Evidence map›Paper›PMID 39915427›Full record

ReviewJournal of natural medicines2025

Biosynthesis of unique natural product scaffolds by Fe(II)/αKG-dependent oxygenases.

Takayoshi Awakawa

Abstract readReview
In one paragraph

Review in Journal of natural medicines, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Total Synthesis of the Nominal Structure of (+)-Talaromyolide D.Journal of the American Chemical Society · 2025
    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

1 author.

Takayoshi AwakawaRIKEN Center for Sustainable Resource Science, Wako, Saitama, 351-0198, Japan. takayoshi.awakawa@riken.jp.ORCID http://orcid.org/0000-0003-2575-3175

Funding

Fusion Oriented REsearch for disruptive Science and Technology JPMJFR2301Japan Society for the Promotion of Science London 21H02636Japan Society for the Promotion of Science London 22H05123
6 · The paper itself

Abstract

Fe(II)/αKG-dependent oxygenases are multifunctional oxidases responsible for the formation of unique natural product skeletons. Studies of these enzymes are important because the knowledge of their catalytic functions, enzyme structures, and reaction mechanisms can be used to create non-natural enzymes through mutation and synthesize non-natural compounds. In this review, I will introduce the research we have conducted on two fungal Fe(II)/αKG-dependent oxygenases, TlxI-J and TqaL. TlxI-J is the first Fe(II)/αKG-dependent oxygenase type enzyme heterodimer that catalyzes consecutive oxidation reactions, hydroxylation followed by retro-aldol or ketal formation, to form the complex skeletons of meroterpenoids. TqaL is the first naturally occurring aziridine synthase, and I will discuss the mechanism of its unique C-N bond formation in nonproteinogenic amino acid biosynthesis. This review will advance research on the discovery of new enzymes and the analysis of their functions by reviewing the structures and functions of these extraordinary Fe(II)/αKG-dependent oxygenases, and promote their use in the synthesis of new natural medicines.

Indexed as

Biological ProductsKetoglutaric AcidsOxygenasesBiological ProductsKetoglutaric AcidsOxygenasesAziridineBiosynthesisFe(II)/αKG-dependent oxygenaseMeroterpenoidNonproteinogenic amino acidOxidation

Identifiers

PMID39915427
PMCPMC11880133

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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.