Evidence map›Paper›PMID 41556626›Full record

ArticleProtein science : a publication of the Protein Society2026

Molecular basis and biological relevance of bacterial and plant pinoresinol/lariciresinol reductase specificities.

Clyde A Smith, Diana L Bedgar, Michael A Costa, Syed G A Moinuddin, Marco N Allemann, Joshua K Michener, Laurence B Davin, Norman G Lewis

Abstract read
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In one paragraph

Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

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

1 citing paper in PubMed.

  1. Article
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

8 authors.

Clyde A SmithStanford Synchrotron Radiation Lightsource, Menlo Park, California, USA.ORCID https://orcid.org/0000-0002-1885-1511
Diana L BedgarInstitute of Biological Chemistry, Washington State University, Pullman, Washington, USA.
Michael A CostaInstitute of Biological Chemistry, Washington State University, Pullman, Washington, USA.ORCID https://orcid.org/0009-0006-8638-2151
Syed G A MoinuddinInstitute of Biological Chemistry, Washington State University, Pullman, Washington, USA.ORCID https://orcid.org/0000-0002-9907-416X
Marco N AllemannBiosciences Division Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA.ORCID https://orcid.org/0000-0002-9290-7296
Joshua K MichenerBiosciences Division Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA.ORCID https://orcid.org/0000-0003-2302-8180
Laurence B DavinInstitute of Biological Chemistry, Washington State University, Pullman, Washington, USA.ORCID https://orcid.org/0000-0002-3248-6485
Norman G LewisInstitute of Biological Chemistry, Washington State University, Pullman, Washington, USA.ORCID https://orcid.org/0000-0001-5742-032X

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Aina E. Cohen, KEITH O HODGSON · 2020 to 2026
$43.3M
National Institute of Food and Agriculture WNP7003632NIGMS NIH HHS P30 GM133894NIGMS NIH HHS P30GM133894Oak Ridge National LaboratoryU.S. Department of Energy
6 · The paper itself

Abstract

A bacterial pinoresinol/lariciresinol reductase (PLR) homolog named NrPinZ was obtained from a Novosphingobium rhizosphaerae sp. LY bacterial strain, with NrPinZ being part of its 5-step biochemical system catabolizing pinoresinol into coniferyl aldehyde and vanillin. Recombinant NrPinZ reduces racemic 8-8' furanofuran lignans [(±)-pinoresinols, medioresinols, and syringaresinols] with similar overall catalytic efficiencies. In those reductions, only one of the two furan ring systems is reduced. Two other bacterial PLR homologs, NaPinZ and SlPinZ, from N. aromaticivorans F199 and Sphingobium lignivorans SYK-6, respectively, had comparable substrate versatilities and catalytic efficacies. Plant PLR homologs, by comparison, are either enantiospecific, enantioselective, or variants thereof, being able to reduce either one or both furan rings. For example, a recombinant enantioselective PLR (PLR_Tp2) from western red cedar (Thuja plicata) preferentially reduces both (+)-pinoresinol furan rings to afford (-)-secoisolariciresinol. BoltZ-2 modeling of NrPinZ and PLR_Tp2, together with substrate docking of (+)- and (-)-pinoresinols, medioresinols, and syringaresinols, was very instructive. The NrPinZ active site P1/P2 sub-pockets allow for both racemic forms to be catabolized. Conversely, the smaller P1 pocket in PLR_Tp2 preferentially positions (+)-pinoresinol for downstream metabolism into (-)-secoisolariciresinol, thereby providing a biochemical explanation for the different stereochemical outcomes. NrPinZ, NaPinZ, and SlPinZ, catalyzing substrate versatile catabolism of both racemic forms, may have important ramifications for gymnosperm and angiosperm lignin and lignan biodegradation, including its evolutionary significance and potential in enzyme engineering.

Indexed as

Bacterial ProteinsFuransLignansOxidoreductasesSphingomonadaceaeRecombinant ProteinsSubstrate SpecificityBacterial ProteinsFuranslariciresinol reductaseLignansOxidoreductasespinoresinolpinoresinol reductaseRecombinant ProteinsBoltz‐2 molecular modelingcatabolismlignansligninlignin biodegradationNovosphingobium aromaticivorans F199Novosphingobium rhizosphaeraepinoresinol lariciresinol reductasepinoresinol reductaseSphingobium lignivorans SYK‐6western red cedar (Thuja plicata)

Identifiers

PMID41556626
PMCPMC12817470

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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.