| http://purl.uniprot.org/citations/10542053 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10542053 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10542053 | http://www.w3.org/2000/01/rdf-schema#comment | "The lipoxygenases (LOs) are a family of nonheme iron dioxygenases that catalyse the insertion of molecular oxygen into polyunsaturated fatty acids. Five members of this gene family have been described in man, 5-LO, 12S-LO, 12R-LO, 15-LO and 15S-LO. Using partially purified recombinant 15S-LO enzyme and cells constitutively expressing this protein, we have compared the activity, substrate specificity, kinetic characteristics and regulation of this enzyme to that previously reported for 15-LO. 15S-LO has a threefold higher Km, similar Vmax and increased specificity of oxygenation for arachidonic acid, and a similar Km but decreased Vmax for linoleic acid in comparison to 15-LO. Unlike 15-LO, 15S-LO is not suicide inactivated by the products of fatty acid oxygenation. However, in common with other LOs, 15S-LO activity is regulated through calcium-dependent association of the enzyme with the membrane fraction of cells. In addition, whilst independently cloning the recently described 15S-LO, we identified a splice variant containing an in-frame 87-bp deletion corresponding to amino acids 401-429 inclusive. Modelling of the 15S-LO and subsequent studies with partially purified recombinant protein suggest that the deleted region comprises a complete alpha-helix flanking the active site of the enzyme resulting in decreased specificity of oxygenation and affinity for fatty acid substrates. Alternative splicing of 15S-LO would therefore provide a further level of regulation of fatty acid metabolism. These results demonstrate that there are substantial differences in the enzyme characteristics and regulation of the 15-LO isozymes which may reflect differing roles for the proteins in vivo."xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://purl.org/dc/terms/identifier | "doi:10.1046/j.1432-1327.1999.00818.x"xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://purl.org/dc/terms/identifier | "doi:10.1046/j.1432-1327.1999.00818.x"xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://purl.uniprot.org/core/author | "Vickers P.J."xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://purl.uniprot.org/core/author | "Vickers P.J."xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://purl.uniprot.org/core/author | "Kilty I."xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://purl.uniprot.org/core/author | "Kilty I."xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://purl.uniprot.org/core/author | "Logan A."xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://purl.uniprot.org/core/author | "Logan A."xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10542053 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10542053 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://purl.uniprot.org/core/pages | "83-93"xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://purl.uniprot.org/core/pages | "83-93"xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://purl.uniprot.org/core/title | "Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase."xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://purl.uniprot.org/core/title | "Differential characteristics of human 15-lipoxygenase isozymes and a novel splice variant of 15S-lipoxygenase."xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://purl.uniprot.org/core/volume | "266"xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://purl.uniprot.org/core/volume | "266"xsd:string |
| http://purl.uniprot.org/citations/10542053 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10542053 |
| http://purl.uniprot.org/citations/10542053 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10542053 |
| http://purl.uniprot.org/citations/10542053 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10542053 |
| http://purl.uniprot.org/citations/10542053 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10542053 |