title: LIPABASE: a database for 'true' lipase family enzymes.
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.
authors: Institut Superieur des Sciences Biologiques Appliquees de Tunis, Universite Tunis El Manar, Tunisie. amessaoudi@tvtc.gov.sa
authors: Abdelmonaem
authors: A
authors: Messaoudi
authors: Hatem
authors: H
authors: Belguith
authors: Imen
authors: I
authors: Ghram
authors: Jeannette Ben
authors: JB
authors: Hamida
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D020134:Catalytic Domain; D030562:Databases, Protein; D008049:Lipase / Q000737:chemistry* / Q000145:classification; D008969:Molecular Sequence Data; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D040901:Proteomics
chemical_list: D008049:Lipase