104409-53-2

Upstream product

• 812644-08-9 N⁶-benzoyl-2',3'-O-isopropylidene-9-(β-D-allofuranosyl)adenine 
• 898221-45-9 N-{9-[(2R,3R,4S,5R)-5-((R)-1,2-Dihydroxy-ethyl)-3,4-dihydroxy-tetrahydro-furan-2-yl]-9H-purin-6-yl}-benzamide 
• 812644-10-3 Methanesulfonic acid (R)-1-[(3aR,4S,6R,6aR)-6-(6-benzoylamino-purin-9-yl)-2,2-dimethyl-tetrahydro-furo[3,4-d][1,3]dioxol-4-yl]-2-(tert-butyl-dimethyl-silanyloxy)-ethyl ester 

Relevant academic research and scientific papers

Inactivation of human S-adenosylhomocysteine hydrolase by covalent labeling of cysteine 195 with thionucleoside derivatives

Thionucleosides 1-4 were synthesized for selectively targeting 195Cys of human placental AdoHcy hydrolase. A new series of 5′-thioadenosine derivatives 1-4 were synthesized for selectively targeting 195Cys of human AdoHcy hydrolase. Their incubation with the enzyme resulted in time- and concentration-dependent inactivation, without major modifications of the NAD+/NADH ratio. The electrospray mass analysis of the inactivated enzyme with 1, 2, 3, and 4b showed that inhibition was accompanied by the formation of a specific and covalent labeling of each AdoHcy hydrolase subunit. Proteolytic cleavage (endo-Lys-C) and subsequent peptide characterization of the labeled enzyme revealed that 195Cys was the residue modified during the inactivation process.