201594-40-3

Upstream product

• 133124-61-5 N-carbonylimidazolyl 1-benzyl-5-nitroimidazole-4-carboxylate 
• 201594-38-9 1-(1-Benzyl-5-nitro-1H-imidazol-4-yl)-4,4-dimethoxy-2-nitro-butan-1-one 
• 69195-96-6 5-nitro-1-(phenylmethyl)-1H-imidazole-4-carboxylic acid 
• 201594-39-0 1-(5-Amino-1-benzyl-1H-imidazol-4-yl)-4,4-dimethoxy-2-nitro-butan-1-one 

Downstream Products

• 201594-42-5 C₃₃H₂₉N₃O₈ 

Relevant academic research and scientific papers

Irreversible, tight-binding inhibition of adenosine deaminase by coformycins: Inhibitor structural features that contribute to the mode of enzyme inhibition

Coformycin analogues 1-6 were synthesized and biochemically screened against adenosine deaminase in order to assess the relative contributions of N-4, N-6, and the N-3 sugar moiety to the mode of enzyme inhibition. Our results indicate that N-4 plays a relatively greater role than N-6 in enzyme tight-binding, and that a benzyl group can substitute for the sugar moiety at N-3. The absence of a sugar or benzyl group at N-3, however, leads to loss of activity. The hydroxyl group at C-8, while crucial for activity, does not alone confer the tight-binding characteristics to coformycins.