Ether lipid biosynthesis

• Verfasst von: Thai, Thanh-Phuong [VerfasserIn]
• Verfasst von: Heid, Hans [VerfasserIn]
• Verfasst von: Rackwitz, Hans-Richard [VerfasserIn]
• Verfasst von: Hunziker, Andreas [VerfasserIn]
• Verfasst von: Gorgas, Karin [VerfasserIn]
• Verfasst von: Just, Wilhelm W. [VerfasserIn]
• Titel: Ether lipid biosynthesis
• Titelzusatz: isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase
• Verf.angabe: Thanh-Phuong Thai, Hans Heid, Hans-Richard Rackwitz, Andreas Hunziker, Karin Gorgas, Wilhelm W Just
• E-Jahr: 1997
• Jahr: December 29, 1997
• Umfang: 7 S.
• Fussnoten: Gesehen am 22.04.2025
• Titel Quelle: Enthalten in: Vereinigung der Europäischen Biochemischen GesellschaftenFEBS letters
• Ort Quelle: Chichester : Wiley, 1968
• Jahr Quelle: 1997
• Band/Heft Quelle: 420(1997), 2-3, Seite 205-211
• ISSN Quelle: 1873-3468
• DOI: doi:10.1016/S0014-5793(97)01495-6
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: Alkyldihydroxyacetonephosphate synthase
• Sach-SW: Dihydroxyacetonephosphate acyltransferase
• Sach-SW: Ether lipid biosynthesis
• Sach-SW: Plasmalogen
• K10plus-PPN: 1923359495

Abstract

In this paper we describe isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase (DAP-AT). The enzyme was extracted from rabbit Harderian gland peroxisomes and isolated as a trimeric complex by sucrose density gradient centrifugation. From peptide sequences matching EST-clones were obtained which allowed cloning and sequencing of the cDNA from a human cDNA library. The nucleotide-derived amino acid sequence revealed a protein consisting of 680 amino acid residues of molecular mass 77 187 containing a C-terminal type 1 peroxisomal targeting signal. Monospecific antibodies raised against this polypeptide efficiently immunoprecipitated DAP-AT activity from solubilized peroxisomal preparations, thus demonstrating that the cloned cDNA codes for DAP-AT.