LIPABASE: a database for 'true' lipase family enzymes.
Identifieur interne : 000142 ( Main/Exploration ); précédent : 000141; suivant : 000143LIPABASE: 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
Affiliations:
Links toward previous steps (curation, corpus...)
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- to stream PubMed, to step Curation: 000675
- to stream PubMed, to step Checkpoint: 000686
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- to stream Main, to step Curation: 000142
Le document en format XML
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Ghram</name></author><author><name sortKey="Hamida, Jeannette Ben" sort="Hamida, Jeannette Ben" uniqKey="Hamida J" first="Jeannette Ben" last="Hamida">Jeannette Ben Hamida</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2011">2011</date><idno type="RBID">pubmed:22112530</idno><idno type="pmid">22112530</idno><idno type="doi">10.1504/IJBRA.2011.043770</idno><idno type="wicri:Area/PubMed/Corpus">000679</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000679</idno><idno type="wicri:Area/PubMed/Curation">000675</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000675</idno><idno type="wicri:Area/PubMed/Checkpoint">000686</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000686</idno><idno type="wicri:Area/Main/Merge">000142</idno><idno type="wicri:Area/Main/Curation">000142</idno><idno 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first="Imen" last="Ghram">Imen Ghram</name></author><author><name sortKey="Hamida, Jeannette Ben" sort="Hamida, Jeannette Ben" uniqKey="Hamida J" first="Jeannette Ben" last="Hamida">Jeannette Ben Hamida</name></author></analytic><series><title level="j">International journal of bioinformatics research and applications</title><idno type="ISSN">1744-5485</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs (MeSH)</term><term>Amino Acid Sequence (MeSH)</term><term>Catalytic Domain (MeSH)</term><term>Databases, Protein (MeSH)</term><term>Lipase (chemistry)</term><term>Lipase (classification)</term><term>Molecular Sequence Data (MeSH)</term><term>Protein Folding (MeSH)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Proteomics (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Bases de données de protéines (MeSH)</term><term>Domaine catalytique (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Motifs d'acides aminés (MeSH)</term><term>Pliage des protéines (MeSH)</term><term>Protéomique (MeSH)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Triacylglycerol lipase (classification)</term><term>Triacylglycerol lipase (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Lipase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="classification" xml:lang="en"><term>Lipase</term></keywords><keywords scheme="MESH" qualifier="classification" xml:lang="fr"><term>Triacylglycerol lipase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Triacylglycerol lipase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Catalytic Domain</term><term>Databases, Protein</term><term>Molecular Sequence Data</term><term>Protein Folding</term><term>Protein Structure, Tertiary</term><term>Proteomics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Bases de données de protéines</term><term>Domaine catalytique</term><term>Données de séquences moléculaires</term><term>Motifs d'acides aminés</term><term>Pliage des protéines</term><term>Protéomique</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI><affiliations><list><country><li>Tunisie</li></country></list><tree><noCountry><name sortKey="Belguith, Hatem" sort="Belguith, Hatem" uniqKey="Belguith H" first="Hatem" last="Belguith">Hatem Belguith</name><name sortKey="Ghram, Imen" sort="Ghram, Imen" uniqKey="Ghram I" first="Imen" last="Ghram">Imen Ghram</name><name sortKey="Hamida, Jeannette Ben" sort="Hamida, Jeannette Ben" uniqKey="Hamida J" first="Jeannette Ben" last="Hamida">Jeannette Ben Hamida</name></noCountry><country name="Tunisie"><noRegion><name sortKey="Messaoudi, Abdelmonaem" sort="Messaoudi, Abdelmonaem" uniqKey="Messaoudi A" first="Abdelmonaem" last="Messaoudi">Abdelmonaem Messaoudi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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