Evidence map›Paper›PMID 42477771›Full record

ArticleJournal of biological engineering2026

A versatile yeast platform for N-demethylation of therapeutic alkaloids.

Daniel J Yaw, Xu Li, Katrine B Kampmann, Kenny W L Lam, Siyi Xue, Jørgen Hansen, Tim A Bowser, Sandra E Kentish, Sally L Gras

Abstract read
In one paragraph

Article in Journal of biological engineering, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Daniel J YawDepartment of Chemical Engineering, The University of Melbourne, Parkville, VIC, 3010, Australia.ORCID http://orcid.org/0000-0002-6214-7257
Xu LiDepartment of Chemical Engineering, The University of Melbourne, Parkville, VIC, 3010, Australia.ORCID http://orcid.org/0000-0003-3317-9257
Katrine B KampmannRiver Stone Biotech ApS, Fruebjergvej 3, København Ø, 2100, Denmark.ORCID http://orcid.org/0009-0005-2448-0605
Kenny W L LamDepartment of Chemical Engineering, The University of Melbourne, Parkville, VIC, 3010, Australia.ORCID http://orcid.org/0009-0009-8212-5889
Siyi XueDepartment of Chemical Engineering, The University of Melbourne, Parkville, VIC, 3010, Australia.ORCID http://orcid.org/0009-0008-7276-6589
Jørgen HansenRiver Stone Biotech ApS, Fruebjergvej 3, København Ø, 2100, Denmark.ORCID http://orcid.org/0000-0003-4806-4014
Tim A BowserRiver Stone Biotech Australia Pty Ltd, 24 Leighton Bay Drive, Metung, VIC, 3904, Australia.ORCID http://orcid.org/0000-0002-2126-8538
Sandra E KentishDepartment of Chemical Engineering, The University of Melbourne, Parkville, VIC, 3010, Australia.ORCID http://orcid.org/0000-0002-4250-7489
Sally L GrasDepartment of Chemical Engineering, The University of Melbourne, Parkville, VIC, 3010, Australia. sgras@unimelb.edu.au.ORCID https://orcid.org/0000-0002-4660-1245

Funding

Australian Research Council LP200301120
6 · The paper itself

Abstract

Alkaloid N-demethylation is a critical step in the production of many semi-synthetic alkaloid therapeutics and has traditionally relied on synthetic chemical routes. Microbial whole-cell bioproduction offers a promising alternate route for generating these valuable pharmaceuticals. This work demonstrated a greener N-demethylation platform applicable to morphinan and tropine alkaloid classes, employing an engineered yeast expressing a cytochrome P450 enzyme with N-demethylase activity, a cytochrome P450 oxidoreductase and purine permeases as transporters. This platform enabled the N-demethylation of the morphinan alkaloids, oripavine and thebaine with high activity, and the tropane alkaloids, atropine and scopolamine with moderate activity. The study systematically evaluated the contributions of substrate uptake and enzymatic conversion within the whole-cell system. Heterologous transporters enabled mass transfer across the cell membrane, with no significant difference detected for the four substrates, while in vitro enzyme catalysis differed between substrates and correlated with yield. Computational molecular docking, combined with deep learning-based protein structure prediction, found all four substrates had high affinity for the enzyme. This approach was also used to identify potential target substrates for future biotransformation. Process performance could be further improved with the use of larger scale, well controlled bioreactors.

Indexed as

Benzylisoquinoline alkaloidsBiotransformationCross-membrane transporterEnzyme affinityMolecular dockingSaccharomyces cerevisiaeSynthetic biologyTropane alkaloids

Identifiers

PMID42477771
PMCPMC13670527

What OpenQuestion holds

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Registered trials

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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.