The C-terminal lectin-like domain modulates the substrate specificity and transglycosylation activity of rice β-galactosidase1 (

Sunaree Choknud, Thipwarin Rimlumduan, Surapoj Sanram, Jenis Chiawitthayanan, Wipa Suginta, James R Ketudat Cairns

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Article in PeerJ, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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3 · Its place in the literature

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1 citing paper in PubMed.

Combined genome and transcriptome analysis of boll weight and lint percentage traits in Gossypium barbadense.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026
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6 authors.

Sunaree ChoknudSchool of Chemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima, Thailand.

Thipwarin RimlumduanDepartment of Applied Biology, Faculty of Science and Liberal Arts, Rajamangala University of Technology Isan, Nakhon Ratchasima, Thailand.

Surapoj SanramSchool of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology, Rayong, Thailand.

Jenis ChiawitthayananSchool of Chemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima, Thailand.

Wipa SugintaSchool of Biomolecular Science and Engineering, Vidyasirimedhi Institute of Science and Technology, Rayong, Thailand.

James R Ketudat CairnsSchool of Chemistry, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima, Thailand.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Background: β-galactosidases (EC 3.2.1.23) are glycosidases that release nonreducing terminal β-d-galactosyl residues from saccharides or glycosides. In plants, most characterized β-galactosidases belong to glycoside hydrolase family 35 (GH35) and function in cell wall remodeling. Over half of plant GH35 enzymes contain a C-terminal lectin-like domain absent in GH35 enzymes from other kingdoms, but its function remains unclear. In this work, we investigate the role of the C-terminal lectin-like domain by the effect of its deletion in rice β-galactosidase 1 ( Methods: We expressed Results:

Indexed as

beta-GalactosidaseOryzaPlant ProteinsGlycosylationKineticsProtein DomainsSaccharomycetalesSubstrate Specificitybeta-GalactosidasePlant ProteinsAccessory domainGlycosidaseGlycoside hydrolaseGlycosylationPichia pastoris

Identifiers

PMID41978877

DOI10.7717/peerj.21066

PMCPMC13070324

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