ArticleThe Journal of biological chemistry2014
Fully deacetylated chitooligosaccharides act as efficient glycoside hydrolase family 18 chitinase inhibitors.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Discovery of conformation constrained tetracyclic compounds as potent chitinaseJournal of enzyme inhibition and medicinal chemistry · 2025Article
- Dissolving Chitin by Novel Deep Eutectic Solvents for Effectively Enzymatic Hydrolysis.Applied biochemistry and biotechnology · 2024Article
- Article
- Discovery of Kasugamycin as a Potent Inhibitor of Glycoside Hydrolase Family 18 Chitinases.Frontiers in molecular biosciences · 2021Article
- Crystal structure-guided design of berberine-based novel chitinase inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2020Article
- A Plumieridine-Rich Fraction FromFrontiers in microbiology · 2020Article
- Structural dissection reveals a general mechanistic principle for group II chitinase (ChtII) inhibition.The Journal of biological chemistry · 2019Article
- Glycoside hydrolase family 18 and 20 enzymes are novel targets of the traditional medicine berberine.The Journal of biological chemistry · 2018Article
- A Review of the Preparation, Analysis and Biological Functions of Chitooligosaccharide.International journal of molecular sciences · 2018Review
- Chitinase Induction Prior to Caspofungin Treatment of Experimental Invasive Aspergillosis in Neutropenic Rats Does Not Enhance Survival.Antimicrobial agents and chemotherapy · 2018Article
- Structure, Catalysis, and Inhibition ofThe Journal of biological chemistry · 2017Article
- Inverse relationship between chitobiase and transglycosylation activities of chitinase-D from Serratia proteamaculans revealed by mutational and biophysical analyses.Scientific reports · 2015Article
- The predominant molecular state of bound enzyme determines the strength and type of product inhibition in the hydrolysis of recalcitrant polysaccharides by processive enzymes.The Journal of biological chemistry · 2015Article
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5 authors.
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Abstract
Small molecule inhibitors against chitinases have potential applications as pesticides, fungicides, and antiasthmatics. Here, we report that a series of fully deacetylated chitooligosaccharides (GlcN)2-7 can act as inhibitors against the insect chitinase OfChtI, the human chitinase HsCht, and the bacterial chitinases SmChiA and SmChiB with IC50 values at micromolar to millimolar levels. The injection of mixed (GlcN)2-7 into the fifth instar larvae of the insect Ostrinia furnacalis resulted in 85% of the larvae being arrested at the larval stage and death after 10 days, also suggesting that (GlcN)2-7 might inhibit OfChtI in vivo. Crystal structures of the catalytic domain of OfChtI (OfChtI-CAD) complexed with (GlcN)5,6 were obtained at resolutions of 2.0 Å. These structures, together with mutagenesis and thermodynamic analysis, suggested that the inhibition was strongly related to the interaction between the -1 GlcN residue of the inhibitor and the catalytic Glu(148) of the enzyme. Structure-based comparison showed that the fully deacetylated chitooligosaccharides mimic the substrate chitooligosaccharides by binding to the active cleft. This work first reports the inhibitory activity and proposed inhibitory mechanism of fully deacetylated chitooligosaccharides. Because the fully deacetylated chitooligosaccharides can be easily derived from chitin, one of the most abundant materials in nature, this work also provides a platform for developing eco-friendly inhibitors against chitinases.
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