Enzymology of long-chain base synthesis by liver: characterization of serine palmitoyltransferase in rat liver microsomes - PubMed (original) (raw)
Enzymology of long-chain base synthesis by liver: characterization of serine palmitoyltransferase in rat liver microsomes
R D Williams et al. Arch Biochem Biophys. 1984 Jan.
Abstract
Serine palmitoyltransferase [palmitoyl-CoA:L-serine C-palmitoyltransferase (decarboxylating) EC 2.3.1.50] catalyzes the initial and committed step in the biosynthesis of the long-chain bases of sphingolipids. A simple assay, based upon the incorporation of [3H]serine into the chloroform-soluble product 3-ketosphinganine, has been developed and demonstrated to be valid for analyzing this enzyme in rat liver microsomes. More than 75% of the serine palmitoyltransferase of rat liver was associated with the microsomal subfraction. The dependencies of activity on the incubation time, pH, temperature, other assay components (e.g., dithiothreitol, EDTA, and pyridoxal 5'-phosphate), and the concentrations of microsomal protein, L-serine, and palmitoyl-CoA were investigated. The requirement of pyridoxal 5'-phosphate for activity was established by formation of the apoenzyme by dialysis against cysteine, and recovery of full activity upon reconstitution with the coenzyme. Activities with fatty acyl-CoA's of varying alkyl chain length were distributed nearly symmetrically around a maximum at 16 carbons (palmitoyl-CoA) for the fully saturated substrates. Less activity was obtained with the CoA thioesters of cis-unsaturated fatty acids, but trans-9-hexadecenoyl-CoA yielded essentially the same activity as palmitoyl-CoA. Hence, this enzyme is capable of initiating the synthesis of the major long-chain bases, as well as compounds that may constitute the unidentified bases reported in analyses of mammalian sphingolipids.
Similar articles
- Activities of serine palmitoyltransferase (3-ketosphinganine synthase) in microsomes from different rat tissues.
Merrill AH Jr, Nixon DW, Williams RD. Merrill AH Jr, et al. J Lipid Res. 1985 May;26(5):617-22. J Lipid Res. 1985. PMID: 4020300 - Utilization of different fatty acyl-CoA thioesters by serine palmitoyltransferase from rat brain.
Merrill AH Jr, Williams RD. Merrill AH Jr, et al. J Lipid Res. 1984 Feb;25(2):185-8. J Lipid Res. 1984. PMID: 6707526 - Regulation of de novo sphingolipid biosynthesis and the toxic consequences of its disruption.
Linn SC, Kim HS, Keane EM, Andras LM, Wang E, Merrill AH Jr. Linn SC, et al. Biochem Soc Trans. 2001 Nov;29(Pt 6):831-5. doi: 10.1042/0300-5127:0290831. Biochem Soc Trans. 2001. PMID: 11709083 Review. - Serine Palmitoyltransferase Subunit 3 and Metabolic Diseases.
Lone MA, Bourquin F, Hornemann T. Lone MA, et al. Adv Exp Med Biol. 2022;1372:47-56. doi: 10.1007/978-981-19-0394-6_4. Adv Exp Med Biol. 2022. PMID: 35503173 Review.
Cited by
- Nogo-A reduces ceramide de novo biosynthesis to protect from heart failure.
Sasset L, Manzo OL, Zhang Y, Marino A, Rubinelli L, Riemma MA, Chalasani MLS, Dasoveanu DC, Roviezzo F, Jankauskas SS, Santulli G, Bucci MR, Lu TT, Di Lorenzo A. Sasset L, et al. Cardiovasc Res. 2023 Mar 31;119(2):506-519. doi: 10.1093/cvr/cvac108. Cardiovasc Res. 2023. PMID: 35815623 Free PMC article. - Sphingolipids and Asthma.
Worgall TS. Worgall TS. Adv Exp Med Biol. 2022;1372:145-155. doi: 10.1007/978-981-19-0394-6_10. Adv Exp Med Biol. 2022. PMID: 35503179 - Palmitic acid causes increased dihydroceramide levels when desaturase expression is directly silenced or indirectly lowered by silencing AdipoR2.
Ruiz M, Henricsson M, Borén J, Pilon M. Ruiz M, et al. Lipids Health Dis. 2021 Nov 28;20(1):173. doi: 10.1186/s12944-021-01600-y. Lipids Health Dis. 2021. PMID: 34839823 Free PMC article. - Serine palmitoyltransferase assembles at ER-mitochondria contact sites.
Aaltonen MJ, Alecu I, König T, Bennett SA, Shoubridge EA. Aaltonen MJ, et al. Life Sci Alliance. 2021 Nov 16;5(2):e202101278. doi: 10.26508/lsa.202101278. Print 2022 Feb. Life Sci Alliance. 2021. PMID: 34785538 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources