Evidence map›Paper›PMID 36697788›Full record

ArticleCommunications chemistry2022

β-Hydroxylation of α-amino-β-hydroxylbutanoyl-glycyluridine catalyzed by a nonheme hydroxylase ensures the maturation of caprazamycin.

Saeid Malek Zadeh, Mei-Hua Chen, Zhe-Chong Wang, Elahe K Astani, I-Wen Lo, Kuan-Hung Lin, Ning-Shian Hsu, Kamal Adhikari, Syue-Yi Lyu, Hsin-Ying Tsai and 5 more

Open access · goldAbstract read
In one paragraph

Article in Communications chemistry, 2022. 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
0.6field-weighted citation impact, top 36% 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, 7 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  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

15 authors at 6 institutions in 3 countries.

Saeid Malek ZadehGenomics Research Center, Academia Sinica, Taipei, Taiwan.
Mei-Hua ChenGenomics Research Center, Academia Sinica, Taipei, Taiwan.
Zhe-Chong WangGenomics Research Center, Academia Sinica, Taipei, Taiwan.
Elahe K AstaniDepartment of Chemistry, Faculty of Science, Tarbiat Modares University, Tehran, Iran.
I-Wen LoGenomics Research Center, Academia Sinica, Taipei, Taiwan.
Kuan-Hung LinGenomics Research Center, Academia Sinica, Taipei, Taiwan.
Ning-Shian HsuGenomics Research Center, Academia Sinica, Taipei, Taiwan.
Kamal AdhikariGenomics Research Center, Academia Sinica, Taipei, Taiwan.
Syue-Yi LyuGenomics Research Center, Academia Sinica, Taipei, Taiwan.
Hsin-Ying TsaiGenomics Research Center, Academia Sinica, Taipei, Taiwan.
Yuma TerasawaGraduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Miyuki YabeGraduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Kazuki YamamotoGraduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.ORCID http://orcid.org/0000-0001-7617-1840
Satoshi IchikawaGraduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.ORCID http://orcid.org/0000-0001-5345-5007
Tsung-Lin LiGenomics Research Center, Academia Sinica, Taipei, Taiwan. tlli@gate.sinica.edu.tw.ORCID http://orcid.org/0000-0002-9739-9761
Genomics Research Center, Academia Sinica · TWHokkaido University · JPTarbiat Modares University · IRNational Chung Hsing University · TWNational Taiwan University · TWNational Tsing Hua University · TW

Funding

Academia Sinica AS-IA-109-L06Ministry of Science and Technology, Taiwan (Ministry of Science and Technology of Taiwan) 108-2113-M-001-021-MY3
6 · The paper itself

Abstract

Caprazamycin is a nucleoside antibiotic that inhibits phospho-N-acetylmuramyl-pentapeptide translocase (MraY). The biosynthesis of nucleoside antibiotics has been studied but is still far from completion. The present study characterized enzymes Cpz10, Cpz15, Cpz27, Mur17, Mur23 out of caprazamycin/muraymycin biosynthetic gene cluster, particularly the nonheme αKG-dependent enzyme Cpz10. Cpz15 is a β-hydroxylase converting uridine mono-phosphate to uridine 5' aldehyde, then incorporating with threonine by Mur17 (Cpz14) to form 5'-C-glycyluridine. Cpz10 hydroxylates synthetic 11 to 12 in vitro. Major product 13 derived from mutant Δcpz10 is phosphorylated by Cpz27. β-Hydroxylation of 11 by Cpz10 permits the maturation of caprazamycin, but decarboxylation of 11 by Mur23 oriented to muraymycin formation. Cpz10 recruits two iron atoms to activate dioxygen with regio-/stereo-specificity and commit electron/charge transfer, respectively. The chemo-physical interrogations should greatly advance our understanding of caprazamycin biosynthesis, which is conducive to pathway/protein engineering for developing more effective nucleoside antibiotics.

Identifiers

PMID36697788
PMCPMC9814697
OpenAlexW4288084400

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.