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Originally published In Press as doi:10.1074/jbc.M009886200 on November 20, 2000
J. Biol. Chem., Vol. 276, Issue 9, 6770-6778, March 2, 2001
Identification of a Novel Acidic Mammalian
Chitinase Distinct from Chitotriosidase*
Rolf G.
Boot §,
Edward F. C.
Blommaart ,
Erwin
Swart ,
Karen
Ghauharali-van der Vlugt ,
Nora
Bijl ,
Cassandra
Moe¶ ,
Allen
Place¶ , and
Johannes M. F. G.
Aerts
From the Department of Biochemistry, University of
Amsterdam, Academic Medical Center, 1105 AZ Amsterdam, The
Netherlands and the ¶ Center of Marine Biotechnology, University
of Maryland Biotechnology Institute, Baltimore, Maryland 21202
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.
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
§
To whom correspondence should be addressed: Dept. of Biochemistry,
University of Amsterdam, Academic Medical Center, P.O. Box 22700, 1100 DE Amsterdam, The Netherlands. Tel.: 31-20-5665161; Fax:
31-20-6915519; E-mail: r.g.boot@amc.uva.nl.
Supported by National Science Foundation Grant IBN-9604265 and
by funds from the Center of Marine Biotechnology, University of
Maryland Biotechnology Institute.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.
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