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Boot, R.G. et al.

Boot, Blommaart, Swart, Ghauharali-van der Vlugt, Bijl, Moe, Place, Aerts,

Identification of a novel acidic mammalian chitinase distinct from chitotriosidase.

Chitinases are ubiquitous chitin-fragmenting hydrolases. Recently we discovered the first human chitinase, named chitotriosidase, that is specifically expressed by phagocytes. We here report the identification, purification, and subsequent cloning of a second mammalian chitinase. This enzyme is characterized by an acidic isoelectric point and therefore named acidic mammalian chitinase ( AMCase). In rodents and man the enzyme is relatively abundant in the gastrointestinal tract and is found to a lesser extent in the lung. Like chitotriosidase, AMCase is synthesized as a 50-kDa protein containing a 39-kDa N-terminal catalytic domain, a hinge region, and a C-terminal chitin-binding domain. In contrast to chitotriosidase, the enzyme is extremely acid stable and shows a distinct second pH optimum around pH 2. AMCase is capable of cleaving artificial chitin-like substrates as well as crab shell chitin and chitin as present in the fungal cell wall. Our 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.[1]

References

Identification of a novel acidic mammalian chitinase distinct from chitotriosidase. Boot, R.G., Blommaart, E.F., Swart, E., Ghauharali-van der Vlugt, K., Bijl, N., Moe, C., Place, A., Aerts, J.M. J. Biol. Chem. (2001) [Pubmed]

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