32216-02-7

Upstream product

• 3014-58-2 dimethyl (exo,endo)-bicyclo[2.2.1]hept-5-ene-2,3-dicarboxylate 
• 1200-88-0 norbornene-5,6-dicarboxylic acid 

Downstream Products

• 198223-94-8 (1S,2R,3R,4R)-Bicyclo[2.2.1]hept-5-ene-2,3-dicarboxylic acid bis-[((S)-2-hydroxy-1-phenyl-ethyl)-amide] 
• 198224-00-9 (1S,2R,3R,4R)-Bicyclo[2.2.1]hept-5-ene-2,3-dicarboxylic acid bis-[((S)-2-chloro-1-phenyl-ethyl)-amide] 

Relevant academic research and scientific papers

Resolution of (±)-Bicyclo[2.2.1]hept-5-ene-trans-2,3-dicarboxylic Acid: Crystal Structure of Its Cinchoninium Salt

Abstract: Single crystals of (+)-cinchoninium (+)-bicyclo[2.2.1]hept-5-ene-trans-2-carboxyl-3-carboxylate (S,S)-2 were obtained upon resolution of racemic (±)-bicyclo[2.2.1]hept-5-ene-trans-2,3-dicarboxylic acid rac-1 with (+)-cinchonine. An X ray diffraction analysis established the most important secondary interactions between the ions that are deemed responsible for the diastereomeric separation process. From (S,S)-2 enantiomerically pure (+)-bicyclo[2.2.1]hept-5-ene-trans-2,3-dicarboxylic acid (S,S)-1 was isolated in 72 % yield. Graphical Abstract: An X-ray diffraction analysis of (+)-cinchoninium (+)-bicyclo[2.2.1]hept-5-ene-trans-2-carboxyl-3-carboxylate (S,S)-2 established the most important secondary interactions between the ions that are deemed responsible for the diastereomeric separation process.[Figure not available: see fulltext.]

Enzymatic optical resolution of norbornanecarboxylic esters using Pig Liver Esterase

The hydrolysis of a series of norbornane-type carboxylic esters catalyzed by pig liver esterase (PLE) has been investigated.It was found that an exo-ester function (syn to the C7 methylene group) is hydrolyzed with high preference.Enantioselective hydrolysis can be accomplished when a vicinal carbonyl-containing function (ester, formyl, acetyl) is present in a trans position with respect to the exo ester.The regiospecifity of the enzymatic hydrolysis has been used for the separation of exo/endo mixtures of the cycloadducts derived from cyclopentadiene and alkene esters.The regiospecifity and enantioselectivity of the enzymatic hydrolysis of norbornane-type esters were analyzed in terms of Tamm's substrate model and also by Griengl's method.

Enzymatic Preparation of Optically Active Bicycloheptene Derivatives, Building Blocks of Terpenoid Natural Products. An Attractive Alternative to Enantioselective Diels-Alder Syntheses

Bicycloheptene derivatives (1)-(3), building blocks of terpenoid natural products, have been prepared with high enantiometric purities by enzymatic hydrolysis of their racemic esters in the presence of porcine liver esterase (PLE) and an ester hydrolase from Pseudomonas sp. (SAM-II).

Chiral rhodium-diphosphine catalyst capable of catalytic reduction of a tetramisole precursor to give a significant excess of the desired S-(-)isomer, levamisole

A soluble, chiral, rhodium-containing catalyst which permits the catalytic reduction of prochiral 3-acyl-1-(2-alkoxyethyl)-4-phenyl-2-imidazolinones to chiral 3-acylimidazolidinones with a substantial excess of the desired S optical isomer. The 3-acylimidazolidinones may in turn be substantially converted to levamisole, and S isomer of tetramisole. The resolution of tetramisole to remove the R isomer is thus avoided.