title: Enantiospecificity of immobilized horse liver alcohol dehydrogenase.
abstract: Horse liver alcohol dehydrogenase (EC 1.1.1.1) accepts a wide structural range of substrates but exhibits a well-defined and predictable stereospecificity. The enzyme was immobilized on CNBr-activated Sepharose 4B. The immobilized preparation was used to oxidize the enantiomeric pair of cis-1,2-bis(hydroxymethyl)-3-cyclopentene enantioselectively to a mixture of two diastereoisomeric chiral lactones. The two diastereoisomeric products are readily separated and each was isolated with an optical yield of greater than 99%.
mesh_terms: D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000818:Animals; D003517:Cyclopentanes; D004800:Enzymes, Immobilized; D006736:Horses; D066298:In Vitro Techniques; D008099:Liver / Q000201:enzymology*; D013237:Stereoisomerism; D013379:Substrate Specificity
chemical_list: C043428:1,2-bis(hydroxymethyl)-3-cyclopentene; D003517:Cyclopentanes; D004800:Enzymes, Immobilized; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase