-3 S-benzyl-L-homocysteine 
• 6027-13-0 L-homocysteine 
• 75027-08-6 (S)-2-Amino-4-[(R)-2-((S)-3-amino-3-carboxy-propyldisulfanyl)-1-(carboxymethyl-carbamoyl)-ethylcarbamoyl]-butyric acid 
• 139427-42-2 S-nitroso-L-homocysteine 
• 63-68-3 L-methionine 
• 79-24-3 Nitroethane 

Downstream Products

• 60175-95-3 1,3-thiazane-4-carboxylic acid 
• 62-49-7 choline 
• 123-41-1 cholin hydroxide 
• 454-29-5 2-amino-4-mercaptobutyric acid 
• 1017-76-1 S-benzyl homocysteine 
• 10593-85-8 DL-homocysteine thiolactone 
• 14160-80-6 2,2'-bis-benzoylamino-4,4'-disulfanediyl-di-butyric acid 
• 31523-80-5 homocysteinesulfinic acid 
• 66076-71-9 (Cbz-D,L-Homo-Cys-OH)₂ 
• 28223-71-4 DL-Homocysteine Sodium Salt 
• 504-33-6 homocysteic acid 
• 20933-67-9 R(-)-2-thioxothiazolidine-4-carboxylic acid 
• 147857-42-9 Dimethyl (2RS,2'RS)-homocystinate dihydrochloride 
• 213487-91-3 Dimethyl (2RS,2'RS)-N,N'-bis(benzyloxycarbonyl)homocysteinate 

Relevant academic research and scientific papers

S-Adenosylhomocysteine Analogue of a Fairy Chemical, Imidazole-4-carboxamide, as its Metabolite in Rice and Yeast and Synthetic Investigations of Related Compounds

During the course of our investigations of fairy chemicals (FCs), we found S-ICAr-H (8a), as a metabolite of imidazole-4-carboxamide (ICA) in rice and yeast (Saccharomyces cerevisiae). In order to determine its absolute configuration, an efficient synthetic method of 8a was developed. This synthetic strategy was applicable to the preparation of analogues of 8a that might be biologically very important, such as S-ICAr-M (9), S-AICAr-H (10), and S-AICAr-M (11).

Reduction of an asymmetric Pt(IV) prodrug fac-[Pt(dach)Cl3(OC(=O)CH3)] by biological thiol compounds: kinetic and mechanistic characterizations

An asymmetric Pt(IV) prodrug fac-[Pt (dach)Cl3(OC(=O)CH3)] (dach = 1,2-diaminocyclohexane) was synthesized, and the reduction of the Pt(IV) prodrug by three biological thiols glutathione (GSH), cysteine (Cys) and homocysteine (Hcy) was investigated by a stopped-flow spectrometer. All the reductions were followed by an overall second-order reaction with first-order in both [Pt(IV)] and [thiol]. The reduction of the Pt(IV) prodrug occurred through a chloride bridge (Pt-Cl-S) mediated two electron transfer process. Therefore, the coordinated chloride possesses a better bridging effect than the oxygen atom from the coordinated –CH3COO? of the Pt(IV) prodrug. A reactivity trend of k′Cys > k′GSH > k′Hcy is found, illustrating that the reactivity is followed by the trend of Cys > GSH > Hcy in pH 7.4 buffer. Graphical abstract: Transition state is formed between the axially coordinated chloride of the platinum(IV) complex and the sulfur atom from the thiol/thiolate group of Cys/Hcy/GSH.[Figure not available: see fulltext.].

Continuous production method DL-cysteine thiolactone hydrochloride (by machine translation)

The method comprises the following steps DL - reacting, methionine as raw material :(1) with DL - sulfuric acid continuously into a liquid-liquid-phase micro-channel reactor to generate, high-cysteine hydrochloride 15-18mol/L containing DL - high-cysteine hydrochloride in a hydrochloric acid system through dehydration condensation to obtain, high cystine hydrochloride DL - in a continuous circulation reaction . high cystine, is obtained by carrying out a continuous circulation reaction to a cathode chamber, DL - of a plate-and-frame type electrolytic cell in a hydrochloric acid system through a continuous circulation reaction to complete DL - collection of cysteine hydrochloride in a hydrochloric acid system through dehydration and condensation reaction, so as to form DL - high-cysteine hydrochloride in the next step; DL - (1) ;(2). The. method comprises the following steps of: continuously circulating the cathode, solution, from, the liquid-phase micro-channel reactor; and carrying out a reduction reaction in a hydrochloric acid system through a liquid-liquid-phase micro-channel reactor. (by machine translation)

METHOD OF PRODUCING S-ICA RIBOSYLHOMOCYSTEINE

PROBLEM TO BE SOLVED: To provide novel techniques regarding a method of producing S-ICA ribosylhomocysteine. SOLUTION: A method of producing a compound represented by formula (1) or a salt thereof comprises reacting a compound represented by formula (2) with a compound represented by formula (3) to generate a compound represented by formula (4), and subjecting the obtained compound represented by formula (4) to a treatment of removing a protecting group. SELECTED DRAWING: None COPYRIGHT: (C)2020,JPOandINPIT

Crystal-facet-dependent denitrosylation: Modulation of NO release from S-nitrosothiols by Cu2O polymorphs

