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http://purl.uniprot.org/citations/9785454http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9785454http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9785454http://www.w3.org/2000/01/rdf-schema#comment"A fragment of genomic DNA from Sulfolobus acidocaldarius DSM 639 encoding a lipolytic enzyme was cloned and sequenced. The 314-amino acid polypeptide displays a maximum sequence similarity (43%) to a putative polyhydroxyalkanoate depolymerase from Pseudomonas oleovorans and contains the pentapeptide G-X1-S-X2-G which is typical of serine hydrolases. The protein is highly thermostable and is able to hydrolyse a variety of lipid substrates thus providing a promising tool for potential biotechnological applications."xsd:string
http://purl.uniprot.org/citations/9785454http://purl.org/dc/terms/identifier"doi:10.1111/j.1574-6968.1998.tb13209.x"xsd:string
http://purl.uniprot.org/citations/9785454http://purl.org/dc/terms/identifier"doi:10.1111/j.1574-6968.1998.tb13209.x"xsd:string
http://purl.uniprot.org/citations/9785454http://purl.uniprot.org/core/author"Jendrossek D."xsd:string
http://purl.uniprot.org/citations/9785454http://purl.uniprot.org/core/author"Jendrossek D."xsd:string
http://purl.uniprot.org/citations/9785454http://purl.uniprot.org/core/author"Jaeger K.E."xsd:string
http://purl.uniprot.org/citations/9785454http://purl.uniprot.org/core/author"Jaeger K.E."xsd:string
http://purl.uniprot.org/citations/9785454http://purl.uniprot.org/core/author"Arpigny J.L."xsd:string
http://purl.uniprot.org/citations/9785454http://purl.uniprot.org/core/author"Arpigny J.L."xsd:string
http://purl.uniprot.org/citations/9785454http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9785454http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9785454http://purl.uniprot.org/core/name"FEMS Microbiol. Lett."xsd:string
http://purl.uniprot.org/citations/9785454http://purl.uniprot.org/core/name"FEMS Microbiol Lett"xsd:string
http://purl.uniprot.org/citations/9785454http://purl.uniprot.org/core/pages"69-73"xsd:string
http://purl.uniprot.org/citations/9785454http://purl.uniprot.org/core/pages"69-73"xsd:string
http://purl.uniprot.org/citations/9785454http://purl.uniprot.org/core/title"A novel heat-stable lipolytic enzyme from Sulfolobus acidocaldarius DSM 639 displaying similarity to polyhydroxyalkanoate depolymerases."xsd:string
http://purl.uniprot.org/citations/9785454http://purl.uniprot.org/core/title"A novel heat-stable lipolytic enzyme from Sulfolobus acidocaldarius DSM 639 displaying similarity to polyhydroxyalkanoate depolymerases."xsd:string
http://purl.uniprot.org/citations/9785454http://purl.uniprot.org/core/volume"167"xsd:string
http://purl.uniprot.org/citations/9785454http://purl.uniprot.org/core/volume"167"xsd:string
http://purl.uniprot.org/citations/9785454http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9785454
http://purl.uniprot.org/citations/9785454http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9785454
http://purl.uniprot.org/citations/9785454http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9785454
http://purl.uniprot.org/citations/9785454http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9785454