Microbial degradation of the morphine alkaloids. Purification and characterization of morphine dehydrogenase from Pseudomonas putida M10
نویسندگان
چکیده
منابع مشابه
Nucleotide sequence and over-expression of morphine dehydrogenase, a plasmid-encoded gene from Pseudomonas putida M10.
Pseudomonas putida M10 was originally isolated from factory waste liquors by selection for growth on morphine. The NADP(+)-dependent morphine dehydrogenase that initiates morphine catabolism is encoded by a large plasmid of 165 kb. Treatment of P. putida M10 with ethidium bromide led to the isolation of a putative plasmid-free strain that was incapable of growth on morphine. The structural gene...
متن کاملPurification and characterization of morphinone reductase from Pseudomonas putida M10.
The NADH-dependent morphinone reductase from Pseudomonas putida M10 catalyses the reduction of morphinone and codeinone to hydromorphone and hydrocodone respectively. Morphinone reductase was purified from crude cell extracts to apparent homogeneity in a single affinity-chromatography step using Mimetic Yellow 2. The purified enzyme was a dimeric flavoprotein with two identical subunits of M(r)...
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The purpose of this study was to isolate and characterize Proline Dehydrogenase (ProDH) enzyme frommicroorganisms isolated from soil in Iran. Isolation and screening of L-proline degradative enzymes from soilsamples was carried out. The isolate was characterized by biochemical markers and 16S rRNA geneanalysis. The target ProDH was purified and the effects of pH and temperatur...
متن کاملBiological synthesis of the analgesic hydromorphone, an intermediate in the metabolism of morphine, by Pseudomonas putida M10.
The morphine alkaloid hydromorphone (dihydromorphinone) was identified as an intermediary metabolite in the degradation of morphine by Pseudomonas putida M10. A constitutive NADH-dependent morphinone reductase capable of catalyzing the reduction of the 7,8-unsaturated bond of morphinone and codeinone, yielding hydromorphone and hydrocodone, respectively, was shown to be present in cell extracts...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1991
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2740875