ArticleActa crystallographica. Section D, Structural biology2018
The deduced role of a chitinase containing two nonsynergistic catalytic domains.
Article in Acta crystallographica. Section D, Structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 36 citations in OpenAlex.
- Genome-Wide Identification and Analysis of Chitinase GH18 Gene Family inJournal of fungi (Basel, Switzerland) · 2025Article
- Three-Step Enzymatic Remodeling of Chitin into Bioactive Chitooligomers.Journal of agricultural and food chemistry · 2024Article
- Insights into Chitin-Degradation Potential ofMicroorganisms · 2024Article
- Secretory CAZymes profile and GH19 enzymes analysis ofFrontiers in microbiology · 2024Article
- Identification and Characterization of Three Chitinases with Potential in Direct Conversion of Crystalline Chitin intoMarine drugs · 2022Article
- A chitinase with two catalytic domains is required for organization of the cuticular extracellular matrix of a beetle.PLoS genetics · 2018Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The glycoside hydrolase family 18 chitinases degrade or alter chitin. Multiple catalytic domains in a glycoside hydrolase family 18 chitinase function synergistically during chitin degradation. Here, an insect group III chitinase from the agricultural pest Ostrinia furnacalis (OfChtIII) is revealed to be an arthropod-conserved chitinase that contains two nonsynergistic GH18 domains according to its catalytic properties. Both GH18 domains are active towards single-chained chitin substrates, but are inactive towards insoluble chitin substrates. The crystal structures of each unbound GH18 domain, as well as of GH18 domains complexed with hexa-N-acetyl-chitohexaose or penta-N-acetyl-chitopentaose, suggest that the two GH18 domains possess endo-specific activities. Physiological data indicated that the developmental stage-dependent gene-expression pattern of OfChtIII was the same as that of the chitin synthase OfChsA but significantly different from that of the chitinase OfChtI, which is indispensable for cuticular chitin degradation. Additionally, immunological staining indicated that OfChtIII was co-localized with OfChsA. Thus, OfChtIII is most likely to be involved in the chitin-synthesis pathway.
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