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睾丸酮假单胞菌中羟基类固醇脱氢酶对吗啡的酶促转化。

Enzymatic transformation of morphine by hydroxysteroid dehydrogenase from Pseudomonas testosteroni.

作者信息

Liras P, Kasparian S S, Umbreit W W

出版信息

Appl Microbiol. 1975 Oct;30(4):650-6. doi: 10.1128/am.30.4.650-656.1975.

Abstract

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.

摘要

来自睾丸酮假单胞菌的含有α-和β-羟基类固醇脱氢酶的酶制剂催化了烟酰胺腺嘌呤二核苷酸对吗啡和可待因的氧化反应。吗啡可能经吗啡酮作为中间体以相对较低的产率转化为14-羟基吗啡酮。可待因转化为可待因酮和14-羟基可待因酮。只有6位的转化是由羟基类固醇脱氢酶进行的。14位的羟基化在6位氧化后确实会自发发生(或由一种污染酶酶促发生)。

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本文引用的文献

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PHYSICAL AND CHEMICAL CHARACTERIZATION OF HYDROXYSTEROID DEHYDROGENASES FROM PSEUDOMONAS TESTOSTERONI.
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PURIFICATION OF STEROID-INDUCED ENZYMES FROM PSEUDOMONAS TESTOSTERONI.
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Enzymatic formation of 3 alpha-hydroxysteroids.
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Purification and substrate specificities of bacterial hydroxysteroid dehydrogenases.
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