Evidence map›Paper›PMID 42669729›Full record

ArticleNature communications2026

De novo L-(+)-tartaric acid biosynthesis in multi-modular engineered yeasts.

Xuan Zhou, Jiaheng Hou, Zikai Wang, Zhendong Li, Yang Li, Xitong Li, Xianhao Xu, Yanfeng Liu, Jianghua Li, Guocheng Du and 5 more

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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

15 authors.

Xuan ZhouState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, China.ORCID 0009-0001-4167-4496
Jiaheng HouDepartment of Biomedical Engineering, College of Future Technology, and Center for Quantitative Biology, Peking University, Beijing, China.
Zikai WangState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, China.
Zhendong LiInstitute of Future Food Technology, JITRl, Yixing, China.
Yang LiState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, China.
Xitong LiKey Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, Jiangnan University, Wuxi, China.
Xianhao XuState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, China.
Yanfeng LiuState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, China.ORCID 0000-0002-0562-9647
Jianghua LiState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, China.
Guocheng DuState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, China.ORCID 0000-0002-3269-3476
Dacheng MaKey Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, Jiangnan University, Wuxi, China.
Jian TangHEC Montreal and Mila-Quebec AI Institute, Quebec, QC, Canada.
Jian ChenState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, China.ORCID 0000-0003-3217-3224
Xueqin LvState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, China. lvxueqin@jiangnan.edu.cn.ORCID 0000-0003-3432-2166
Long LiuState Key Laboratory of Food Science and Resources, Jiangnan University, Wuxi, China. longliu@jiangnan.edu.cn.ORCID 0000-0002-9679-9130

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

L-(+)-tartaric acid (L-TA) is a high-value chiral organic acid essential for food and pharmaceuticals. Despite its industrial importance, sustainable green production is constrained by the lack of a fully defined biosynthetic pathway. Here, we report the de novo biosynthesis of L-TA in Saccharomyces cerevisiae through reaction-guided enzyme mining, experimental validation, and Enzyme Commission-specific Catalytic Hybrid Optimizer (ECHO)-assisted enzyme prioritization. We first elucidate the elusive two-step conversion from precursor 5-keto-D-gluconic acid (5-KGA) to L-TA, catalyzed by transketolase (TK) and succinate semialdehyde dehydrogenase (SSDH). To optimize this critical step, we develop the ECHO. This multimodal framework integrates sequence, substrate, and pocket-aware structural information to identify high-performance TK-SSDH pairs. By integrating this pathway with de novo precursor synthesis, cofactor engineering, and semi-rational protein engineering, a final L-TA titer of 6.59 mg L

Indexed as

Metabolic EngineeringSaccharomyces cerevisiaeTartratesProtein EngineeringSaccharomyces cerevisiae ProteinsSuccinate-Semialdehyde DehydrogenaseSaccharomyces cerevisiae ProteinsSuccinate-Semialdehyde Dehydrogenasetartaric acidTartrates

Identifiers

PMID42669729
PMCPMC13527115

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.