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Application Area

S-Adenosyl-L-cysteine

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

L-Amino Acids

Catalog number

BAT-014229

CAS number

35899-53-7

Molecular Formula

C13H18N6O5S

Molecular Weight

370.38

IUPAC Name

(2R)-2-amino-3-[[(2S,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methylsulfanyl]propanoic acid

Synonyms

Adenosine, 5'-S-(2-amino-2-carboxyethyl)-5'-thio-, (R)-; S-(5'-Deoxyadenosin-5'-yl)-L-cysteine; 5'-S-Adenosyl-L-cysteine; Adenosylcysteine; S-(((2S,3S,4R,5R)-5-(6-Amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl)-L-cysteine

Related CAS

2425611-77-2 (Deleted CAS)

Density

2.00±0.1 g/cm3

Melting Point

~217°C (dec.) (approx)

Boiling Point

778.5±70.0°C at 760 mmHg

InChI

InChI=1S/C13H18N6O5S/c14-5(13(22)23)1-25-2-6-8(20)9(21)12(24-6)19-4-18-7-10(15)16-3-17-11(7)19/h3-6,8-9,12,20-21H,1-2,14H2,(H,22,23)(H2,15,16,17)/t5-,6+,8+,9+,12+/m0/s1

InChI Key

RVFHZLGRQFCOKV-MACXSXHHSA-N

Canonical SMILES

C1=NC(=C2C(=N1)N(C=N2)C3C(C(C(O3)CSCC(C(=O)O)N)O)O)N

S-Adenosyl-L-cysteine (SAC) is a naturally occurring compound that plays a significant role in metabolic processes within the body. It is formed as a byproduct of methylation reactions involving S-adenosyl methionine (SAM), an essential methyl donor. Specifically, SAC is produced when methyl groups are transferred from SAM to various substrates, including DNA, proteins, and lipids. This process is crucial for numerous physiological functions, including gene expression, enzyme activity regulation, and cellular membrane fluidity. SAC accumulates as a regulatory feedback mechanism in these methylation cycles. In biochemical pathways, it is hydrolyzed to homocysteine and adenosine, connecting it to pathways related to cardiovascular health and cellular methylation status.

One of the critical applications of S-Adenosyl-L-cysteine is in the field of epigenetics, where it plays an influential role in gene expression regulation. Methylation of DNA and histones is essential for modulating gene activity and expression. SAC, as a byproduct of these methylation reactions, can influence the availability of SAM and ultimately affect the epigenetic landscape. This makes it a point of interest in studies aimed at understanding and potentially rectifying aberrant gene expression patterns associated with diseases such as cancer, where epigenetic dysregulation is a common hallmark.

In cardiovascular health, the regulation of homocysteine levels is another significant application area for S-Adenosyl-L-cysteine. Elevated levels of homocysteine in the blood have been associated with an increased risk of cardiovascular diseases. Because SAC is part of the metabolic pathway that converts SAM to homocysteine, it can indirectly influence homocysteine concentrations. Through dietary and therapeutic interventions that affect these pathways, SAC may be central to strategies aimed at reducing cardiovascular risk factors by modulating homocysteine levels.

S-Adenosyl-L-cysteine is also pertinent in the study of liver health. The liver is the primary site of methylation reactions involving SAM and subsequent production of SAC. Abnormalities in these pathways can lead to hepatic disorders. Therefore, SAC serves as a biomarker for liver function, and interventions targeting its balance can help address liver diseases. Furthermore, the detoxification processes in the liver involve methylation, making SAC a significant player in maintaining hepatic health and preventing toxic accumulation by ensuring efficient methylation cycles.

Lastly, SAC is increasingly explored in the development of nutritional supplements and pharmaceuticals aimed at enhancing metabolic functions. Given its central role in methylation and homocysteine regulation, SAC is considered a promising compound in supplements targeting metabolic and cognitive enhancement, anti-aging, and systemic detoxification. Its influence on epigenetics also opens potential applications in therapies designed to modulate gene expression for treating neurologic and systemic diseases, marking it as a versatile compound in therapeutic avenues.

1. Affinity labeling of histamine N-methyltransferase by 2',3'-dialdehyde derivatives of S-adenosylhomocysteine and S-adenosylmethionine. Kinetics of inactivation

R T Borchardt, Y S Wu, B S Wu Biochemistry. 1978 Oct 3;17(20):4145-52. doi: 10.1021/bi00613a007.

S-Adenosyl-L-methionine (AdoMet), S-adenosyl-L-homocysteine (L-AdoHcy), and related ribonucleosides have been oxidized with periodic acid to the corresponding 2',3'-dialdehydes. Both AdoMet dialdehyde and L-AdoHcy dialdehyde were observed to rapidly and irreversibly inactivate histamine N-methyltransferase (HMT). Equally active as an irreversible inhibitor was S-adenosyl-D-homocysteine dialdehyde (D-AdoHcy dialdehyde), which is consistent with the known affinity of HMT for S-adenosyl-D-homocysteine (D-AdoHcy). Other analogues of AdoHcy dialdehyde (S-adenosyl-L-cysteine dialdehyde, S-adenosyl-L-homocysteine sulfoxide dialdehyde, and adenosine dialdehyde) also produced irreversible inactivation of HMT, but at predictably slower rates. The corresponding acyclic 2',3'-ribonucleosides, which were obtained by NaBH4 reduction of the ribonucleosides dialdehydes, were found to be very weak, reversible inhibitors of HMT. Kinetic analysis of the inactivation of HMT produced by L-AdoHcy dialdehyde, AdoMet dialdehyde, and D-AdoHcy dialdehyde suggested mechanisms involving the formation of dissociable enzyme-inhibitor complexes prior to irreversible inactivation. Studies using L-[2,8-3H] AdoHcy dialdehyde revealed that incorporation of radioactivity into HMT closely paralleled the loss of enzyme activity. The results of these studies indicate that L-AdoHcy dialdehyde, D-AdoHcy dialdehyde, and AdoMet dialdehyde are affinity labeling reagents for HMT.

2. The structure of two N-methyltransferases from the caffeine biosynthetic pathway

Andrew A McCarthy, James G McCarthy Plant Physiol. 2007 Jun;144(2):879-89. doi: 10.1104/pp.106.094854. Epub 2007 Apr 13.

Caffeine (1,3,7-trimethylxanthine) is a secondary metabolite produced by certain plant species and an important component of coffee (Coffea arabica and Coffea canephora) and tea (Camellia sinensis). Here we describe the structures of two S-adenosyl-l-methionine-dependent N-methyltransferases that mediate caffeine biosynthesis in C. canephora 'robusta', xanthosine (XR) methyltransferase (XMT), and 1,7-dimethylxanthine methyltransferase (DXMT). Both were cocrystallized with the demethylated cofactor, S-adenosyl-L-cysteine, and substrate, either xanthosine or theobromine. Our structures reveal several elements that appear critical for substrate selectivity. Serine-316 in XMT appears central to the recognition of XR. Likewise, a change from glutamine-161 in XMT to histidine-160 in DXMT is likely to have catalytic consequences. A phenylalanine-266 to isoleucine-266 change in DXMT is also likely to be crucial for the discrimination between mono and dimethyl transferases in coffee. These key residues are probably functionally important and will guide future studies with implications for the biosynthesis of caffeine and its derivatives in plants.

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

Roman Rohac, et al. Nat Chem. 2016 May;8(5):491-500. doi: 10.1038/nchem.2490. Epub 2016 Apr 4.

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.