ArticleApplied and environmental microbiology2000
Cofactor regeneration by a soluble pyridine nucleotide transhydrogenase for biological production of hydromorphone.
Article in Applied and environmental microbiology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 63 citations in OpenAlex.
- Review
- A conserved sequence motif in the Escherichia coli soluble FAD-containing pyridine nucleotide transhydrogenase is important for reaction efficiency.The Journal of biological chemistry · 2022Article
- Minimal Pathway for the Regeneration of Redox Cofactors.JACS Au · 2021Article
- Identification and Characterization of a Novel Soluble Pyridine Nucleotide Transhydrogenase from Streptomyces avermitilis.Current microbiology · 2021Article
- Alkaloids in Contemporary Drug Discovery to Meet Global Disease Needs.Molecules (Basel, Switzerland) · 2021Review
- The soluble transhydrogenase UdhA affecting the glutamate-dependent acid resistance system ofBiology open · 2018Article
- NADPH-generating systems in bacteria and archaea.Frontiers in microbiology · 2015Review
- The role of biocatalysis in the asymmetric synthesis of alkaloids.RSC advances · 2013Review
- Efficient one-step production of (S)-1-phenyl-1,2-ethanediol from (R)-enantiomer plus NAD(+)-NADPH in-situ regeneration using engineered Escherichia coli.Microbial cell factories · 2012Article
- Co-expression of P450 BM3 and glucose dehydrogenase by recombinant Escherichia coli and its application in an NADPH-dependent indigo production system.Journal of industrial microbiology & biotechnology · 2007Article
- Biocatalytic hydrogen-borrowing cascades.Chimica oggiArticle
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have applied the soluble pyridine nucleotide transhydrogenase of Pseudomonas fluorescens to a cell-free system for the regeneration of the nicotinamide cofactors NAD and NADP in the biological production of the important semisynthetic opiate drug hydromorphone. The original recombinant whole-cell system suffered from cofactor depletion resulting from the action of an NADP(+)-dependent morphine dehydrogenase and an NADH-dependent morphinone reductase. By applying a soluble pyridine nucleotide transhydrogenase, which can transfer reducing equivalents between NAD and NADP, we demonstrate with a cell-free system that efficient cofactor cycling in the presence of catalytic amounts of cofactors occurs, resulting in high yields of hydromorphone. The ratio of morphine dehydrogenase, morphinone reductase, and soluble pyridine nucleotide transhydrogenase is critical for diminishing the production of the unwanted by-product dihydromorphine and for optimum hydromorphone yields. Application of the soluble pyridine nucleotide transhydrogenase to the whole-cell system resulted in an improved biocatalyst with an extended lifetime. These results demonstrate the usefulness of the soluble pyridine nucleotide transhydrogenase and its wider application as a tool in metabolic engineering and biocatalysis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.