Evidence map›Paper›PMID 37000297›Full record

ArticleArchives of microbiology2023

Identification of levoglucosan degradation pathways in bacteria and sequence similarity network analysis.

Arashdeep Kaur, Nichollas E Scott, Marion Herisse, Ethan D Goddard-Borger, Sacha Pidot, Spencer J Williams

Open access · hybridAbstract read
In one paragraph

Article in Archives of microbiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 33% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Identification and characterization of the lipoproteinProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. 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

6 authors at 1 institution in 1 country.

Arashdeep KaurSchool of Chemistry, University of Melbourne, Parkville, VIC, 3010, Australia.
Nichollas E ScottDepartment of Microbiology and Immunology, University of Melbourne, at the Peter Doherty Institute for Infection and Immunity, Victoria, 3000, Australia.
Marion HerisseDepartment of Microbiology and Immunology, University of Melbourne, at the Peter Doherty Institute for Infection and Immunity, Victoria, 3000, Australia.
Ethan D Goddard-BorgerDepartment of Medical Biology, University of Melbourne, Parkville, VIC, 3010, Australia.
Sacha PidotDepartment of Microbiology and Immunology, University of Melbourne, at the Peter Doherty Institute for Infection and Immunity, Victoria, 3000, Australia.
Spencer J WilliamsSchool of Chemistry, University of Melbourne, Parkville, VIC, 3010, Australia. sjwill@unimelb.edu.au.ORCID http://orcid.org/0000-0001-6341-4364
The University of Melbourne · AU

Funding

Australian Research Council DP210100233Australian Research Council FT200100270National Health and Medical Research Council GNT2000517
6 · The paper itself

Abstract

Levoglucosan is produced in the pyrolysis of cellulose and starch, including from bushfires or the burning of biofuels, and is deposited from the atmosphere across the surface of the earth. We describe two levoglucosan degrading Paenarthrobacter spp. (Paenarthrobacter nitrojuajacolis LG01 and Paenarthrobacter histidinolovorans LG02) that were isolated from soil by metabolic enrichment using levoglucosan as the sole carbon source. Genome sequencing and proteomics analysis revealed the expression of a series of genes encoding known levoglucosan degrading enzymes, levoglucosan dehydrogenase (LGDH, LgdA), 3-keto-levoglucosan β -eliminase (LgdB1) and glucose 3-dehydrogenase (LgdC), along with an ABC transporter cassette and an associated solute binding protein. However, no homologues of 3-ketoglucose dehydratase (LgdB2) were evident, while the expressed genes contained a range of putative sugar phosphate isomerases/xylose isomerases with weak similarity to LgdB2. Sequence similarity network analysis of genome neighbours of LgdA revealed that homologues of LgdB1 and LgdC are generally conserved in a range of bacteria in the phyla Firmicutes, Actinobacteria and Proteobacteria. One group of sugar phosphate isomerase/xylose isomerase homologues (named LgdB3) was identified with limited distribution that is mutually exclusive with LgdB2, and we propose that they may fulfil a similar function. LgdB1, LgdB2 and LgdB3 adopt similar predicted 3D folds, suggesting overlapping function in processing intermediates in LG metabolism. Our findings highlight diversity within the LGDH pathway, through which bacteria utilize levoglucosan as a nutrient source.

Indexed as

ActinobacteriaSugar PhosphatesBacteriaGlucose1,6-anhydro-beta-glucopyranoseGlucoseSugar PhosphatesAnhydrosugarCarbohydrateMetabolismSequence similarity network analysis

Identifiers

PMID37000297
PMCPMC10066097
OpenAlexW4362522592

What OpenQuestion holds

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LicenceCC BY
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.