Evidence map›Paper›PMID 30153835›Full record

ArticleMicrobial cell factories2018

Discovery and characterization of the tubercidin biosynthetic pathway from Streptomyces tubercidicus NBRC 13090.

Yan Liu, Rong Gong, Xiaoqin Liu, Peichao Zhang, Qi Zhang, You-Sheng Cai, Zixin Deng, Margit Winkler, Jianguo Wu, Wenqing Chen

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 22% of its field
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

13 citing papers in PubMed, 29 citations in OpenAlex.

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  10. Structure and Mechanism ofACS catalysis · 2021
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  12. Screening and Isolation of a Novel Polyene-ProducingFrontiers in bioengineering and biotechnology · 2021
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  13. Review
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

10 authors at 2 institutions in 2 countries.

Yan LiuState Key Laboratory of Virology, and College of Life Sciences, Wuhan University, Wuhan, 430072, China.
Rong GongKey Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan, 430071, China.
Xiaoqin LiuKey Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan, 430071, China.
Peichao ZhangKey Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan, 430071, China.
Qi ZhangState Key Laboratory of Virology, and College of Life Sciences, Wuhan University, Wuhan, 430072, China.
You-Sheng CaiKey Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan, 430071, China.
Zixin DengKey Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan, 430071, China.
Margit WinklerAustrian Centre of Industrial Biotechnology, Petersgasse 14, 8010, Graz, Austria.
Jianguo WuState Key Laboratory of Virology, and College of Life Sciences, Wuhan University, Wuhan, 430072, China. jwu@whu.edu.cn.
Wenqing ChenKey Laboratory of Combinatorial Biosynthesis and Drug Discovery, Ministry of Education, and School of Pharmaceutical Sciences, Wuhan University, Wuhan, 430071, China. wqchen@whu.edu.cn.ORCID http://orcid.org/0000-0003-2557-8960
Wuhan University · CNAustrian Centre of Industrial Biotechnology (Austria) · AT

Funding

National Natural Science Foundation of China 31770041
6 · The paper itself

Abstract

backgroundTubercidin (TBN), an adenosine analog with potent antimycobacteria and antitumor bioactivities, highlights an intriguing structure, in which a 7-deazapurine core is linked to the ribose moiety by an N-glycosidic bond. However, the molecular logic underlying the biosynthesis of this antibiotic has remained poorly understood.

resultsHere, we report the discovery and characterization of the TBN biosynthetic pathway from Streptomyces tubercidicus NBRC 13090 via reconstitution of its production in a heterologous host. We demonstrated that TubE specifically utilizes phosphoribosylpyrophosphate and 7-carboxy-7-deazaguanine for the precise construction of the deazapurine nucleoside scaffold. Moreover, we provided biochemical evidence that TubD functions as an NADPH-dependent reductase, catalyzing irreversible reductive deamination. Finally, we verified that TubG acts as a Nudix hydrolase, preferring Co

conclusionsThese findings lay a foundation for the rational generation of TBN analogs through synthetic biology strategy, and also open the way for the target-directed search of TBN-related antibiotics.

Indexed as

StreptomycesSynthetic BiologyTubercidinTubercidin7-deazapurineBiosynthesisNADPH-dependent reductaseNudix hydrolasePhosphoribosylpyrophosphateSynthetic biologyTubercidin

Identifiers

PMID30153835
PMCPMC6112128
OpenAlexW2888900988

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.