Cited by 8Microbial metabolism and enzyme functionMicrobial bioremediation and biosurfactantsEnzyme Production and Characterization

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

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Kaur, Arashdeep, Scott, Nichollas E., Herisse, Marion, Goddard-Borger, Ethan D., Pidot, Sacha, Williams, Spencer J.·2023·Archives of Microbiology

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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.

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Metadata

Authors
Kaur, A., Scott, N. E., Herisse, M., Goddard-Borger, E. D., Pidot, S., & Williams, S. J.
Affiliations
The University of Melbourne (AU)
Corresponding author
Williams, Spencer J.
Venue
Archives of Microbiology
Published
2023-03-31
Volume
205
Issue
4
Pages
155-155
ISSN
  • 0003-9276 (ISSN-L)
  • 0302-8933
  • 1432-072X
OpenAlex
W4362522592
Cited by
8
References
1
Citations by year
2026: 2 · 2024: 5 · 2023: 1
FWCI
0.71
Type
journal article
Language
en
Open access
Locations
  • Archives of Microbiology (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Minerva Access (University of Melbourne) (submittedVersion, cc-by)
Funders
  • Australian Research Council (FT200100270, DP210100233)
  • National Health and Medical Research Council (GNT2000517)
  • University of Melbourne
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial metabolism and enzyme function
  • Physical Sciences › Environmental Science › Pollution › Microbial bioremediation and biosurfactants
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
Keywords
soil bacteria, ABC transporters, solute binding protein, levoglucosan, bacterial metabolic pathways, protein structure prediction
MeSH terms
Bacteria, Glucose, Sugar Phosphates, Actinobacteria

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