1637-71-4

Usage

Uses

Used in Pharmaceutical Industry:
S-SULFO-L-CYSTEINE SODIUM SALT is used as a neuropathological agent for its role as an NMDA receptor ligand. It aids in the research and development of treatments for neurological disorders by modulating the activity of the NMDA receptors, which are crucial in various brain functions and implicated in several neurological conditions.
Used in Research Applications:
In the field of scientific research, S-SULFO-L-CYSTEINE SODIUM SALT serves as a valuable tool for studying the mechanisms of NMDA receptor function and its implications in cognitive processes and neurological diseases. Its use as a research compound facilitates a deeper understanding of receptor interactions and potential therapeutic targets.

InChI:InChI=1/C3H7NO5S2/c5-3(6)2(1-10)4-11(7,8)9/h2,4,10H,1H2,(H,5,6)(H,7,8,9)/t2-/m1/s1

Upstream product

• 56-89-3 L-cystine 
• 52-89-1 l-cysteine hydrochloride 
• 52-90-4 L-Cysteine 
• 7664-93-9 sulfuric acid 
• 7664-41-7 ammonia 
• 7732-18-5 water 
• 407-41-0 L-phosphoserine 
• 67799-13-7 O-ureido-L-serine 

Downstream Products

• 52-90-4 L-Cysteine 
• 7664-93-9 sulfuric acid 
• 498-40-8 L-Cysteic acid 

Relevant academic research and scientific papers

Establishment of an in vitro D-cycloserine-synthesizing system by using O-ureido-L-serine synthase and D-cycloserine synthetase found in the biosynthetic pathway

We have recently cloned a DNA fragment containing a gene cluster that is responsible for the biosynthesis of an antituberculosis antibiotic, D-cycloserine. The gene cluster is composed of 10 open reading frames, designated dcsA to dcsJ. Judging from the sequence similarity between each putative gene product and known proteins, DcsC, which displays high homology to diaminopimelate epimerase, may catalyze the racemization of O-ureidoserine. DcsD is similar to O-acetylserine sulfhydrylase, which generates L-cysteine using O-acetyl-L-serine with sulfide, and therefore, DcsD may be a synthase to generate O-ureido-L-serine using O-acetyl-L-serine and hydroxyurea. DcsG, which exhibits similarity to a family of enzymes with an ATP-grasp fold, may be an ATP-dependent synthetase converting O-ureido-D-serine into D-cycloserine. In the present study, to characterize the enzymatic functions of DcsC, DcsD, and DcsG, each protein was overexpressed in Escherichia coli and purified to near homogeneity. The biochemical function of each of the reactions catalyzed by these three proteins was verified by thin-layer chromatography (TLC), high-performance liquid chromatography (HPLC), and, in some cases, mass spectrometry. The results from this study demonstrate that by using a mixture of the three purified enzymes and the two commercially available substrates O-acetyl-L-serine and hydroxyurea, synthesis of D-cycloserine was successfully attained. These in vitro studies yield the conclusion that DcsD and DcsG are necessary for the syntheses of O-ureido-L-serine and D-cycloserine, respectively. DcsD was also able to catalyze the synthesis of L-cysteine when sulfide was added instead of hydroxyurea. Furthermore, the present study shows that DcsG can also form other cyclic D-amino acid analogs, such as D-homocysteine thiolactone. Copyright

Unnatural amino acid synthesis by thermostable O-phospho-L-serine sulfhydrylase from hyperthermophilic archaeon Aeropyrum pernix K1

O-Acetyl-L-serine sulfhydrylase (OASS) from plants and bacteria synthesizes cysteine and unnatural amino acids that are important building blocks for active pharmaceuticals and agrochemicals. A thermostable O-phospho-L-serine sulfhydrylase from hyperthermophilic archaeon Aeropyrum pernix K1 (OPSSAp) exhibits a function similar to OASS. In the present study, we examined the synthesis of various unnatural amino acids using OPSSAp and demonstrated OPSSAp could efficiently synthesize various sulfur-containing amino acids. OPSSAp would be useful for industrial production of biologically important unnatural amino acids.