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http://purl.uniprot.org/SHA-384/85F978DF728E9772148A03284F3527F6CAA016B6826AA60BE30E18D2B615A7A3BDC85F6E682072E40F11E8F3605F7AB2http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/85F978DF728E9772148A03284F3527F6CAA016B6826AA60BE30E18D2B615A7A3BDC85F6E682072E40F11E8F3605F7AB2http://www.w3.org/2000/01/rdf-schema#comment"Protein/gene_name: Cytochrome P450;CYP124A1. Function: Oxidizes cholesterol derivatives or methyl branched lipids at the omega terminus of the cholesterol, phytanic acid, farnesol and farnesyl acetate. Comments: Sulphate binding site His-101, Asp-102, Gln-103. Phytanic acid Kd = 0.1 uM. X-Ray crystallography structure: Fersnasol bound (PDB ID- 8FKB, 1.42 A) T271E (Threonine at 271 was mutated to Glutamic acid), The mutant was able to metabolize farnesol substrate generating low levels of terminal alcohol metabolite, whereas WT enzyme could not."xsd:string
http://purl.uniprot.org/uniprot/#_FE31FCA569F69585CBAEDA149F8BD85ABCE02E3F9E8BDDBFC28C37A04C2FAAB741F2F0F1B7CEE36E7584FF7637BEB385http://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/85F978DF728E9772148A03284F3527F6CAA016B6826AA60BE30E18D2B615A7A3BDC85F6E682072E40F11E8F3605F7AB2
http://purl.uniprot.org/uniprot/B2HHT9http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/85F978DF728E9772148A03284F3527F6CAA016B6826AA60BE30E18D2B615A7A3BDC85F6E682072E40F11E8F3605F7AB2
http://purl.uniprot.org/uniprot/#_B2HHT9-mappedCitation-36842492http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/85F978DF728E9772148A03284F3527F6CAA016B6826AA60BE30E18D2B615A7A3BDC85F6E682072E40F11E8F3605F7AB2