Functional Properties of the Catalytic Domain of Mouse Acidic Mammalian Chitinase Expressed in Escherichia coli

@article{Kashimura2015FunctionalPO,
  title={Functional Properties of the Catalytic Domain of Mouse Acidic Mammalian Chitinase Expressed in Escherichia coli},
  author={Akinori Kashimura and Masahiro Kimura and Kazuaki Okawa and Hirotaka Suzuki and Atsushi Ukita and Satoshi Wakita and Kana Okazaki and Misa Ohno and Peter O. Bauer and Masayoshi Sakaguchi and Yasusato Sugahara and Fumitaka Oyama},
  journal={International Journal of Molecular Sciences},
  year={2015},
  volume={16},
  pages={4028 - 4042}
}
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… 
Effects of domains modification on the catalytic potential of chitinase from Pseudomonas aeruginosa.
TLDR
The improved solubility and activity of CHA by domain deficiency is an interesting pathway to study the relationship of structure and function of chitinase and support its potential use in commercial applications.
Functional Properties of Mouse Chitotriosidase Expressed in the Periplasmic Space of Escherichia coli
TLDR
It is indicated that Chit1 degrades chitin substrates under physiological conditions and suggest its important pathophysiological roles in vivo.
Comparative functional analysis between human and mouse chitotriosidase: Substitution at amino acid 218 modulates the chitinolytic and transglycosylation activity.
TLDR
A substantially higher chitinolytic and transglycosylation activity of human Chit1 against artificial and natural chitin substrates as compared to the mouse enzyme is revealed.
Acidic mammalian chitinase is a proteases-resistant glycosidase in mouse digestive system
TLDR
Evidence is provided that acidic mammalian chitinase (AMCase) can function as a protease-resistant major glycosidase under the conditions of stomach and intestine and degrade chit in substrates to produce (GlcNAc)2, a source of carbon, nitrogen and energy.
Loss and Gain of Human Acidic Mammalian Chitinase Activity by Nonsynonymous SNPs
TLDR
The data suggest that human AMCase has lost its chitinolytic activity by integration of nsSNPs during evolution and that the enzyme can be reactivated by introducing amino acids conserved in the mouse counterpart.
Characterization of two Listeria innocua chitinases of different sizes that were expressed in Escherichia coli
TLDR
Two putative chitinase genes, lin0153 and lin1996, from the nonpathogenic bacterium Listeria innocua were expressed in Escherichia coli, and the gene products were characterized, which showed different reactivity toward oligomeric substrates.
Protease resistance of porcine acidic mammalian chitinase under gastrointestinal conditions implies that chitin-containing organisms can be sustainable dietary resources
TLDR
It is reported that pig AMCase is stable in the presence of other digestive proteases and functions as chitinolytic enzyme under the gastrointestinal conditions and indicates that chitin-containing organisms may be a sustainable feed ingredient in pig diet.
Cloning and expression of a chitinase gene from Eisenia fetida.
TLDR
The optimal catalytic temperature of rEF-chi was identified as 60°C, and the hydrolytic product from colloidal chitin was N-acetyl-chitobiose, suggesting that EF-Chi is an exo-type enzyme.
Mouse acidic mammalian chitinase exhibits transglycosylation activity at somatic tissue pH
TLDR
The results indicate that mouse AMCase catalyzes hydrolysis as well as transglycosylation and suggest that this enzyme can play a novel role under physiological conditions in peripheral tissues, such as the lungs.
Characterization of mouse di-N-acetylchitobiase that can degrade chitin-oligosaccharides
TLDR
The results suggest that Ctbs digests chitin-oligosaccharides or (GlcNAc)2 of reducing-end residues of oligosACcharides and produces Glc NAc in mouse tissues, which is similar to previous reports on di-N-acetylchitobiase.
...
1
2
...

References

SHOWING 1-10 OF 41 REFERENCES
Protein A-Mouse Acidic Mammalian Chitinase-V5-His Expressed in Periplasmic Space of Escherichia coli Possesses Chitinase Functions Comparable to CHO-Expressed Protein
TLDR
The E. coli-expressed Protein A-mouse AMCase-V5-His fusion protein possesses chitinase functions comparable to the CHO-expressive AMCase and can be used to elucidate detailed biomedical functions of the mouse AMCase.
Structural and Functional Definition of the Human Chitinase Chitin-binding Domain*
TLDR
Structural features of the minimal domain of human chitinase required for both specifically binding to and hydrolyzing insoluble ch itin are defined and relevant binding within the context of the fungal cell wall is demonstrated.
Identification of a Novel Acidic Mammalian Chitinase Distinct from Chitotriosidase*
TLDR
The study has revealed the existence of a chitinolytic enzyme in the gastrointestinal tract and lung that may play a role in digestion and/or defense.
Triad of polar residues implicated in pH specificity of acidic mammalian chitinase
TLDR
The novel structure of the AMCase catalytic domain, both in the apo form and in complex with the inhibitor methylallosamidin, determined to high resolution by X‐ray crystallography provides a structural basis for understanding some of the unique characteristics of this enzyme, including the low pH optimum and the preference for the β‐anomer of the substrate.
Differential Enzymatic Activity of Common Haplotypic Versions of the Human Acidic Mammalian Chitinase Protein*
TLDR
The structural, kinetic, and genetic data regarding the AMCase isoforms are consistent with the Th2-priming effects of environmental chitin and a role for AMCase in negatively regulating this stimulus.
Chitotriosidase, a chitinase, and the 39-kDa human cartilage glycoprotein, a chitin-binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages.
TLDR
It is experimentally demonstrated that a single amino acid substitution in the catalytic centre of the 39-kDa isoform of chitotriosidase, which generates a similar sequence to that in HC gp-39, results in a loss of hydrolytic activity and creates the capacity to bind to chitin.
Evolution of Mammalian Chitinase(-Like) Members of Family 18 Glycosyl Hydrolases
TLDR
Molecular phylogenetic analyses suggest that both active chitinases (chitotriosidase and AMCase) result from an early gene duplication event, and substantial gene specialization has occurred in time, allowing for tissue-specific expression of pH optimized chit inases and chi-lectins.
Cloning of a cDNA Encoding Chitotriosidase, a Human Chitinase Produced by Macrophages (*)
TLDR
The results show that, in contrast to previous beliefs, human macrophages can synthesize a functional chitinase, a highly conserved enzyme with a strongly regulated expression that may play a role in the degradation of chitIn-containing pathogens and can be used as a marker for specific disease states.
The third chitinase gene (chiC) of Serratia marcescens 2170 and the relationship of its product to other bacterial chitinases.
TLDR
Phylogenetic analysis showed that bacterial family 18 chitinases can be clustered in three subfamilies which have diverged at an early stage of bacterial chit inase evolution.
Purification and Characterization of Human Chitotriosidase, a Novel Member of the Chitinase Family of Proteins (*)
TLDR
The human chitotriosidase described here showed chitinolytic activity toward artificial substrates as well as chitin and may therefore be considered to be a chit inase.
...
1
2
3
4
5
...