LIPABASE: a database for 'true' lipase family enzymes.
Identifieur interne : 000675 ( PubMed/Curation ); précédent : 000674; suivant : 000676LIPABASE: a database for 'true' lipase family enzymes.
Auteurs : Abdelmonaem Messaoudi [Tunisie] ; Hatem Belguith ; Imen Ghram ; Jeannette Ben HamidaSource :
- International journal of bioinformatics research and applications [ 1744-5485 ] ; 2011.
Descripteurs français
- KwdFr :
- Bases de données de protéines (MeSH), Domaine catalytique (MeSH), Données de séquences moléculaires (MeSH), Motifs d'acides aminés (MeSH), Pliage des protéines (MeSH), Protéomique (MeSH), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Triacylglycerol lipase (classification), Triacylglycerol lipase (composition chimique).
- MESH :
- classification : Triacylglycerol lipase.
- composition chimique : Triacylglycerol lipase.
- Bases de données de protéines, Domaine catalytique, Données de séquences moléculaires, Motifs d'acides aminés, Pliage des protéines, Protéomique, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Lipase.
- chemical , classification : Lipase.
- Amino Acid Motifs, Amino Acid Sequence, Catalytic Domain, Databases, Protein, Molecular Sequence Data, Protein Folding, Protein Structure, Tertiary, Proteomics.
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.
DOI: 10.1504/IJBRA.2011.043770
PubMed: 22112530
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pubmed:22112530Le document en format XML
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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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22112530</PMID><DateCompleted><Year>2012</Year><Month>04</Month><Day>04</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>05</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1744-5485</ISSN><JournalIssue CitedMedium="Print"><Volume>7</Volume><Issue>4</Issue><PubDate><Year>2011</Year></PubDate></JournalIssue><Title>International journal of bioinformatics research and applications</Title><ISOAbbreviation>Int J Bioinform Res Appl</ISOAbbreviation></Journal><ArticleTitle>LIPABASE: a database for 'true' lipase family enzymes.</ArticleTitle><Pagination><MedlinePgn>390-401</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1504/IJBRA.2011.043770</ELocationID><Abstract><AbstractText>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. 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