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Volume 272, Number 43, Issue of October 24, 1997 pp. 27218-27223
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

cDNA Cloning, Tissue Distribution, and Identification of the Catalytic Triad of Monoglyceride Lipase
EVOLUTIONARY RELATIONSHIP TO ESTERASES, LYSOPHOSPHOLIPASES, AND HALOPEROXIDASES

(Received for publication, May 27, 1997, and in revised form, July 21, 1997)

Marie Karlsson , Juan A. Contreras , Ulf Hellman ^§ , Hans Tornqvist ^¶ and Cecilia Holm

From the  Section for Molecular Signalling, Department of Cell and Molecular Biology, Lund University, P.O. Box 94, S-221 00 Lund, Sweden, the ^§ Ludwig Institute for Cancer Research, P.O. Box 595, S-751 24 Uppsala, Sweden, and the ^¶ Department of Pediatrics, University Hospital, S-221 85 Lund, Sweden, and  Novo Nordisk A/S, Niels Steensens Vej 1, DK-2820 Gentofte, Denmark

Monoglyceride lipase catalyzes the last step in the hydrolysis of stored triglycerides in the adipocyte and presumably also complements the action of lipoprotein lipase in degrading triglycerides from chylomicrons and very low density lipoproteins. Monoglyceride lipase was cloned from a mouse adipocyte cDNA library. The predicted amino acid sequence consisted of 302 amino acids, corresponding to a molecular weight of 33,218. The sequence showed no extensive homology to other known mammalian proteins, but a number of microbial proteins, including two bacterial lysophospholipases and a family of haloperoxidases, were found to be distantly related to this enzyme. By means of multiple sequence alignment and secondary structure prediction, the structural elements in monoglyceride lipase, as well as the putative catalytic triad, were identified. The residues of the proposed triad, Ser-122, in a GXSXG motif, Asp-239, and His-269, were confirmed by site-directed mutagenesis experiments. Northern blot analysis revealed that monoglyceride lipase is ubiquitously expressed among tissues, with a transcript size of about 4 kilobases.

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