Activity-stability trade-off observed in variants at position 315 of the GH10 xylanase XynR.

Tomoka Nakamura, Teisuke Takita, Kohei Kuwata, Kimihiko Mizutani, Bunzo Mikami, Satoshi Nakamura, Kiyoshi Yasukawa

Abstract read

In one paragraph

Article in Scientific reports, 2024. 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

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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

2 citing papers in PubMed.

Endo-β-1,4-Xylanase GH10 fromInternational journal of molecular sciences · 2026
Article
Recent progress in the microbial production of Xylanase.World journal of microbiology & biotechnology · 2025
Review

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.

Tomoka NakamuraDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, 606-8502, Japan.

Teisuke TakitaDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, 606-8502, Japan.

Kohei KuwataDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, 606-8502, Japan.

Kimihiko MizutaniDivision of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Uji, Kyoto, 611-0011, Japan.

Bunzo MikamiResearch Institute for Sustainable Humanosphere, Kyoto University, Uji, Kyoto, 611-0011, Japan.

Satoshi NakamuraDepartment of Life Science and Technology, Tokyo Institute of Technology, Midori-ku, Yokohama, 226-8501, Japan.

Kiyoshi YasukawaDivision of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto, 606-8502, Japan. yasukawa.kiyoshi.7v@kyoto-u.ac.jp.

Funding

Japan Society for the Promotion of Science 22H03332Salt Science Research Foundation Research Grant

6 · The paper itself

Abstract

XynR is a thermostable alkaline GH10 xylanase, for which we have previously examined the effects of saturation mutagenesis at position 315 on enzyme alkaliphily, and found that at pH 10, the activities of variants could be ordered as follows: T315Q > T315S = T315N > T315H = wild-type XynR (WT) > 15 other variants. In this study, we sought to elucidate the mechanisms underlying the variable activity of these different variants. Crystallographic analysis revealed that the Ca

Indexed as

Endo-1,4-beta XylanasesCalcium ChlorideEnzyme StabilityHydrogen-Ion ConcentrationMutagenesisMutationTemperatureCalcium ChlorideEndo-1,4-beta Xylanases

Identifiers

PMID38565938

DOI10.1038/s41598-024-57819-z

PMCPMC10987496

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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.