Genetic and functional diversity of β-N-acetylgalactosamine-targeting glycosidases expanded by deep-sea metagenome analysis

Tomomi Sumida (), Satoshi Hiraoka, Keiko Usui, Akihiro Ishiwata, Toru Sengoku, Keith A. Stubbs, Katsunori Tanaka, Shigeru Deguchi, Shinya Fushinobu () and Takuro Nunoura
Additional contact information
Tomomi Sumida: Japan Agency for Marine-Earth Science and Technology (JAMSTEC)
Satoshi Hiraoka: Japan Agency for Marine-Earth Science and Technology (JAMSTEC)
Keiko Usui: Japan Agency for Marine-Earth Science and Technology (JAMSTEC)
Akihiro Ishiwata: Cluster for Pioneering Research
Toru Sengoku: Yokohama City University Graduate School of Medicine, Kanazawa-ku
Keith A. Stubbs: The University of Western Australia
Katsunori Tanaka: Cluster for Pioneering Research
Shigeru Deguchi: Japan Agency for Marine-Earth Science and Technology (JAMSTEC)
Shinya Fushinobu: The University of Tokyo
Takuro Nunoura: Japan Agency for Marine-Earth Science and Technology (JAMSTEC)

Nature Communications, 2024, vol. 15, issue 1, 1-18

Abstract: Abstract β-N-Acetylgalactosamine-containing glycans play essential roles in several biological processes, including cell adhesion, signal transduction, and immune responses. β-N-Acetylgalactosaminidases hydrolyze β-N-acetylgalactosamine linkages of various glycoconjugates. However, their biological significance remains ambiguous, primarily because only one type of enzyme, exo-β-N-acetylgalactosaminidases that specifically act on β-N-acetylgalactosamine residues, has been documented to date. In this study, we identify four groups distributed among all three domains of life and characterize eight β-N-acetylgalactosaminidases and β-N-acetylhexosaminidase through sequence-based screening of deep-sea metagenomes and subsequent searching of public protein databases. Despite low sequence similarity, the crystal structures of these enzymes demonstrate that all enzymes share a prototype structure and have diversified their substrate specificities (oligosaccharide-releasing, oligosaccharide/monosaccharide-releasing, and monosaccharide-releasing) through the accumulation of mutations and insertional amino acid sequences. The diverse β-N-acetylgalactosaminidases reported in this study could facilitate the comprehension of their structures and functions and present evolutionary pathways for expanding their substrate specificity.

Date: 2024
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-024-47653-2 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-47653-2

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-024-47653-2

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().