ArticleInternational journal of molecular sciences2015
Functional properties of the catalytic domain of mouse acidic mammalian chitinase expressed in Escherichia coli.
Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- Evolution of Acidic Mammalian Chitinase Gene (Ecology and evolution · 2026Article
- A Simplified Method for Evaluating Chitin-Binding Activity Applied to YKL-40 (HC-gp39, CHI3L1) and Chitotriosidase.Molecules (Basel, Switzerland) · 2024Article
- Article
- Irreversible evolutionary loss of chitin-degrading ability in the chitinase-like protein Ym1 under positive selection in rodents.Protein science : a publication of the Protein Society · 2023Article
- Mouse Acidic Chitinase Effectively Degrades Random-Type Chitosan to Chitooligosaccharides of Variable Lengths under Stomach and Lung Tissue pH Conditions.Molecules (Basel, Switzerland) · 2021Article
- Residues of acidic chitinase cause chitinolytic activity degrading chitosan in porcine pepsin preparations.Scientific reports · 2019Article
- Chitins and chitinase activity in airway diseases.The Journal of allergy and clinical immunology · 2018Review
- Acidic Mammalian Chitinase Negatively Affects Immune Responses during Acute and Chronic Aspergillus fumigatus Exposure.Infection and immunity · 2018Article
- Acidic Chitinase-Chitin Complex Is Dissociated in a Competitive Manner by Acetic Acid: Purification of Natural Enzyme for Supplementation Purposes.International journal of molecular sciences · 2018Article
- Protease resistance of porcine acidic mammalian chitinase under gastrointestinal conditions implies that chitin-containing organisms can be sustainable dietary resources.Scientific reports · 2017Article
- Gastric and intestinal proteases resistance of chicken acidic chitinase nominates chitin-containing organisms for alternative whole edible diets for poultry.Scientific reports · 2017Article
- Loss and Gain of Human Acidic Mammalian Chitinase Activity by Nonsynonymous SNPs.Molecular biology and evolution · 2016Article
- Acidic mammalian chitinase is a proteases-resistant glycosidase in mouse digestive system.Scientific reports · 2016Article
- Functional Properties of Mouse Chitotriosidase Expressed in the Periplasmic Space of Escherichia coli.PloS one · 2016Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mouse acidic mammalian chitinase (AMCase) plays important physiological roles in defense and nutrition. AMCase is composed of an N-terminal catalytic domain (CatD) and a C-terminal chitin-binding domain (CBD). We expressed CatD of mouse AMCase as a recombinant fusion protein with Protein A and V5-His in Escherichia coli (Protein A-CatD-V5-His), evaluated its functional properties and compared them to the full-length AMCase (Protein A-AMCase-V5-His). Under our experimental conditions, the chitinolytic activity of both proteins against 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside was equivalent with regard to their specific enzymatic activities, optimal pH and temperature as well as to the pH and temperature stability. CatD bound to chitin beads and cleaved the N-acetylglucosamine hexamer, colloidal and crystalline chitin as well as the shrimp shell, and released primarily N,N'-diacetylchitobiose fragments at pH 2.0. These results indicate that the primary structure of CatD is sufficient to form a proper tertiary structure required for chitinolytic activity, recognize chitin substrates and degrade them in the absence of a CBD. Our recombinant proteins can be used for further studies evaluating pathophysiological roles of AMCase in different diseases.
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