35899-53-7

Basic information

• Product Name: S-ADENOSYL-L-CYSTEINE
• Synonyms: S-ADENOSYL-L-CYSTEINE;s-(5'-adenosyl)-l-cysteine
• CAS NO: 35899-53-7
• Molecular Formula: C₁₃H₁₈N₆O₅S
• Molecular Weight: 370.38
• Product Categories: A - H;Amino Acids;Modified Amino Acids
• Mol File: 35899-53-7.mol
• Article Data: 4

Chemical Properties

• Melting Point: 217 °C (approx, decomp)
• Boiling Point: 778.5±70.0 °C(Predicted)
• Appearance: /
• Density: 2.00±0.1 g/cm3(Predicted)
• Storage Temp.: −20°C
• PKA: 2.08±0.10(Predicted)
• CAS DataBase Reference: S-ADENOSYL-L-CYSTEINE(CAS DataBase Reference)
• NIST Chemistry Reference: S-ADENOSYL-L-CYSTEINE(35899-53-7)
• EPA Substance Registry System: S-ADENOSYL-L-CYSTEINE(35899-53-7)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 35899-53-7(Hazardous Substances Data)

Usage

Biochem/physiol Actions

S-adenosyl-L-cysteine, an analogue of S-adenosyl-L-homocysteine (L-AdoHcy), is used in the cyrstallizaton of methytransferases such as XMT and DXMT N-methyltransferases.

Upstream product

• 52-90-4 L-Cysteine 
• 892-48-8 5'-deoxy-5'-chloroadenosine 
• 14031-35-7 S-Adenosyl-L-methionine 
• 34592-47-7 L-thioproline 
• 58-61-7 adenosine 
• 24514-56-5 9-((3aR,4R,6S,6aS)-6-(chloromethyl)-2,2-dimethyltetrahydrofuro[3,4-d][1,3]dioxol-4-yl)-9H-purin-6-amine 
• 99051-70-4 S-(2',3'-O-Isopropylideneadenosyl)-L-cysteine 

Downstream Products

• 58-61-7 adenosine 

Relevant articles and documents

Radical SAM Enzyme HydE Generates Adenosylated Fe(I) Intermediates En Route to the [FeFe]-Hydrogenase Catalytic H-Cluster

The H-cluster of [FeFe]-hydrogenase consists of a [4Fe-4S]H-subcluster linked by a cysteinyl bridge to a unique organometallic [2Fe]H-subcluster assigned as the site of interconversion between protons and molecular hydrogen. This [2Fe]H-subcluster is assembled by a set of Fe-S maturase enzymes HydG, HydE and HydF. Here we show that the HydG product [FeII(Cys)(CO)2(CN)] synthon is the substrate of the radical SAM enzyme HydE, with the generated 5′-deoxyadenosyl radical attacking the cysteine S to form a C5′-S bond concomitant with reduction of the central low-spin Fe(II) to the Fe(I) oxidation state. This leads to the cleavage of the cysteine C3-S bond, producing a mononuclear [FeI(CO)2(CN)S] species that serves as the precursor to the dinuclear Fe(I)Fe(I) center of the [2Fe]H-subcluster. This work unveils the role played by HydE in the enzymatic assembly of the H-cluster and expands the scope of radical SAM enzyme chemistry.

Carbon-sulfur bond-forming reaction catalysed by the radical SAM enzyme HydE

Carbon-sulfur bond formation at aliphatic positions is a challenging reaction that is performed efficiently by radical S-adenosyl-L-methionine (SAM) enzymes. Here we report that 1,3-thiazolidines can act as ligands and substrates for the radical SAM enzyme HydE, which is involved in the assembly of the active site of [FeFe]-hydrogenase. Using X-ray crystallography, in vitro assays and NMR spectroscopy we identified a radical-based reaction mechanism that is best described as the formation of a C-centred radical that concomitantly attacks the sulfur atom of a thioether. To the best of our knowledge, this is the first example of a radical SAM enzyme that reacts directly on a sulfur atom instead of abstracting a hydrogen atom. Using theoretical calculations based on our high-resolution structures we followed the evolution of the electronic structure from SAM through to the formation of S-adenosyl-L-cysteine. Our results suggest that, at least in this case, the widely proposed and highly reactive 5′-deoxyadenosyl radical species that triggers the reaction in radical SAM enzymes is not an isolable intermediate.

AN IMPROVED SYNTHESIS OF S-ADENOSYL-L-HOMOCYSTEINE AND RELATED COMPOUNDS

5'-Chloro-5'-deoxy-2',3'-O-isopropylideneadenosine reacts with disodium salts of L-homocysteine, L-cysteine or 3-mercaptopropanoic acid in liquid ammonia to afford 2',3'-O-isopropylidene derivatives which are easily desalted by chromatography on octadecyl-silica column.On acid treatment, the high purity preparations of S-adenosyl-L-homocysteine, S-adenosyl-L-cysteine, and 5'-carboxyethylthio-5'-deoxyadenosine are obtained in respectable yield.