Nitric oxide (NO), a gaseous small molecule generated by the nitric oxide synthase (NOS) enzymes, plays key roles in signal transduction. The thiol groups present in many proteins and small molecules undergo nitrosylation to form the corresponding S-nitrosothiols. The release of NO from S-nitrosothiols is a key strategy to maintain the NO levels in biological systems. However, the controlled release of NO from the nitrosylated compounds at physiological pH remains a challenge. In this paper, we describe the synthesis and NO releasing ability of Cu2O nanomaterials and provide the first experimental evidence that the nanocrystals having different crystal facets within the same crystal system exhibit different activities toward S-nitrosothiols. We used various imaging techniques and time-dependent spectroscopic measurements to understand the nature of catalytically active species involved in the surface reactions. The denitrosylation reactions by Cu2O can be carried out multiple times without affecting the catalytic activity.

Colorimetric and fluorometric determination of homocysteine and cysteine

Colorimetric and fluorometric methods are disclosed for the rapid, accurate, selective, and inexpensive detection of homocysteine, or of homocysteine and cysteine, or of cysteine. The methods may be employed with materials that are readily available commercially. The novel methods are selective for homocysteine, for cysteine, or for total homocysteine and cysteine, and do not cross-react substantially with chemically-related species such as glutathione. The homocysteine-selective method does not have substantial cross-reactivity to the very closely related species cysteine. The cysteine-selective method does not have substantial cross-reactivity to the very closely related species homocysteine. The methods may be used, for example, in a direct assay of human blood plasma for homocysteine levels.

The development of a new class of inhibitors for betaine-homocysteine S-methyltransferase

Betaine-homocysteine S-methyltransferase (BHMT) is an important zinc-dependent methyltransferase that uses betaine as the methyl donor for the remethylation of homocysteine to form methionine. In the liver, BHMT performs to half of the homocysteine remethylation. In this study, we systematically investigated the tolerance of the enzyme for modifications at the "homocysteine" part of the previously reported potent inhibitor (R,S)-5-(3-amino-3-carboxy-propylsulfanyl)-pentanoic acid (1). In the new compounds, which are S-alkylated homocysteine derivatives, we replaced the carboxylic group in the "homocysteine" part of inhibitor 1 with different isosteric moieties (tetrazole and oxadiazolone); we suppressed the carboxylic negative charge by amidations; we enhanced acidity by replacing the carboxylate with phosphonic or phosphinic acids; and we introduced pyrrolidine steric constraints. Some of these compounds display high affinity toward human BHMT and may be useful for further pharmacological studies of this enzyme. Although none of the new compounds were more potent inhibitors than the reference inhibitor 1, this study helped to completely defi ne the structural requirements of the active site of BHMT and revealed the remarkable selectivity of the enzyme for homocysteine.

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.

Identification and characterization of the first ovothiol biosynthetic Enzyme

Ovothiols are histidine-derived thiols that were first isolated from marine invertebrates. We have identified a 5-histidylcysteine sulfoxide synthase (OvoA) as the first ovothiol biosynthetic enzyme and characterized OvoAs from Erwinia tasmaniensis and Trypanosoma cruzi. Homologous enzymes are encoded in more than 80 genomes ranging from proteobacteria to animalia.

Modulation of homocysteine toxicity by S-nitrosothiol formation: A mechanistic approach

The metabolic conversion of homocysteine (HCYSH) to homocysteine thiolactone (HTL) has been reported as the major cause of HCYSH pathogenesis. It was hypothesized that inhibition of the thiol group of HCYSH by S-nitrosation will prevent its metabolic conversion to HTL. The kinetics, reaction dynamics, and mechanism of reaction of HCYSH and nitrous acid to produce S-nitrosohomocysteine (HCYSNO) was studied in mildly to highly acidic pHs. Transnitrosation of this non-protein-forming amino acid by 5-nitrosoglutathione (GSNO) was also studied at physiological pH 7.4 in phosphate buffer. In both cases, HCYSNO formed quantitatively. Copper ions were found to play dual roles, catalyzing the rate of formation of HCYSNO as well as its rate of decomposition. In the presence of a transition-metal ions chelator, HCYSNO was very stable with a halflife of 198 h at pH 7.4. Nitrosation by nitrous acid occurred via the formation of more powerful nitrosating agents, nitrosonium cation (NO +) and dinitrogen trioxide (N2O3). In highly acidic environments, NO+ was found to be the most effective nitrosating agent with a first-order dependence on nitrous acid. N 2O3 was the most relevant nitrosating agent in a mildly acidic environment with a second-order dependence on nitrous acid. The bimolecular rate constants for the direct reactions of HCYSH and nitrous acid, N2O3, and NO+were 9.0 × 10-2, 9.50 × 103, and 6.57 × 1010 M-1 s-1, respectively. These rate constant values agreed with the electrophilic order of these nitrosating agents: HNO2 2O3 +. Transnitrosation of HCYSH by GSNO produced HCYSNO and other products including glutathione (reduced and oxidized) and homocysteineglutathione mixed disulfide. A computer modeling involving eight reactions gave a good fit to the observed formation kinetics of HCYSNO. This study has shown that it is possible to modulate homocysteine toxicity by preventing its conversion to a more toxic HTL by S-nitrosation.