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PreprintCC BYbioRxiv

GlyEnzEA: reaction-informed enrichment of enzyme-centered glycan sets from glycomics data

  1. 1Institute for Glyco-core Research (iGCORE), Tokai National Higher Education and Research System, Nagoya, Japan

Abstract

Enzyme-centered interpretation of glycomic changes requires testing whether glycans associated with particular reactions change collectively. Motif analyses and reaction databases do not directly provide enzyme-specific sets of measured glycans, and structural ambiguity or overlapping reactions can give different enzymes identical sets. A framework is needed to construct these sets and define distinguishable test hypotheses. GlyEnzEA constructs sets by matching reaction rules to candidate glycan topologies, groups enzymes sharing identical sets, and tests each set once. In an Mgat3-knockout mouse glycome, 48 enzymes yielded 16 sets; only the MGAT3 set showed significant negative enrichment after correction (Storey q=0.033). Across seven HEK293 perturbations, target sets were significant in two conditions: MGAT1 and class-I mannosidase knockouts. GlyEnzEA supports enzyme-centered interpretation at the resolution of distinguishable enzymes or enzyme groups.

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BibTeX
@misc{himori2026glyenzea,
  title = {{GlyEnzEA: reaction-informed enrichment of enzyme-centered glycan sets from glycomics data}},
  author = {K. Himori and B. Zhang and Y. Matsui},
  howpublished = {bioRxiv},
  year = {2026},
  month = oct,
  doi = {10.64898/2026.10.14.759156},
  url = {https://www.biorxiv.org/content/10.64898/2026.10.14.759156v1},
  note = {CC BY},
}
RIS
TY  - UNPB
TI  - GlyEnzEA: reaction-informed enrichment of enzyme-centered glycan sets from glycomics data
AU  - K. Himori
AU  - B. Zhang
AU  - Y. Matsui
PY  - 2026
DA  - 2026/10/14
PB  - bioRxiv
DO  - 10.64898/2026.10.14.759156
UR  - https://www.biorxiv.org/content/10.64898/2026.10.14.759156v1
AB  - Enzyme-centered interpretation of glycomic changes requires testing whether glycans associated with particular reactions change collectively. Motif analyses and reaction databases do not directly provide enzyme-specific sets of measured glycans, and structural ambiguity or overlapping reactions can give different enzymes identical sets. A framework is needed to construct these sets and define distinguishable test hypotheses. GlyEnzEA constructs sets by matching reaction rules to candidate glycan topologies, groups enzymes sharing identical sets, and tests each set once. In an Mgat3-knockout mouse glycome, 48 enzymes yielded 16 sets; only the MGAT3 set showed significant negative enrichment after correction (Storey q=0.033). Across seven HEK293 perturbations, target sets were significant in two conditions: MGAT1 and class-I mannosidase knockouts. GlyEnzEA supports enzyme-centered interpretation at the resolution of distinguishable enzymes or enzyme groups.
ER  -