Structural insight into the unique substrate specificity of glutamate dehydrogenase from Saccharolobus solfataricus.

Itsuki Okabe, Masashi Hirano, Taketo Ohmori, Minako Segawa, Kazunari Yoneda, Toshihisa Ohshima, Haruhiko Sakuraba

Abstract read

In one paragraph

Article in Extremophiles : life under extreme conditions, 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.

Itsuki OkabeDepartment of Applied Biological Science, Faculty of Agriculture, Kagawa University, 2393 Ikenobe, Miki-cho, Kita-gun, Kagawa, 761-0795, Japan.

Masashi HiranoDepartment of Food and Life Sciences, School of Agriculture, Tokai University, 871-12 Sugido, Mashiki-machi, Kamimashiki-gun, Kumamoto, 861-2205, Japan.

Taketo OhmoriDepartment of Biomedical Engineering, Faculty of Engineering, Osaka Institute of Technology, 5-16-1 Ohmiya, Asahi-ku, Osaka, 535-8585, Japan.

Minako SegawaDepartment of Biomedical Engineering, Faculty of Engineering, Osaka Institute of Technology, 5-16-1 Ohmiya, Asahi-ku, Osaka, 535-8585, Japan.

Kazunari YonedaDepartment of Food and Life Sciences, School of Agriculture, Tokai University, 871-12 Sugido, Mashiki-machi, Kamimashiki-gun, Kumamoto, 861-2205, Japan.

Toshihisa OhshimaDepartment of Biomedical Engineering, Faculty of Engineering, Osaka Institute of Technology, 5-16-1 Ohmiya, Asahi-ku, Osaka, 535-8585, Japan.

Haruhiko SakurabaDepartment of Applied Biological Science, Faculty of Agriculture, Kagawa University, 2393 Ikenobe, Miki-cho, Kita-gun, Kagawa, 761-0795, Japan. sakuraba.haruhiko@kagawa-u.ac.jp.

Funding

Japan Society for the Promotion of Science 20K05816Japan Society for the Promotion of Science 23K05658

6 · The paper itself

Abstract

The gene (SSO1457) encoding a L-glutamate dehydrogenase (GDH) homolog from the thermoacidophilic archaeon Saccharolobus solfataricus P2 was overexpressed in Escherichia coli. At a substrate concentration of 50 mM, the enzyme (SSO1457) produced exhibited much higher specific activity toward L-norvaline than L-glutamate at temperatures between 55 and 75°C, whereas the enzyme showed higher activity for L-glutamate than L-norvaline at 85°C. The crystal structures of both NAD

Indexed as

Archaeal ProteinsGlutamate DehydrogenaseSulfolobus solfataricusGlutamic AcidKetoglutaric AcidsSubstrate SpecificityValineArchaeal ProteinsGlutamate DehydrogenaseGlutamic AcidKetoglutaric AcidsnorvalineValineCrystal structureGlutamate dehydrogenaseHyperthermophilic enzymeMolecular dynamics simulationSubstrate specificity

Identifiers

PMID40705132

DOI10.1007/s00792-025-01395-1

What OpenQuestion holds

Textmetadata

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.