Keyword search (4,163 papers available)

"Saccharomyces cerevisiae" Keyword-tagged Publications:

Title Authors PubMed ID
1 Benzylisoquinoline Alkaloid Production in Yeast via Norlaudanosoline Improves Titer, Selectivity, and Yield Narcross L; Pyne ME; Kevvai K; Siu KH; Dueber JE; Martin VJJ; 41779670
BIOLOGY
2 PARPAL: PARalog Protein Redistribution using Abundance and Localization in Yeast Database Greco BM; Zapata G; Dandage R; Papkov M; Pereira V; Lefebvre F; Bourque G; Parts L; Kuzmin E; 40580499
BIOLOGY
3 Thermotolerance in S. cerevisiae as a model to study extracellular vesicle biology Logan CJ; Staton CC; Oliver JT; Bouffard J; Kazmirchuk TDD; Magi M; Brett CL; 38711329
BIOLOGY
4 CRAPS: Chromosomal-Repair-Assisted Pathway Shuffling in Yeast Dykstra CB; Pyne ME; Martin VJJ; 37584634
BIOLOGY
5 Engineering Yeast for De Novo Synthesis of the Insect Repellent Nepetalactone Davies ME; Tsyplenkov D; Martin VJJ; 34748704
BIOLOGY
6 An Engineered Aro1 Protein Degradation Approach for Increased cis,cis-Muconic Acid Biosynthesis in Saccharomyces cerevisiae. Pyne ME, Narcross L, Melgar M, Kevvai K, Mookerjee S, Leite GB, Martin VJJ 29934332
BIOLOGY
7 A Highly Characterized Synthetic Landing Pad System for Precise Multicopy Gene Integration in Yeast. Bourgeois L, Pyne ME, Martin VJJ 30372609
BIOLOGY
8 Engineering of a Nepetalactol-Producing Platform Strain of Saccharomyces cerevisiae for the Production of Plant Seco-Iridoids. Campbell A, Bauchart P, Gold ND, Zhu Y, De Luca V, Martin VJ 26981892
CSFG
9 Seamless site-directed mutagenesis of the Saccharomyces cerevisiae genome using CRISPR-Cas9. Biot-Pelletier D, Martin VJ 27134651
BIOLOGY
10 Reconstituting Plant Secondary Metabolism in Saccharomyces cerevisiae for Production of High-Value Benzylisoquinoline Alkaloids. Pyne ME, Narcross L, Fossati E, Bourgeois L, Burton E, Gold ND, Martin VJ 27417930
CSFG
11 Mining Enzyme Diversity of Transcriptome Libraries through DNA Synthesis for Benzylisoquinoline Alkaloid Pathway Optimization in Yeast. Narcross L, Bourgeois L, Fossati E, Burton E, Martin VJ 27442619
BIOLOGY

 

Title:Benzylisoquinoline Alkaloid Production in Yeast via Norlaudanosoline Improves Titer, Selectivity, and Yield
Authors:Narcross LPyne MEKevvai KSiu KHDueber JEMartin VJJ
Link:https://pubmed.ncbi.nlm.nih.gov/41779670/
DOI:10.1021/acssynbio.5c00897
Publication:ACS synthetic biology
Keywords:Saccharomyces cerevisiaebenzylisoquinoline alkaloidsmetabolic engineeringreticulinesynthetic biologyyeast
PMID:41779670 Category: Date Added:2026-03-04
Dept Affiliation: BIOLOGY
1 Department of Biology, Concordia University, Montréal, Québec H4B 1R6, Canada.
2 Centre for Applied Synthetic Biology, Concordia University, Montréal, Québec H4B 1R6, Canada.
3 Department of Bioengineering, University of California, Berkeley, Berkeley, California 94720, United States.
4 Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, United States.

Description:

The benzylisoquinoline alkaloid (BIA) family of tetrahydroisoquinolines (THIQs) comprises >2,500 members, including the pharmaceuticals morphine, codeine, and papaverine, as well as the antibiotics sanguinarine and chelerythrine. Agricultural cultivation can supply the demand for the BIAs that accumulate in plants, but broader access to the BIA family would facilitate additional research and commercialization. Microbial synthesis presents an attractive option due to cheap feedstock, genetic tractability, and ease of scale-up. Previously, we reported titers of the branch-point BIA (S)-reticuline of 4.6 g/L in yeast, which was achieved through leveraging the Ehrlich pathway 2-oxoacid decarboxylase Aro10 to generate the intermediate 4-hydroxyphenylacetaldehyde (4-HPAA). Here, we establish a superior route to (S)-reticuline by switching the pathway intermediate from 4-HPAA to 3,4-dihydroxyphenylacetaldehyde (3,4-dHPAA) using monoamine oxidase A (MAO). The resulting (S)-norlaudanosoline route to (S)-reticuline synthesis is more selective, resolving prior issues with off-pathway THIQs synthesized due to cascading enzyme promiscuity, and more efficient, enabling titers of 4.8 g/L (S)-reticuline while improving yields by over 40%, from 17 to 24 mg/g sucrose in fed-batch fermentations. Finally, we extend de novo (S)-reticuline synthesis to dihydrosanguinarine, achieving 635 mg/L dihydrosanguinarine and sanguinarine in fed-batch fermentation, the highest reported titer of these BIAs by a factor of 40.





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