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Int J Bioinform Res Appl ; 7(4): 390-401, 2011.
Article in English | MEDLINE | ID: mdl-22112530

ABSTRACT

Lipase enzymes play an important role in lipid metabolism and are produced by a variety of species. Compared with animal, bacterial and fungal, little is known about plant lipases. Although lipases belong to many different protein families, they have the same architecture, the ?/?-hydrolase fold and a conserved active site signature, the Gly-Xaa-Ser-Xaa-Gly motif. Several studies on enzymatic activity and interfacial activation phenomenon of lipases confirm the presence of consensus sequence and a conserved domain. Lipases can be divided into two main groups: carboxylesterases (EC 3.1.1.1); 'true' lipases (EC 3.1.1.3), which differ in several biochemical features, which allow us to develop a database that regroups all 'true' lipase proprieties to establish relationship between structure and function. LIPABASE is a centralised resource database, which provides information about 'true' lipase from different species. It includes general, taxonomic, physicochemical and molecular data. Access to LIPABASE is free and available at http://www.lipabase-pfba-tun.org.


Subject(s)
Databases, Protein , Lipase/chemistry , Amino Acid Motifs , Amino Acid Sequence , Catalytic Domain , Lipase/classification , Molecular Sequence Data , Protein Folding , Protein Structure, Tertiary , Proteomics
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