285560-99-8

Upstream product

• 39170-51-9 7-azabicyclo[4.2.0]oct-4-en-8-one 

Downstream Products

• 131783-54-5 (1S,2R)-2-aminocyclohex-3-enecarboxylic acid hydrochloride 
• 1206630-74-1 ethyl cis-2-aminocyclohex-3-enecarboxylate hydrochloride 

Relevant academic research and scientific papers

Selective syntheses of novel highly functionalized β- aminocyclohexanecarboxylic acids

Highly functionalized β-aminocyclohexanecarboxylate regio- and stereoisomers were synthetized from racemic unsaturated bicyclic β-lactams via enzymatic resolution, selective transformation of the C-C double bond by stereoselective epoxidation, and regiose

Synthesis of orthogonally protected azepane β-amino ester enantiomers

A simple and convenient route is presented for the preparation of regio- and stereoisomers of novel azepane β-amino esters, starting from bicyclic β-lactam isomers. The synthetic procedure consists of dihydroxylation of the olefinic bond of the alicyclic amino esters, followed by NaIO4-mediated cleavage of the diol intermediate and reductive ring closure, which furnishes novel regioisomeric 5-aminoazepane-4-carboxylate and 3-aminoazepane-4-carboxylates. This method also allows the preparation of amino esters with an azepane skeleton in enantiomerically pure form.

Efficient synthesis of 3,4- and 4,5-dihydroxy-2-amino-cyclohexanecarboxylic acid enantiomers

An efficient method for the synthesis of (1S,2R,4R,5S)- and (1R,2R,4R,5S)-2-amino-4,5-dihydroxycyclohexanecarboxylic acids (-)-6 and (-)-9 and (1R,2R,3S,4R)- and (1S,2R,3S,4R)-2-amino-3,4-dihydroxycyclohexanecarboxylic acids (-)-15 and (-)-18 was develope

Vapour-assisted enzymatic hydrolysis of β-lactams in a solvent-free system

A new, solvent-free, vapour-assisted method, developed for the synthesis of carbocyclic cis β-amino acid enantiomers through the Candida antarctica lipase B-catalysed enantioselective (E >200) hydrolysis of β-lactams with 0.5 equiv of H2O at 70 °C, has been demonstrated to be applicable on a preparative scale to produce (±)-2 (the starting racemate for cispentacin), (±)-3 (the starting racemate for 4-tert-butylcispentacin, a new cispentacin analogue) and (±)-7 (the starting racemate for 1,4-ethylene-bridged cispentacin).

Advanced procedure for the enzymatic ring opening of unsaturated alicyclic β-lactams

Enantiopure β-amino acids 1a-4a and β-lactams 1b-4b were prepared simultaneously through the lipolase-catalysed enantioselective ring opening of unsaturated racemic β-lactams (±)-1-(±)-4. High enantioselectivities (E>200) were observed when the reactions

Molecular Basis for the Enantioselective Ring Opening of β-Lactams Catalyzed by Candida antarctica Lipase B

Lipase B from Candida antarctica (CAL-B) catalyzes the slow, but highly enantioselective (E>200), ring-opening alcoholysis of two bicyclic and two 4-aryl-substituted β-lactams. Surprisingly, the rate of the reaction varies with the nature of the alcohols and was fastest with either enantiomer of 2-octanol. A 0.5-g scale reaction with 2-octanol as the nucleophile in diisopropyl ether at 60°C yielded the unreacted β-lactam in 39-46% yield (maximum yield is 50%) with ≥96% ee. The product β-amino acid esters reacted further by polymerization (not isolated or characterized) or by hydrolysis due to small amounts of water in the reaction mixture yielding β-amino acids (7-11% yield, ≥96% ee). The favored enantiomer of all four β-lactams had similar 3-D orientation of substituents, as did most previously reported β-lactams and β-lactones in similar ring-opening reactions. Computer modeling of the ring opening of 4-phenylazetidin-2-one suggests that the reaction proceeds via an unusual substrate-assisted transition state, where the substrate alcohol bridges between the catalytic histidine and the nitrogen of the β-lactam. Computer modeling also suggested that the molecular basis for the high enantioselectivity is a severe steric clash between Ile189 in CAL-B and the phenyl substituent on the slow-reacting enantiomer of the β-lactam.