Avtor/Urednik		Karlsson, M; Contreras, JA; Hellman, U; Tornqvist, H; Holm, C
Naslov		cDNA cloning, tissue distribution, and identification of the catalytic triad of monoglyceride lipase. Evolutionary relationship to esterases, lysophospholipases, and haloperoxidases
Tip		članek
Vir		J Biol Chem
Vol. in št.		Letnik 272, št. 43
Leto izdaje		1997
Obseg		str. 27218-23
Jezik		eng
Abstrakt		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.
Deskriptorji		EVOLUTION, MOLECULAR ESTERASES LYSOPHOSPHOLIPASE MICE MOLECULAR SEQUENCE DATA MONOACYLGLYCEROL LIPASES ORGAN SPECIFICITY PEROXIDASES RATS RECOMBINANT PROTEINS SEQUENCE ALIGNMENT SEQUENCE HOMOLOGY, AMINO ACID TRANSFECTION ADIPOCYTES AMINO ACID SEQUENCE BASE SEQUENCE COS CELLS CATALYSIS CLONING, MOLECULAR DNA, COMPLEMENTARY