Evidence map›Paper›PMID 39792592›Full record

ArticleFEBS letters2025

Characterization of fungal carbonyl sulfide hydrolase belonging to clade D β-carbonic anhydrase.

Ryuka Iizuka, Takahiro Ogawa, Rikako Tsukida, Keiichi Noguchi, David Hibbett, Yoko Katayama, Makoto Yoshida

Abstract read
In one paragraph

Article in FEBS letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

7 authors.

Ryuka IizukaDepartment of Symbiotic Science of Environment and Natural Resources, United Graduate School of Agricultural Science, Tokyo University of Agriculture and Technology, Fuchu, Japan.ORCID https://orcid.org/0009-0000-5281-5453
Takahiro OgawaGraduate School of Engineering, Tokyo University of Agriculture and Technology, Koganei, Japan.
Rikako TsukidaGraduate School of Agriculture, Tokyo University of Agriculture and Technology, Fuchu, Japan.ORCID https://orcid.org/0009-0006-9817-1407
Keiichi NoguchiInstrumentation Analysis Center, Tokyo University of Agriculture and Technology, Koganei, Japan.ORCID https://orcid.org/0000-0003-0833-0808
David HibbettDepartment of Biology, Clark University, Worcester, MA, USA.ORCID https://orcid.org/0000-0002-9145-3165
Yoko KatayamaGraduate School of Agriculture, Tokyo University of Agriculture and Technology, Fuchu, Japan.ORCID https://orcid.org/0000-0002-4365-6320
Makoto YoshidaDepartment of Symbiotic Science of Environment and Natural Resources, United Graduate School of Agricultural Science, Tokyo University of Agriculture and Technology, Fuchu, Japan.ORCID https://orcid.org/0000-0001-6318-8109

Funding

Japan Science and Technology Agency JPMJPF2104Japan Society for the Promotion of Science 20K12202Japan Society for the Promotion of Science 22J22163Japan Society for the Promotion of Science 23K23668
6 · The paper itself

Abstract

Carbonyl sulfide hydrolase (COSase) is a unique enzyme that exhibits high activity towards carbonyl sulfide (COS) but low carbonic anhydrase (CA) activity, despite belonging to the CA family. COSase was initially identified in a sulfur-oxidizing bacterium and later discovered in the ascomycete Trichoderma harzianum strain THIF08. The COSase from T. harzianum has been recognized as a key enzyme in the assimilation of gaseous COS, and homologous genes are widely present not only in Ascomycota but also in Basidiomycota. Here, we characterized the COSases from the basidiomycete Gloeophyllum trabeum NBRC 6430 and T. harzianum to obtain detailed characteristics of fungal COSase. This study contributes to a better understanding of COS metabolism in fungi.

Indexed as

Carbonic AnhydrasesFungal ProteinsSulfur OxidesAmino Acid SequencePhylogenySubstrate SpecificityCarbonic Anhydrasescarbonyl sulfideFungal ProteinsSulfur Oxidescarbonic anhydrasecarbonyl sulfidecarbonyl sulfide hydrolasefungisulfur metabolism

Identifiers

PMID39792592
PMCPMC12035519

What OpenQuestion holds

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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.