312957-76-9

Upstream product

• 100-39-0 benzyl bromide 
• 312957-53-2 1,3,2',6'-tetra-N-tert-butoxycarbonyl-3'-O-tert-butyldimethylsilyl-5,6-O-cyclohexylideneneamine 
• 933-40-4 cycloxexanone dimethyl ketal 
• 24424-99-5 di-tert-butyl dicarbonate 
• 54230-38-5 C₃₈H₆₆N₄O₁₄ 
• 54230-72-7 {(1R,2S,3R,4R,5S)-5-tert-Butoxycarbonylamino-4-[(2R,3R,4R,5S,6R)-3-tert-butoxycarbonylamino-6-(tert-butoxycarbonylamino-methyl)-4,5-dihydroxy-tetrahydro-pyran-2-yloxy]-2,3-dihydroxy-cyclohexyl}-carbamic acid tert-butyl ester 
• 15446-43-2 neamine tetrahydrochloride 

Downstream Products

• 312957-79-2 3'-O-(6''-bromohexyl)-4'-O-benzyl-5,6-O-cyclohexylidene-tetra-N-benzyl-tetra-N-tert-butoxycarbonylneamine 
• 312957-78-1 1,3,2',6'-tetra-N-benzyl-4'-O-benzyl-1,3,2',6'-tetra-N-tert-butoxycarbonyl-3'-O-(5''-bromopentyl)-5,6-O-cyclohexylideneneamine 
• 312957-77-0 1,3,2',6'-tetra-N-benzyl-4'-O-benzyl-1,3,2',6'-tetra-N-tert-butoxycarbonyl-5,6-O-cyclohexylideneneamine 

Relevant academic research and scientific papers

Tethered bisubstrate derivatives as probes for mechanism and as inhibitors of aminoglycoside 3'-phosphotransferases

Aminoglycoside 3'-phosphotransferases [APH(3')s] phosphorylate aminoglycoside antibiotics, a reaction that inactivates the antibiotics. These enzymes are the primary cause of resistance to aminoglycosides in bacteria. APH(3')-Ia operates by a random-equilibrium BiBi mechanism, whereas APH(3')-IIIa catalyzes its reaction by the Theorell-Chance mechanism, a form of ordered BiBi mechanism. Hence, both substrates have to be present in the active site prior to the transfer of phosphate by both mechanisms. Four bisubstrate analogues, compounds 1 - 4, were designed and synthesized as inhibitors for APH(3')s. These compounds are made of adenosine linked covalently to the 3'-hydroxyl of neamine (an aminoglycoside) via all-methylene tethers of 5 - 8 carbons. The K(i) values measured for these compounds indicated that affinities of APH(3')-Ia and APH(3')-IIa for compounds 2 and 8 (six- and seven-carbon tethers, respectively) were the best, and the inhibition constants for the two were comparable.