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September 15, 2026Microbiology

β-Fructosidases of Planctomycetes: Structure and Evolution

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Authors

DND. G. Naumoff

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Overview

Genomic analysis reveals horizontal gene transfer of GH32 enzymes in planctomycetes, highlighting diverse mechanisms of bacterial carbohydrate utilization.

Key Points

  • Investigate the genetic diversity, domain architecture, and evolutionary trajectory of potential β-fructosidases across the bacterial phylum Planctomycetes.
  • Analyzed genomic sequences from planctomycetes to profile glycoside hydrolase genes linked to fructan degradation.
  • Conducted phylogenetic evaluations and protein domain architecture analyses focusing on glycoside hydrolase family GH32 and carbohydrate-binding module family CBM38.
  • Identified subfamily 32b of the GH32 glycoside hydrolase family as the key enzymatic driver of fructan utilization in planctomycetes.
  • Demonstrated multiple lateral gene transfer events of β-fructosidase genes within Planctomycetes and across diverse bacterial phyla.
  • Uncovered structural variations in planctomycetal β-fructosidases, specifically the selective presence or absence of the CBM38 substrate-binding domain.

Cite This Study

D. G. Naumoff (2026) studied this question.

synapsesocial.com/papers/6aa9134b9013453be30a114bhttps://doi.org/10.1134/s002626172660179x
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