| http://purl.uniprot.org/citations/9675028 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9675028 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9675028 | http://www.w3.org/2000/01/rdf-schema#comment | "Recombinant human neutrophil leukotriene B4 (LTB4) omega-hydroxylase (cytochrome P450 4F3) has been purified to a specific content of 14. 8 nmol of P450/mg of protein from yeast cells. The purified enzyme was homogenous as judged from the SDS-PAGE, with an apparent molecular weight of 55 kDa. The enzyme catalyzed the omega-hydroxylation of LTB4 with a Km of 0.64 microM and Vmax of 34 nmol/min/nmol of P450 in the presence of rabbit hepatic NADPH-P450 reductase and cytochrome b5. Furthermore, various eicosanoids such as 20-hydroxy-LTB4, 6-trans-LTB4, lipoxin A4, lipoxin B4, 5-HETE and 12-HETE, and 12-hydroxy-stearate and 12-hydroxy-oleate were efficiently omega-hydroxylated, although their Km values were much higher than that of LTB4. In contrast, no activity was detected toward laurate, palmitate, arachidonate, 15-HETE, prostaglandin A1, and prostaglandin E1, all of which are excellent substrates for the CYP4A fatty acid omega-hydroxylases. This is the first time human neutrophil LTB4 omega-hydroxylase has been isolated in a highly purified state and characterized especially with respect to its substrate specificity."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.org/dc/terms/identifier | "doi:10.1006/abbi.1998.0724"xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.org/dc/terms/identifier | "doi:10.1006/abbi.1998.0724"xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/author | "Kikuta Y."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/author | "Kikuta Y."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/author | "Mizukami Y."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/author | "Mizukami Y."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/author | "Takeshige K."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/author | "Takeshige K."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/author | "Yabusaki Y."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/author | "Yabusaki Y."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/author | "Sakaki T."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/author | "Sakaki T."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/author | "Sumimoto H."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/author | "Sumimoto H."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/author | "Kusunose E."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/author | "Kusunose E."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/author | "Kusunose M."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/author | "Kusunose M."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/date | "1998"xsd:gYear |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/name | "Arch. Biochem. Biophys."xsd:string |
| http://purl.uniprot.org/citations/9675028 | http://purl.uniprot.org/core/name | "Arch. Biochem. Biophys."xsd:string |