Evidence map›Paper›PMID 42010116›Full record

ArticleApplied microbiology and biotechnology2026

Characterization of a membrane-bound PQQ-dependent D-lactate dehydrogenase in Gluconobacter japonicus.

Naoya Kataoka, Shu Takeuchi, Shintaro Maeno, Minenosuke Matsutani, Kazunobu Matsushita, Toshiharu Yakushi

Abstract read
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In one paragraph

Article in Applied microbiology and biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

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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

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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

6 authors.

Naoya KataokaOrganization for Research Initiatives, Yamaguchi University, Yamaguchi, Japan. nkataoka@yamaguchi-u.ac.jp.
Shu TakeuchiDivision of Agricultural Sciences, Graduate School of Sciences and Technology for Innovation, Yamaguchi University, Yamaguchi, Japan.
Shintaro MaenoOrganization for Research Initiatives, Yamaguchi University, Yamaguchi, Japan.
Minenosuke MatsutaniDepartment of Food, Aroma and Cosmetic Chemistry, Tokyo University of Agriculture, Hokkaido, Japan.
Kazunobu MatsushitaResearch Center for Thermotolerant Microbial Resources, Yamaguchi University, Yamaguchi, Japan.
Toshiharu YakushiOrganization for Research Initiatives, Yamaguchi University, Yamaguchi, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Membrane-bound pyrroloquinoline quinone (PQQ)-dependent quinoproteins are key components of the periplasmic oxidative metabolism of acetic acid bacteria, yet several predicted enzymes remain experimentally uncharacterized. Here, we identified and characterized Pqq5 from Gluconobacter japonicus NBRC 3271 as a membrane-bound PQQ-dependent D-lactate dehydrogenase (mLDH). Overexpression of mLDH in a strain lacking six major membrane bound dehydrogenases markedly increased D-lactate dehydrogenase activity in membrane fractions. The enzyme showed a clear preference for D-lactate over L-lactate, exhibited maximal activity at pH 6.0, and retained substantial activity at pH 4.0-6.0. Kinetic analysis using membrane fractions yielded an apparent K

Indexed as

Cell MembraneGluconobacterLactate DehydrogenasesPQQ CofactorHydrogen-Ion ConcentrationKineticsLactic AcidOxidation-ReductionPyruvic AcidSubstrate SpecificityD-lactate dehydrogenaseLactate DehydrogenasesLactic AcidPQQ CofactorPyruvic Acidd-lactate dehydrogenaseGluconobacter japonicusMembrane-bound enzymeQuinoprotein

Identifiers

PMID42010116
PMCPMC13230246

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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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.