Evidence map›Paper›PMID 18467457›Full record

ArticlePlant physiology2008

The beta-glucosidases responsible for bioactivation of hydroxynitrile glucosides in Lotus japonicus.

Anne Vinther Morant, Nanna Bjarnholt, Mads Emil Kragh, Christian Hauge Kjaergaard, Kirsten Jørgensen, Suzanne Michelle Paquette, Markus Piotrowski, Anne Imberty, Carl Erik Olsen, Birger Lindberg Møller and 1 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.0field-weighted citation impact, top 9% of its field
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

25 citing papers in PubMed, 72 citations in OpenAlex.

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  13. Insights into Glucose-6-phosphate Allosteric Activation of β-Glucosidase A.Journal of chemical information and modeling · 2021
    Article
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

11 authors at 1 institution in 1 country.

Anne Vinther MorantPlant Biochemistry Laboratory, Department of Plant Biology, Center for Molecular Plant Physiology and VKR Research Centre "Pro-Active Plants" , University of Copenhagen, DK-1871 Frederiksberg C, Copenhagen, Denmark.
Nanna Bjarnholt
Mads Emil Kragh
Christian Hauge Kjaergaard
Kirsten Jørgensen
Suzanne Michelle Paquette
Markus Piotrowski
Anne Imberty
Carl Erik Olsen
Birger Lindberg Møller
Søren Bak
University of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lotus japonicus accumulates the hydroxynitrile glucosides lotaustralin, linamarin, and rhodiocyanosides A and D. Upon tissue disruption, the hydroxynitrile glucosides are bioactivated by hydrolysis by specific beta-glucosidases. A mixture of two hydroxynitrile glucoside-cleaving beta-glucosidases was isolated from L. japonicus leaves and identified by protein sequencing as LjBGD2 and LjBGD4. The isolated hydroxynitrile glucoside-cleaving beta-glucosidases preferentially hydrolyzed rhodiocyanoside A and lotaustralin, whereas linamarin was only slowly hydrolyzed, in agreement with measurements of their rate of degradation upon tissue disruption in L. japonicus leaves. Comparative homology modeling predicted that LjBGD2 and LjBGD4 had nearly identical overall topologies and substrate-binding pockets. Heterologous expression of LjBGD2 and LjBGD4 in Arabidopsis (Arabidopsis thaliana) enabled analysis of their individual substrate specificity profiles and confirmed that both LjBGD2 and LjBGD4 preferentially hydrolyze the hydroxynitrile glucosides present in L. japonicus. Phylogenetic analyses revealed a third L. japonicus putative hydroxynitrile glucoside-cleaving beta-glucosidase, LjBGD7. Reverse transcription-polymerase chain reaction analysis showed that LjBGD2 and LjBGD4 are expressed in aerial parts of young L. japonicus plants, while LjBGD7 is expressed exclusively in roots. The differential expression pattern of LjBGD2, LjBGD4, and LjBGD7 corresponds to the previously observed expression profile for CYP79D3 and CYP79D4, encoding the two cytochromes P450 that catalyze the first committed step in the biosyntheis of hydroxynitrile glucosides in L. japonicus, with CYP79D3 expression in aerial tissues and CYP79D4 expression in roots.

Indexed as

ArabidopsisBinding SitesCellulasesCytochrome P-450 Enzyme SystemGlucosidesHydrolysisIsoenzymesLotusModels, MolecularNaphthalenesNitrilesPhylogenyPlant LeavesPlant RootsPlants, Genetically ModifiedSequence Homology, Amino AcidCellulasescytochrome P-450 79D3, Lotus japonicusCytochrome P-450 Enzyme SystemGlucosidesIsoenzymeslotaustralinNaphthalenesNitriles

Identifiers

PMID18467457
PMCPMC2442532
OpenAlexW2141855846

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.