3021-21-4

Basic information

• Product Name: 6-thioinosine 2',3',5'-triacetate
• Synonyms: 6-thioinosine 2',3',5'-triacetate;9-(2-O,3-O,5-O-Triacetyl-β-D-ribofuranosyl)-9H-purine-6-thiol;Einecs 221-169-9;6-Mercaptopurine-9-β-D-ribofuranoside 2',3',5'-Triacetate
• CAS NO: 3021-21-4
• Molecular Formula: C₁₆H₁₈N₄O₇S
• Molecular Weight: 410.40172
• EINECS: 221-169-9
• Mol File: 3021-21-4.mol
• Article Data: 4

Chemical Properties

• Melting Point: 214-216 °C
• Boiling Point: 622.3°Cat760mmHg
• Flash Point: 330.1°C
• Appearance: /
• Density: 1.61g/cm³
• Storage Temp.: -20°C Freezer, Under inert atmosphere
• Solubility: DMSO, Methanol
• PKA: 8.40±0.20(Predicted)
• CAS DataBase Reference: 6-thioinosine 2',3',5'-triacetate(CAS DataBase Reference)
• NIST Chemistry Reference: 6-thioinosine 2',3',5'-triacetate(3021-21-4)
• EPA Substance Registry System: 6-thioinosine 2',3',5'-triacetate(3021-21-4)

Safety Data

• Hazardous Substances Data: 3021-21-4(Hazardous Substances Data)

Usage

Uses

2'',3'',5''-Triacetate derivative of 6-Mercaptopurine-9-β-D-ribofuranoside (M257125), a substrate for adenosine deaminase.

Upstream product

• 157930-09-1 6-Mercaptopurine 
• 13035-61-5 1,2,3,5-tetraacetylribose 
• 5987-73-5 2',3',5'-O-triacetyl-6-chloroinosine 
• 108-24-7 acetic anhydride 
• 574-25-4 6-mercaptopurine riboside 

Downstream Products

• 15981-63-2 2',3',5'-tri-O-acetylnebularine 
• 574-25-4 6-mercaptopurine riboside 
• 14675-48-0 6-methyl-9-(β-D-ribofuranosyl)purine 
• 143330-48-7 6-<<4-benzyl>thio>-9-(β-D-ribofuranosyl)purine 
• 58-61-7 adenosine 
• 1867-73-8 N⁶-methyladenosine 
• 7387-57-7 triacetyladenosine 

Relevant articles and documents

Molecular recognition at the active site of catechol-O-methyltransferase (COMT): Adenine replacements in bisubstrate inhibitors

L-Dopa, the standard therapeutic for Parkinson's disease, is inactivated by the enzyme catechol-O-methyltransferase (COMT). COMT catalyzes the transfer of an activated methyl group from S-adenosylmethionine (SAM) to its catechol substrates, such as L-dopa, in the presence of magnesium ions. The molecular recognition properties of the SAM-binding site of COMT have been investigated only sparsely. Here, we explore this site by structural alterations of the adenine moiety of bisubstrate inhibitors. The molecular recognition of adenine is of special interest due to the great abundance and importance of this nucleobase in biological systems. Novel bisubstrate inhibitors with adenine replacements were developed by structure-based design and synthesized using a nucleosidation protocol introduced by Vorbrueggen and co-workers. Key interactions of the adenine moiety with COMT were measured with a radiochemical assay. Several bisubstrate inhibitors, most notably the adenine replacements thiopyridine, purine, N-methyladenine, and 6-methylpurine, displayed nanomolar IC50 values (median inhibitory concentration) for COMT down to 6 nM. A series of six cocrystal structures of the bisubstrate inhibitors in ternary complexes with COMT and Mg2+ confirm our predicted binding mode of the adenine replacements. The cocrystal structure of an inhibitor bearing no nucleobase can be regarded as an intermediate along the reaction coordinate of bisubstrate inhibitor binding to COMT. Our studies show that solvation varies with the type of adenine replacement, whereas among the adenine derivatives, the nitrogen atom at position 1 is essential for high affinity, while the exocyclic amino group is most efficiently substituted by a methyl group. Copyright

Pyridine-free and solvent-free acetylation of nucleosides promoted by molecular sieves

A practical method for the acetylation of purine and pyrimidine nucleosides employing a combination of acetic anhydride and potassium-exchanged molecular sieves is described. Besides the high yields obtained for the acylated nucleosides, the procedure is simple, inexpensive and environmentally benign, avoiding the use of pyridine or co-solvents as additives. Georg Thieme Verlag Stuttgart.