Evidence map›Paper›PMID 25960001›Full record

ArticleScientific reports2015

Structure and mechanism of an antibiotics-synthesizing 3-hydroxykynurenine C-methyltransferase.

Sheng-Chia Chen, Chi-Hung Huang, Shu-Jung Lai, Jai-Shin Liu, Pin-Kuei Fu, Shih-Ting Tseng, Chia Shin Yang, Mei-Chin Lai, Tzu-Ping Ko, Yeh Chen

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

4 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Context-Dependent Chemoselectivity of Aromatic C-Methyltransferases.Chembiochem : a European journal of chemical biology · 2026
    Article
  3. Article
  4. 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

10 authors at 7 institutions in 1 country.

Sheng-Chia Chen1] Department of Biotechnology, Hungkuang University, Taichung, Taiwan [2] Taiwan Advance Biopharm (TABP), Inc., Xizhi City, New Taipei City, Taiwan.
Chi-Hung Huang1] Department of Biotechnology, Hungkuang University, Taichung, Taiwan [2] Taiwan Advance Biopharm (TABP), Inc., Xizhi City, New Taipei City, Taiwan.
Shu-Jung LaiDepartment of Life Sciences, National Chung Hsing University, Taichung, Taiwan.
Jai-Shin LiuInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, Taiwan.
Pin-Kuei Fu1] Division of Critical Care &Respiratory Therapy, Department of Internal Medicine, Taichung Veterans General Hospital, Taichung, Taiwan [2] Department of Applied Chemistry, National Chi Nan University, Nantou County, Taiwan.
Shih-Ting Tseng1] Department of Food and Nutrition, Providence University, Taichung, Taiwan [2] Department of Endocrinology and Metabolism, Kuang Tien General Hospital, Taiwan.
Chia Shin Yang1] Department of Biotechnology, Hungkuang University, Taichung, Taiwan [2] Taiwan Advance Biopharm (TABP), Inc., Xizhi City, New Taipei City, Taiwan.
Mei-Chin LaiDepartment of Life Sciences, National Chung Hsing University, Taichung, Taiwan.
Tzu-Ping KoInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
Yeh ChenDepartment of Biotechnology, Hungkuang University, Taichung, Taiwan.
Hungkuang University · TWNational Chung Hsing University · TWInstitute of Biological Chemistry, Academia Sinica · TWNational Tsing Hua University · TWProvidence University · TWScinoPharm Taiwan (Taiwan) · TWTaichung Veterans General Hospital · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Streptosporangium sibiricum SibL catalyzes the methyl transfer from S-adenosylmethionine (SAM) to 3-hydroxykynurenine (3-HK) to produce S-adenosylhomocysteine (SAH) and 3-hydroxy-4-methyl-kynurenine for sibiromycin biosynthesis. Here, we present the crystal structures of apo-form Ss-SibL, Ss-SibL/SAH binary complex and Ss-SibL/SAH/3-HK ternary complex. Ss-SibL is a homodimer. Each subunit comprises a helical N-terminal domain and a Rossmann-fold C-terminal domain. SAM (or SAH) binding alone results in domain movements, suggesting a two-step catalytic cycle. Analyses of the enzyme-ligand interactions and further mutant studies support a mechanism in which Tyr134 serves as the principal base in the transferase reaction of methyl group from SAM to 3-HK.

Indexed as

ActinobacteriaAnti-Bacterial AgentsBacterial ProteinsBinding SitesCrystallography, X-RayKynurenineLigandsMethyltransferasesModels, MolecularMutant ProteinsProtein MultimerizationProtein Structure, Secondary3-hydroxykynurenineAnti-Bacterial AgentsBacterial ProteinsKynurenineLigandsMethyltransferasesMutant Proteins

Identifiers

PMID25960001
PMCPMC4426599
OpenAlexW2267514402

What OpenQuestion holds

Textmetadata
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.