Biological synthesis of the analgesic hydromorphone, an intermediate in the metabolism of morphine, by Pseudomonas putida M10

Hailes, A M; Bruce, Neil C.

doi:10.1128/aem.59.7.2166-2170.1993

Cited by 33 publications

(14 citation statements)

References 18 publications

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“…Pseudomonas putida M10, was originally isolated by selective enrichment of industrial waste liquors [3] and was grown in the same manner as described in [7]. Media contained 20 mM glucose or 50 mM acetate as a carbon and energy source.…”

Section: Bacterial Strains and Culture Conditionsmentioning

confidence: 99%

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Transformations of codeine to important semisynthetic opiate derivatives by Pseudomonas putida m10

Lister¹

1999

FEMS Microbiology Letters

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A biotransformation mixture which contained codeine and washed cells of Pseudomonas putida M10 gave rise to a number of transformation products that are of clinical importance which included hydrocodone, dihydrocodeine and 14L-hydroxycodeine. Incubations with the same organism and codeinone gave rise to 14L-hydroxycodeinone and 14L-hydroxycodeine. Cell-free extracts and membrane fractions of P. putida M10 were shown to catalyse the 14L-hydroxylation of codeinone. In addition, the potent analgesic oxycodone was shown to be produced from 14L-hydroxycodeinone. ß

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Section: Bacterial Strains and Culture Conditionsmentioning

confidence: 99%

“…A fermentation (50 l) of P. putida M10 grown on a de¢ned mineral medium [7] plus 20 mM glucose, was carried out in a 75 l fermenter at 30³C and pH 7.0, with continuous sparging with air. The fermentation was fed with an additional 50 mM glucose over the period of growth (18 h).…”

Section: Codeine Biotransformationmentioning

confidence: 99%

Transformations of codeine to important semisynthetic opiate derivatives by Pseudomonas putida m10

Lister¹

1999

FEMS Microbiology Letters

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“…The forward primer 5'-TGCTACTCATATGCCGGATACATCCTTCTCC-3' consisted of seven random bases to allow effective cutting by NdeI, followed by the introduced NdeI site and the first 21 bases of morB. The reverse primer 5 (Figure 1), and pT7-7 cut with NdeI and ClaI. The resulting construct was designated pMORBI.…”

Section: Assembly Of An Intact Morb Gene and Expression Of Morphinonementioning

confidence: 99%

“…This question is currently under investigation in our laboratory. We are also working towards the use of morphine dehydrogenase and morphinone reductase as biocatalysts for the preparation of semisynthetic opiate pharmaceuticals such as hydromorphone and hydrocodone [5].…”

Section: Assembly Of An Intact Morb Gene and Expression Of Morphinonementioning

confidence: 99%

“…The requirement for enzymes specifically active against morphine for use in a biosensor for the detection of illicit heroin [1,2] led to the isolation of the Gram-negative bacterium Pseudomonas putida M10 from opiate factory waste liquor [31. This organism was shown to transform morphine initially through the action of two constitutively expressed enzymes, morphine dehydrogenase [4] and morphinone reductase [5] (Scheme 1). Morphine dehydrogenase has been purified and characterized [4] and the structural gene, located -on a large natural plasmid, has been cloned and sequenced [6].…”

Section: Introductionmentioning

confidence: 99%

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Bacterial morphinone reductase is related to Old Yellow Enzyme

French

Bruce

1995

Biochemical Journal

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Morphinone reductase, produced by Pseudomonas putida M10, catalyses the NADH-dependent saturation of the carbon-carbon double bond of morphinone and codeinone, and is believed to be involved in the metabolism of morphine and codeine. The structural gene encoding morphinone reductase, designated morB, was cloned from Ps. putida M10 genomic DNA by the use of degenerate oligonucleotide probes based on elements of the amino acid sequence of the purified enzyme. Sequence analysis and structural characteristics indicated that morphinone reductase is related to the flavoprotein alpha/beta-barrel oxidoreductases, and is particularly similar to Old Yellow Enzyme of Saccharomyces spp. and the related oestrogen-binding protein of Candida albicans. Expressed sequence tags from several plant species show high homology to these enzymes, suggesting the presence of a family of enzymes conserved in plants and fungi. Although related bacterial proteins are known, morphinone reductase appears to be more similar to the eukaryotic proteins. Morphinone reductase was overexpressed in Escherichia coli, and has potential applications for the industrial preparation of semisynthetic opiates.

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Enzymes, Enolate Reductases “Old Yellow Enzyme”

Hall

Yanto

Bommarius

2010

Encyclopedia of Industrial Biotechnology

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Reported enoate reductase activity is mostly displayed by enzymes belonging to the “Old Yellow Enzyme” family of flavoproteins. They have received increased interest over the last couple of years due to their huge potential in biocatalysis. These FMN‐containing enzymes catalyze the asymmetric reduction of activated C═C bonds at the expense of a nicotinamide cofactor, producing up to two chiral centers. They are also involved in other reductive processes, such as cleavage of nitrate esters, reduction of aromatic nitro groups, and even reduction of alkynes. Increasing knowledge about this family of biocatalysts together with recent advances in biotechnology render the enoate reductases a tool of choice for industrial applications, as catalyzed reactions are usually chemo‐, regio‐ and stereo‐selective, and the enzymes most importantly display a wide substrate spectrum. With enzymatic reactions and mechanisms being generally clearly understood, the efficient production of a number of enantiopure compounds via recycling of the cofactor is now feasible.

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Biological synthesis of the analgesic hydromorphone, an intermediate in the metabolism of morphine, by Pseudomonas putida M10

Cited by 33 publications

References 18 publications

Transformations of codeine to important semisynthetic opiate derivatives by Pseudomonas putida m10

Transformations of codeine to important semisynthetic opiate derivatives by Pseudomonas putida m10

Bacterial morphinone reductase is related to Old Yellow Enzyme

Enzymes, Enolate Reductases “Old Yellow Enzyme”

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