643760-41-2

Upstream product

• 643760-51-4 6-benzyloxymethyl-5-chloro-2,2-dimethyl-3a,6a-dihydro-cyclopenta[1,3]dioxol-4-one 
• 117307-62-7 (3aR,6aR)-6-Benzyloxymethyl-2,2-dimethyl-4,6a-dihydro-3aH-cyclopenta[d][1,3]dioxol-4-one 
• 124-63-0 methanesulfonyl chloride 
• 643760-40-1 6-benzyloxymethyl-5-chloro-2,2-dimethyl-4,6a-dihydro-3aH-cyclopenta[1,3]dioxol-4-ol 

Downstream Products

• 643760-45-6 9-(6-benzyloxymethyl-5-chloro-2,2-dimethyl-4,6a-dihydro-3aH-cyclopenta[1,3]dioxol-4-yl)-9H-purin-6-ylamine 

Relevant academic research and scientific papers

X-ray crystal structure and binding mode analysis of human S-adenosylhomocysteine hydrolase complexed with novel mechanism-based inhibitors, haloneplanocin A analogues

The X-ray crystal structure of human S-adenosylhomocysteine (AdoHcy) hydrolase was first determined as a tetrameric form bound with the novel mechanism-based inhibitor fluoroneplanocin A (4b). The crystallized enzyme complex showed the closed conformation

Synthesis and biological evaluation of halo-neplanocin A as novel mechanism-based inhibitors of S-Adenosylhomocysteine hydrolase

Halogenated analogues of neplanocin A were synthesized from the key intermediate 1, among which fluoro-neplanocin A was found to be novel mechanism-based irreversible inhibitor of S-Adenosylhomocysteine hydrolase.