630108-98-4

Upstream product

• 630108-94-0 N-tert-butoxycarbonyl-L-homocysteine tert-butyl ester 
• 630108-95-1 (4R,5R,6R)-2,6-bis(p-methoxybenzyloxy)-4-(p-methoxybenzyloxymethyl)-[1,3,2]dioxathiepane 2,2-dioxide 
• 532-20-7 D-lyxose 
• 630108-92-8 allyl 2,3,5-tris(p-methoxybenzyl)-D-lyxofuranoside 
• 630108-93-9 (2R,3S,4R)-2,3,5-tris(4-methoxybenzyloxy)-pentane-1,4-diol 
• 24424-99-5 di-tert-butyl dicarbonate 
• 773896-71-2 allyl α/β-D-lyxofuranoside 
• 130981-51-0 (2S,2'S)-4,4'-disulfanediylbis(2-(tert-butoxycarbonyl)amino)butanoic acid 
• 601491-40-1 N,N′-di(tert-butoxycarbonyl)-L-homocystine di(tert-butyl)ester 

Relevant academic research and scientific papers

Catalytic Mechanism of S-Ribosylhomocysteinase (LuxS): Direct Observation of Ketone Intermediates by 13C NMR Spectroscopy

S-Ribosylhomocysteinase (LuxS) catalyzes the cleavage of the thioether linkage of S-ribosylhomocysteine (SRH) to produce l-homocysteine and 4,5-dihydroxy-2,3-pentanedione (DHPD). This is a key step in the biosynthetic pathway of the type II autoinducer (AI-2) in both Gram-positive and Gram-negative bacteria. Previous studies demonstrated that LuxS contains a catalytically essential Fe2+ ion. The catalytic mechanism of LuxS was investigated using 2- and 3-13C-labeled SRH as substrate and 13C NMR spectroscopy. These studies revealed the presence of 2- and 3-keto intermediates in the catalytic pathway. The 2-keto intermediate was chemically synthesized, and its chemical and kinetic competence was demonstrated. The results support a catalytic mechanism in which the metal ion catalyzes an internal redox reaction, shifting the carbonyl group from the C-1 position to the C-3 position. Subsequent β-elimination at the C-4 and C-5 positions releases homocysteine as a free thiol. The results also suggest that Cys-84 and Glu-57 are the possible general acids/bases for proton transfer during catalysis and that the keto intermediates are released from the enzyme active site before rebinding and completion of the reaction. Copyright