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April 1, 2026Journal of Biological ChemistryOpen Access

MoChia1 is a GH18 Reducing-End GlcNAc–Releasing Chitin Oligosaccharide Hydrolase from the Rice Blast Fungus Magnaporthe oryzae

Takayuki Ohnuma Shun Imaoka Chikara Kataoka Teruki Yoshimoto Ryuta Okada Toru Takeda T Fukamizo Shohei Sakuda Makoto Ogata

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Key Points

The research aims to characterize MoChia1, a glycoside hydrolase from Magnaporthe oryzae, and its role in chitin oligosaccharide hydrolysis.
Identified MoChia1 enzyme from Magnaporthe oryzae.
Analyzed hydrolytic activity on chitin oligosaccharides using HPLC.
Assessed substrate specificity and anomeric selectivity.
Evaluated the inhibitory effects of allosamidin on MoChia1.
MoChia1 hydrolyzed chitin oligosaccharides with a minimum polymerization degree of 3.
It specifically recognized the -anomer of substrates and cleaved at the reducing end.
Allosamidin inhibited MoChia1 activity with an IC50 of 54.4 ± 6.91 µM, suggesting its potential as a pesticide.

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Implication

This research identifies MoChia1 hydrolase that releases GlcNAc from chitin oligosaccharides, suggesting potential pesticide use.

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Cite This Study

Ohnuma et al. (2026) studied this question.

synapsesocial.com/papers/69e4745f010ef96374d9020a https://doi.org/10.1016/j.jbc.2026.111462

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