Enzymatic transformation of morphine by hydroxysteroid dehydrogenase from Pseudomonas testosteroni.
Eznyme preparations from Pseudomonas testosteroni containing alpha- and beta- 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 carred out by the hydroxysteroid dehydrogenase. Hydroxylation at the 14-position did occur spontaneously (or enzymatically with a contaminating enzyme) ater oxidation at the 6-position.
D000738:Androsterone / Q000494:pharmacology; D002474:Cell-Free System; D003061:Codeine / Q000031:analogs & derivatives / Q000378:metabolism; D006913:Hydroxysteroid Dehydrogenases / Q000378:metabolism*; D007527:Isoenzymes / Q000378:metabolism*; D009020:Morphine / Q000378:metabolism*; D009022:Morphine Derivatives / Q000378:metabolism; D009243:NAD / Q000378:metabolism; D010084:Oxidation-Reduction; D011549:Pseudomonas / Q000201:enzymology*; D013739:Testosterone / Q000494:pharmacology
D007527:Isoenzymes; D009022:Morphine Derivatives; D009243:NAD; D013739:Testosterone; D009020:Morphine; D000738:Androsterone; D006913:Hydroxysteroid Dehydrogenases; D003061:Codeine