840476-05-3

Basic information

• Product Name: (S)-2-Amino-4-[(3aS,4S,6R,6aR)-6-(6-benzoylamino-purin-9-yl)-2,2-dimethyl-tetrahydro-furo[3,4-d][1,3]dioxol-4-ylmethylsulfanyl]-butyric acid
• Synonyms: (S)-2-Amino-4-[(3aS,4S,6R,6aR)-6-(6-benzoylamino-purin-9-yl)-2,2-dimethyl-tetrahydro-furo[3,4-d][1,3]dioxol-4-ylmethylsulfanyl]-butyric acid
• CAS NO: 840476-05-3
• Molecular Weight: 528.589
• Mol File: 840476-05-3.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: (S)-2-Amino-4-[(3aS,4S,6R,6aR)-6-(6-benzoylamino-purin-9-yl)-2,2-dimethyl-tetrahydro-furo[3,4-d][1,3]dioxol-4-ylmethylsulfanyl]-butyric acid(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-2-Amino-4-[(3aS,4S,6R,6aR)-6-(6-benzoylamino-purin-9-yl)-2,2-dimethyl-tetrahydro-furo[3,4-d][1,3]dioxol-4-ylmethylsulfanyl]-butyric acid(840476-05-3)
• EPA Substance Registry System: (S)-2-Amino-4-[(3aS,4S,6R,6aR)-6-(6-benzoylamino-purin-9-yl)-2,2-dimethyl-tetrahydro-furo[3,4-d][1,3]dioxol-4-ylmethylsulfanyl]-butyric acid(840476-05-3)

Safety Data

• Hazardous Substances Data: 840476-05-3(Hazardous Substances Data)

Upstream product

• 68200-72-6 N⁶-benzoyl-5'-deoxy-5'-iodo-2',3'-O-isopropylideneadenosine 
• 626-72-2 L-homocystine 
• 39947-04-1 N-6-benzoyl-2',3'-O-isopropylideneadenosine 
• 39947-05-2 ((3aR,4R,6R,6aR)-6-(6-benzamido-9H-purin-9-yl)-2,2-dimethyltetrahydrofuro[3,4-d][1,3]dioxol-4-yl)methyl 4-methylbenzenesulfonate 

Relevant articles and documents

Determinants of cofactor binding to DNA methyltransferases: Insights from a systematic series of structural variants of S-adenosylhomocysteine

S-Adenosylmethionine (AdoMet) is a commonly used cofactor, second only to ATP in the variety of reactions in which it participates. It is the methyl donor in the majority of methyl transfer reactions, including methylation of DNA, RNA, proteins and small molecules. Almost all structurally characterised methyltransferases share a conserved AdoMet-dependent methyltransferase fold, in which AdoMet is bound in the same orientation. Although potential interactions between the cofactor and methyltransferases have been inferred from crystal structures, there has not been a systematic study of the contributions of each functional group to binding. To explore the binding interaction we synthesised a series of seven analogues of the methyltransferase inhibitor S-adenosylhomocysteine (AdoHcy), each containing a single modification, and tested them for the ability to inhibit methylation by HhaI and HaeIII DNA methyltransferase. Comparison of the Ki values highlights the structural determinants for cofactor binding, and indicates which nucleoside and amino acid functional groups contribute significantly to AdoMet binding. An understanding of the binding of AdoHyc to methyltransferases will greatly assist the design of AdoMet inhibitors.