Evidence mapPaperPMID 40970329Full record

ArticleActa crystallographica. Section F, Structural biology communications2025

Crystal structure of D-aspartate oxidase from Cryptococcus humicola UJ1.

Masaru Goto, Risako Nonaka, Taichi Mizobuchi, Daiki Imanishi, Shouji Takahashi

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 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

5 authors.

Masaru GotoFaculty of Science, Toho University, 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan.ORCID 0000-0002-9317-0521
Risako NonakaFaculty of Science, Toho University, 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan.
Taichi MizobuchiFaculty of Science, Toho University, 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan.
Daiki ImanishiDepartment of Material Science and Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka, Niigata 940-2188, Japan.ORCID 0009-0008-2009-5576
Shouji TakahashiDepartment of Material Science and Bioengineering, Nagaoka University of Technology, 1603-1 Kamitomioka, Nagaoka, Niigata 940-2188, Japan.ORCID 0000-0002-0279-9173

Funding

Japan Society for the Promotion of Science 22770113
6 · The paper itself

Abstract

The enzyme D-aspartate oxidase (DDO) oxidizes acidic D-amino acids using the coenzyme flavin adenine dinucleotide to generate the corresponding α-keto acids and ammonia. DDO differs from D-amino-acid oxidase (DAAO), which acts on neutral and basic D-amino acids. Although the enzymatic properties of DDO have been characterized in several species, the structure of DDO had remained unclear. The structure of DDO derived from Cryptococcus humicola strain UJ1 (chDDO) was determined by X-ray crystallography at 1.70 Å resolution. While the three-dimensional structures of DAAOs are known to be homodimers, chDDO forms a homotetramer. This difference was found to be caused by the deletion of one loop and the insertion of two loops.

Indexed as

CryptococcusD-Aspartate OxidaseFungal ProteinsAmino Acid SequenceCloning, MolecularCrystallography, X-RayEscherichia coliGene ExpressionModels, MolecularProtein ConformationProtein MultimerizationRecombinant ProteinsD-Aspartate OxidaseFungal ProteinsRecombinant Proteinscrystal structured-aspartate oxidasesFAD-dependent enzymes

Identifiers

PMID40970329
PMCPMC12485492

What Socratic 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 Socratic graph.