53186-57-5

Basic information

• Product Name: S-adenosyl-3-thiopropylamine
• Synonyms: S-adenosyl-3-thiopropylamine;5′-[(3-Aminopropyl)thio]-5′-deoxyadenosine;dcAdoHcy;dc-SAH;decarboxylated S-Adenosyl-L-homocysteine;S-(5′-Adenosyl)-3-thiopropylamine;(2S,3S,4R,5R)-2-(3-aminopropylsulfanylmethyl)-5-(6-aminopurin-9-yl)oxolane-3,4-diol
• CAS NO: 53186-57-5
• Molecular Formula: C13H20N6O3S
• Molecular Weight: 340.4
• Mol File: 53186-57-5.mol
• Article Data: 6

Chemical Properties

• Boiling Point: 683.7°Cat760mmHg
• Flash Point: 367.3°C
• Appearance: /
• Density: 1.78g/cm³
• Storage Temp.: 2-8°C
• CAS DataBase Reference: S-adenosyl-3-thiopropylamine(CAS DataBase Reference)
• NIST Chemistry Reference: S-adenosyl-3-thiopropylamine(53186-57-5)
• EPA Substance Registry System: S-adenosyl-3-thiopropylamine(53186-57-5)

Safety Data

• Hazard Codes: T+
• Statements: 28
• Safety Statements: 28-36/37-45
• RIDADR: UN 2811 6.1 / PGII
• WGK Germany: 3
• Hazardous Substances Data: 53186-57-5(Hazardous Substances Data)

Usage

Uses

S-(5′-Adenosyl)-3-thiopropylamine has been used as a calibrant solution to spike human urine samples for solid-phase extraction studies. It has also been used as an analyte in capillary electrophoresis (CE) and micellar electrokinetic chromatography (MEKC).

Definition

ChEBI: A thioadenosine that is adenosine in which the hydroxy group at C-5' is replaced by a 3-aminopropyl group.

Biochem/physiol Actions

S-(5′-Adenosyl)-3-thiopropylamine or S-adenosyl-L-homocysteine comprises base, sugar or amino acid. It acts as an inhibitor for spermidine synthase and spermine synthase.

Upstream product

• 3483-12-3 diothiothreitol 
• 115465-32-2 5'-deoxy-5'-[3-(phthalimido)propylthio]adenosine 
• 109-79-5 n-butanethiol 
• 892-48-8 5'-deoxy-5'-chloroadenosine 
• 462-47-5 mercapto-3 propylamine 
• 58-61-7 adenosine 
• 263715-50-0 5'-deoxy-2',3'-O-isopropylidene-5'-[3-(phthalimido)propylthio]adenosine 
• 84365-04-8 5'-acetylthio-5'-deoxy-2',3'-O-isopropylidene adenosine 
• 362-75-4 2',3'-isopropylidene adenosine 
• 23909-16-2 3-benzylmercaptopropylamine 

Relevant articles and documents

Efficient synthesis of s-adenosyl-L-homocysteine natural product analogues and their use to elucidate the structural determinant for cofactor binding of the DNA methyltransferase M·HhaI

5'-Acetylthio-5'-deoxy-2',3'-O-isopropylideneadenosine (8) was directly prepared from commercially available 2',3'-O-isopropylideneadenosine (7) and thioacetic acid under Mitsunobu conditions in almost quantitative yield. In situ cleavage of the acetylthio function of 8 followed by coupling with different alkyl bromides proceeded with high yields. Deprotection of the obtained 5'-thionucleosides yielded the S-adenosyl-L-homocysteine analogues decarboxylated AdoHcy (11), deaminated AdoHcy (14) and 5'- [3(cyano)propylthio]-5'-deoxyadenosine (16) in good overall yields. Direct deprotection of the thionucleoside 8 delivered 5'-thio-5'-deoxyadenosine (18) in excellent yield. In addition, binding constants of these AdoHcy analogues and the DNA methyltransferase M·HhaI were determined in a fluorescence assay.

SAH derived potent and selective EZH2 inhibitors

A series of novel enhancer of zeste homolog 2 (EZH2) inhibitors was designed based on the chemical structure of the histone methyltransferase (HMT) inhibitor SAH (S-adenosyl-l-homocysteine). These nucleoside-based EZH2 inhibitors blocked the methylation of nucleosomes at H3K27 in biochemical assays employing both WT PRC2 complex as well as a Y641N mutant PRC2 complex. The most potent compound, 27, displayed IC50's against both complexes of 270 nM and 70 nM, respectively. To our knowledge, compound 27 is the most potent SAH-derived inhibitor of the EZH2 PRC2 complex yet identified. This compound also displayed improved potency, lipophilic efficiency (LipE), and selectivity profile against other lysine methyltransferases compared with SAH.

Constrained (l-)-S-adenosyl-l-homocysteine (SAH) analogues as DNA methyltransferase inhibitors

Potent SAH analogues with constrained homocysteine units have been designed and synthesized as inhibitors of human DNMT enzymes. The five membered (2S,4S)-4-mercaptopyrrolidine-2-carboxylic acid, in 1a, was a good replacement for homocysteine, while the corresponding six-member counterpart was less active. Further optimization of 1a, changed the selectivity profile of these inhibitors. A Chloro substituent at the 2-position of 1a, compound 1d, retained potency against DNMT1, while N6 alkylation, compound 7a, conserved DNMT3b2 activity. The concomitant substitutions of 1a at both 2- and N6 positions reduced activity against both enzymes.