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Identification of a novel acidic mammalian chitinase distinct from chitotriosidase.

Authors: Boot, RG  Blommaart, EF  Swart, E  Ghauharali-van der Vlugt, K  Bijl, N  Moe, C  Place, A  Aerts, JM 
Citation: Boot RG, etal., J Biol Chem. 2001 Mar 2;276(9):6770-8. Epub 2000 Nov 20.
Pubmed: (View Article at PubMed) PMID:11085997
DOI: Full-text: DOI:10.1074/jbc.M009886200

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.

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CRRD Object Information
CRRD ID: 5000759
Created: 2011-03-01
Species: All species
Last Modified: 2011-03-01
Status: ACTIVE



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