Evidence map›Paper›PMID 33824341›Full record

ArticleNature communications2021

Biochemical and structural characterization of the BioZ enzyme engaged in bacterial biotin synthesis pathway.

Sitao Zhang, Yongchang Xu, Hongxin Guan, Tao Cui, Yuling Liao, Wenhui Wei, Jun Li, Bachar H Hassan, Huimin Zhang, Xu Jia and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Exploring the Link Between Biotin Metabolism andPathogens (Basel, Switzerland) · 2026
    Article
  3. Article
  4. Article
  5. A ferritin-like diiron oxygenase BioE initiates bacterial biotin synthesis, a promising antivirulence target.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Switching the strict substrate specificities of the β-ketoacyl-acyl carrier protein synthases, FabH and BioZ.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Cocrystal structure reveals the mechanism of FSP1 inhibition by FSEN1.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Biotin pathway in novelFrontiers in microbiology · 2022
    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

12 authors.

Sitao Zhang *Laboratory of Innate Immune Biology of Fujian Province, Provincial University Key Laboratory of Cellular Stress Response and Metabolic Regulation, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal University, Fuzhou, Fujian, China.
Yongchang Xu *Department of Pathogen Biology & Microbiology and General Intensive Care Unit of Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China.
Hongxin Guan *Laboratory of Innate Immune Biology of Fujian Province, Provincial University Key Laboratory of Cellular Stress Response and Metabolic Regulation, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal University, Fuzhou, Fujian, China.
Tao Cui *School of Life Sciences, Northwestern Polytechnical University, Xi'an, Shaanxi, China.
Yuling Liao *Guangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, Guangdong, China.
Wenhui Wei *Department of Pathogen Biology & Microbiology and General Intensive Care Unit of Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China.
Jun LiDepartment of Pathogen Biology & Microbiology and General Intensive Care Unit of Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China.
Bachar H HassanStony Brook University, Stony Brook, NY, USA.
Huimin ZhangDepartment of Pathogen Biology & Microbiology and General Intensive Care Unit of Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China.
Xu JiaNon-coding RNA and Drug Discovery Key Laboratory of Sichuan Province, Chengdu Medical College, Chengdu, Sichuan, China.
Songying OuyangLaboratory of Innate Immune Biology of Fujian Province, Provincial University Key Laboratory of Cellular Stress Response and Metabolic Regulation, Biomedical Research Center of South China, Key Laboratory of OptoElectronic Science and Technology for Medicine of the Ministry of Education, College of Life Sciences, Fujian Normal University, Fuzhou, Fujian, China. ouyangsy@fjnu.edu.cn.ORCID 0000-0002-1120-1524
Youjun FengDepartment of Pathogen Biology & Microbiology and General Intensive Care Unit of Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang, China. fengyj@zju.edu.cn.ORCID 0000-0001-8083-0175

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biotin is an essential micro-nutrient across the three domains of life. The paradigm earlier step of biotin synthesis denotes "BioC-BioH" pathway in Escherichia coli. Here we report that BioZ bypasses the canonical route to begin biotin synthesis. In addition to its origin of Rhizobiales, protein phylogeny infers that BioZ is domesticated to gain an atypical role of β-ketoacyl-ACP synthase III. Genetic and biochemical characterization demonstrates that BioZ catalyzes the condensation of glutaryl-CoA (or ACP) with malonyl-ACP to give 5'-keto-pimeloyl ACP. This intermediate proceeds via type II fatty acid synthesis (FAS II) pathway, to initiate the formation of pimeloyl-ACP, a precursor of biotin synthesis. To further explore molecular basis of BioZ activity, we determine the crystal structure of Agrobacterium tumefaciens BioZ at 1.99 Å, of which the catalytic triad and the substrate-loading tunnel are functionally defined. In particular, we localize that three residues (S84, R147, and S287) at the distant bottom of the tunnel might neutralize the charge of free C-carboxyl group of the primer glutaryl-CoA. Taken together, this study provides molecular insights into the BioZ biotin synthesis pathway.

Indexed as

Biosynthetic PathwaysAcyl Carrier ProteinAcyl Coenzyme AAgrobacteriumAmino Acid SequenceBiocatalysisBiotinCrystallography, X-RayEscherichia coliEscherichia coli ProteinsMolecular Docking SimulationPhylogenyProtein MultimerizationStructural Homology, ProteinSubstrate SpecificityAcyl Carrier ProteinAcyl Coenzyme ABiotinEscherichia coli Proteinsglutaryl-coenzyme A

Identifiers

PMID33824341
PMCPMC8024396

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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.