2906-60-7

Usage

Chemical Properties

beige to light brown fine crystalline powder

Upstream product

• 1003-10-7 Thiobutyrolactone 
• 2537-66-8 5,6-dithia-decanedioic acid diamide 
• 28341-54-0 4-(4-nitrophenoxy)butanoic acid 
• 13095-73-3 4-mercaptobutyric acid 
• 454-29-5 2-amino-4-mercaptobutyric acid 
• 89988-29-4 4,4-dithiobutanenitrile 

Downstream Products

• 13095-73-3 4-mercaptobutyric acid 
• 30453-20-4 4,4'-dithiodibutan-1-ol 
• 1102-39-2 4,5-Dithia-octandicarbonsaeure-(1,8)-dianilid 
• 863239-34-3 C₃₀H₄₂N₄O₆S₂ 
• 1052647-55-8 5-[2-amino-6-(3-carboxypropylsulfanyl)pyrimidin-4-yl]-2,4-dimethylbenzoic acid tert-butyl ester 
• 1201937-86-1 C₅₅H₆₃NO₁₇S₂ 
• 1201937-87-2 C₅₃H₆₅NO₁₇S₂ 

Relevant academic research and scientific papers

Structure-activity study of new inhibitors of human betaine-homocysteine S-methyltransferase

Betaine-homocysteine S-methyltransferase (BHMT) catalyzes the transfer of a methyl group from betaine to L-homocysteine, yielding dimethylglycine and L-methionine. In this study, we prepared a new series of BHMT inhibitors. The inhibitors were designed to mimic the hypothetical transition state of BHMT substrates and consisted of analogues with NH, N(CH3), or N(CH 3)2 groups separated from the homocysteine sulfur atom by a methylene, ethylene, or a propylene spacer. Only the inhibitor with the N(CH3) moiety and ethylene spacer gave moderate inhibition. This result led us to prepare two inhibitors lacking a nitrogen atom in the S-linked alkyl chain: (RS,RS)-5-(3-amino-3-carboxypropylthio)-3-methylpentanoic acid and (RS)-5-(3-amino-3-carboxypropylthio)-3,3-dimethylpentanoic acid. Both of these compounds were highly potent inhibitors of BHMT. The finding that BHMT does not tolerate a true betaine mimic within these inhibitors, especially the nitrogen atom, is surprising and evokes questions about putative conformational changes of BHMT upon the binding of the substrates/products and inhibitors.

Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase

S-Ribosylhomocysteinase (LuxS) catalyzes the cleavage of the thioether linkage in S-ribosylhomocysteine (SRH) to produce homocysteine and 4,5-dihydroxy-2,3-pentanedione, the precursor of autoinducer 2. Inhibitors of LuxS should interfere with bacterial interspecies communication and potentially provide a novel class of antibacterial agents. LuxS utilizes a divalent metal ion as a Lewis acid during catalysis. In this work, a series of structural analogues of the substrate SRH and a 2-ketone intermediate were designed and synthesized. Kinetic studies indicate that the compounds act as reversible, competitive inhibitors against LuxS, with the most potent inhibitors having K1 values in the submicromolar range. These represent the most potent LuxS inhibitors that have been reported to date. Cocrystal structures of LuxS bound with two of the inhibitors largely confirmed the design principles, i.e., the importance of both the homocysteine and ribose moieties in high-affinity binding to the LuxS active site.