Affiliation:
1. Department of Microbiology, Rutgers The State University, New Brunswick, New Jersey 08903
Abstract
Enzyme preparations from
Pseudomonas testosteroni
containing α- and β-hydroxysteroid dehydrogenases catalyzed the oxidation of morphine and codeine by nicotinamide adenine dinucleotide. Morphine was converted in relatively low yield into 14-hydroxymorphinone probably via morphinone as an intermediate. Codeine was converted to codeinone and 14-hydroxycodeinone. Only the conversions at the 6-position were carried out by the hydroxysteroid dehydrogenase. Hydroxylation at the 14-position did occur spontaneously (or enzymatically with a contaminating enzyme) after oxidation at the 6-position.
Publisher
American Society for Microbiology
Subject
General Pharmacology, Toxicology and Pharmaceutics,General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,General Medicine
Cited by
3 articles.
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