3024-83-7

Usage

InChI:InChI=1/C3H7NO5S/c4-2(3(5)6)1-10(7,8)9/h2H,1,4H2,(H2-,5,6,7,8,9)

Upstream product

• 52-90-4 L-Cysteine 
• 56-89-3 cysteine disulfide 
• 56-89-3 L-cystine 
• 98022-26-5 sulfo-pyruvic acid 
• 101872-01-9 4-benzoylamino-1,1-dioxo-1λ⁶-isothiazolidin-3-one 
• 59-51-8 DL-methionine 
• 7553-56-2 iodine 
• 7647-01-0 hydrogenchloride 
• 7732-18-5 water 
• 498-40-8 L-Cysteic acid 
• 921-01-7 rac-cysteine 
• 616-91-1 N-acetylcystein 
• 3820-45-9 (R)-2-amino-3-sulfo-propionic acid amide 
• 75893-05-9 H-Cys(Acm)(O)-OH 

Downstream Products

• 99691-25-5 2-amino-3-phenacyloxysulfonyl-propionic acid phenacyl ester 
• 13100-82-8 cysteic acid 
• 751470-47-0 (R)-2-((((9H-fluoren-9-yl)methoxy)carbonyl)amino)-3-sulfopropanoic acid 
• 75-07-0 acetaldehyde 

Relevant academic research and scientific papers

Studies on the aerobic photooxidation of cysteine using riboflavin as a sensitizer: Evidence for the photogeneration of a superoxide anion and hydrogen peroxide

The riboflavin sensitized oxidation of cysteine under an aerobic condition was investigated. The effects of various scavengers, such as superoxide dismutase, catalase, mannitol, sodium azide and potassium ferrocyanide (an electron donor), on the photooxidation were determined. A reaction mechanism involving the superoxide anion is proposed for the photooxidation of cysteine to cysteic acid.

Alotamide A, a novel neuropharmacological agent from the marine cyanobacterium Lyngbya bouillonii

Alotamide A (1), a structurally Intriguing cyclic depsipeptide, was isolated from the marine mat-forming cyanobacterlum Lyngbya bouillonii collected In Papua New Guinea. It features three contiguous peptidic residues and an unsaturated heptaketide with oxidations and methylations unlike those found In any other marine cyanobacterial metabolite. Pure alotamide A (1) displays an unusual calcium influx activation profile In murine cerebrocortical neurons with an EC50 of 4.18 uU.

Synthesis of l-cysteic acid by indirect electrooxidation and an example of paired synthesis: L-cysteic and l-cysteine from l-cystine

This paper studies the synthesis of 1-cysteic acid from 1-cystine by oxidation with electrochemically generated bromine in aqueous-HBr solution. High current efficiency and material yield were obtained. A very interesting process of paired synthesis has been proposed to obtain 1-cysteic acid and 1-cysteine from cystine that improves notably the economical parameters.

Synthesis of L-cysteine and L-cysteic acid by paired electrolysis method

L-Cysteine and L-cysteic acid were synthesized by paired eletrolysis method. A high purity over 98% and high yield over 90% of both products were gained. When current density was 7 A/dm2 and concentration of L-cysteine was 0.6 mol/dm3, the highest current efficiency of anode and cathode was achieved. Total current efficiency was over 180%. The cyclic voltammetry behaviors of hydrobromic acid and cystine showed that a typical EC reaction took place in the anodic cell. The anode reaction and successive chemical reaction accelerated each other to get a high speed and current efficiency.

First steps in the oxidation of sulfur-containing amino acids by hypohalogenation: Very fast generation of intermediate sulfenyl halides and halosulfonium cations

Sulfur-containing amino acids show an extraordinary binding towards HOCl/ClO-. During the process, the Cl is transferred from the O to the S of the amino acid. Met reacts with HOCl one order of magnitude faster than the non-S containing amino acids (k((Met+HOCl))=8.7 · 108 mol-1 dm3 s-1). Instead, Cys reacts as its thiolate (RS-), two orders-of-magnitude faster (k((RS- +HOCl))=1.2 · 109 mol-1 dm3 s-1). Cys reacts also with ClO- (k((RS- +ClO-))=1.9 · 105 mol-1 dm3 s-1). Such processes take place much more readily than the corresponding N-halogenation of the non-sulfur containing amino acids. To our knowledge, these are the first kinetic measurements of the rate of formation of sulfenyl halides and halosulfonium cations in aqueous solution. Sulfenyl chlorides and chlorosulfonium ions derived from amino acids are elusive, and sulfide-type amino acids (Met) eventually yield sulfoxides (MetO), while thiol-type amino acids (Cys) lead to disulfides (Cys/Cys) and sulfonic acids (Cya). The fate of sulfur- containing amino acids upon oxidation with HOCl/ClO- seems to be related to their mutagen-inactivation ability. (C) 2000 Elsevier Science Ltd.

Noncovalently Functionalized Commodity Polymers as Tailor-Made Additives for Stereoselective Crystallization

Stereoselective inhibition of the nucleation and crystal growth of one enantiomer aided by “tailor-made” polymeric additives is an efficient method to obtain enantiopure compounds. However, the conventional preparation of polymeric additives from chiral monomers are laborious and limited in structures, which impedes their rapid optimization and applicability. Herein, we report a “plug-and-play” strategy to facilitate synthesis by using commercially available achiral polymers as the platform to attach various chiral small molecules as the recognition side-chains through non-covalent interactions. A library of supramolecular polymers made up of two vinyl polymers and six small molecules were applied with seeds in the selective crystallization of seven racemates in different solvents. They showed good to excellent stereoselectivity in yielding crystals with high enantiomeric purities in conglomerates and racemic compound forming systems. This convenient, low-cost modular synthesis strategy of polymeric additives will allow for high-efficient, economical resolution of various racemates on different scales.

Krisynomycins, Imipenem Potentiators against Methicillin-Resistant Staphylococcus aureus, Produced by Streptomyces canus

A reinvestigation of the acetone extract of the strain CA-091830 of Streptomyces canus, producer of the imipenem potentiator krisynomycin, resulted in the isolation of two additional analogues, krisynomycins B (1) and C (2), with different chlorination patterns. Genome sequencing of the strain followed by detailed bioinformatics analysis led to the identification of the corresponding biosynthetic gene cluster (BGC) of this cyclic nonribosomal peptide family. The planar structure of the new molecules was determined using HRMS, ESI-qTOF-MS/MS, and 1D and 2D NMR data. Their absolute configuration was proposed using a combination of Marfey's and bioinformatic BGC analyses. The krisynomycins displayed weak to negligible antibiotic activity against methicillin-resistant Staphylococcus aureus (MRSA), which was significantly enhanced when tested in combination with sublethal concentrations of imipenem. The halogenation pattern plays a key role in the antimicrobial activity and imipenem-potentiating effects of the compounds, with molecules having a higher number of chlorine atoms potentiating the effect of imipenem at lower doses.

N-Phenylacetylation and Nonribosomal Peptide Synthetases with Substrate Promiscuity for Biosynthesis of Heptapeptide Variants, JBIR-78 and JBIR-95

JBIR-78 (1) and JBIR-95 (2), both of which are heptapeptide derivatives isolated from Kibdelosporangium sp. AK-AA56, have the same amino acid sequences except for the second amino acid: phenylacetic acid (Paa)-l-Val-d-Asp (1)/d-cysteic acid (2)-l-Ala-(3S)-3-hydroxy-d-Leu-Gly-d-Ala-l-Phe. Heterologous expression of the biosynthetic gene cluster including genes encoding nonribosomal peptide synthetases (NRPS) and in vitro assays with recombinant Orf3, an l-cysteic acid synthase homologue, suggested the single A domain in module 2 activates both l-Asp and l-cysteic acid to yield 1 and 2, respectively, although the substrate specificities of the A domains of NRPSs are usually strict. Biosynthetic mechanism of introduction of N-terminal Paa was also investigated. Recombinant Orf1 and Orf2 similar to subunits of pyruvate dehydrogenase complex catalyzed the conversion of phenylpyruvate into phenylacetyl-CoA together with dihydrolipoyl dehydrogenase whose encoding gene is located outside of the gene cluster. Moreover, we showed that phenylacetyl-CoA was directly condensed with l-Val, which was tethered to a peptidyl carrier protein, at the first condensation domain in the NRPS.

Iodate oxidation of n-acetyl l-cysteine: Application in drug determination and characterization of its oxidation and degradation product by mass spectrometry

A kinetic spectrophotometric method based on the initial rate measurement has been developed for the determination of N-acetyl L-cysteine. The developed method is based on the oxidation of N-acetyl L-cysteine with iodate. The reaction product was studied and characterized using the mass spectrometry and the structure of the product was proposed. From the mass spectrometric studies it was concluded that the oxidation of the drug resulted in the formation of a disulfide. The developed method was validated as per the guidelines of international conference on harmonization. The developed initial rate method was found to be linear in the concentration range of 1.25-30 μg ml-1. The detection and quantitation limits were found to be 0.018 and 0.056 μg ml-1. In the current study, the degradation product of N-acetyl L cysteine was also prepared and identified using mass spectrometry.

Synthesis of sulfonyl chlorides and sulfonic acids in SDS micelles

H2O2/POCl3 is found to be a reactive reagent system that can be used in sodium dodecyl sulfate (SDS) micellar solution in aqueous media for the direct oxidative chlorination of thiol and di-sulfide derivatives to give the desired sulfonyl chlorides. The oxidation of thiols and disulfides to sulfonic acids with this system is also reported. In most cases, these reactions are highly selective, simple, and clean, affording products in excellent yields and high purity. Georg Thieme Verlag Stuttgart · New York.