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Chemical Compound Review

Palmitoyl     hexadecanal

Synonyms: palmitaldehyde, N-hexadecanal, QSPL 064, AG-C-27198, CHEMBL1235338, ...
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Disease relevance of palmitaldehyde

  • Mutations in palmitoyl-protein thioesterase were recently found to cause the neurodegenerative disorder infantile neuronal ceroid lipofuscinosis, a disease characterized by accumulation of amorphous granular deposits in cortical neurons, leading to blindness, seizures, and brain death by the age of three [1].
  • We have further demonstrated that this palmitoyl-protein Delta-9 desaturase activity is deficient in cln3(-/-) mouse pancreas and is completely ablated in neuroblastoma cells by RNA inhibition [2].
  • INTERPRETATION: We propose that palmitoyl-protein desaturation defines a new mechanism of proteolipid modification, and that deficiency of this process leads to the signs and symptoms of Batten's disease [2].
  • Upon deacylation by PagL, E. coli lipid A underwent another modification, which was the result of the activity of the endogenous palmitoyl transferase PagP [3].
  • Bordetella bronchiseptica PagP is a Bvg-regulated lipid A palmitoyl transferase that is required for persistent colonization of the mouse respiratory tract [4].

High impact information on palmitaldehyde

  • This review focuses on the mechanisms underlying biogenesis of the mature Hh proteins, which are dually modified by cholesteryl and palmitoyl adducts, as well as on the relationship between Hh proteins and the self-splicing proteins (i.e., proteins containing inteins) and the Hh-like proteins of nematodes [5].
  • The studies reveal new roles for palmitoylated proteins as molecular switches and LRAT as a palmitoyl transferase whose role is to catalyze the mRPE65 to sRPE65 conversion [6].
  • The infantile form, INCL, is caused by lysosomal palmitoyl-protein thioesterase (PPT) deficiency, which impairs the cleavage of thioester linkages in palmitoylated proteins, preventing their hydrolysis by lysosomal proteinases [7].
  • Palmitoylation on TMD 2 is upregulated by the palmitoyl acyl transferase GODZ and leads to an accumulation of the receptor in the Golgi and a reduction of receptor surface expression [8].
  • These findings define HIP14 as a mammalian palmitoyl transferase involved in the palmitoylation and trafficking of multiple neuronal proteins [9].

Chemical compound and disease context of palmitaldehyde


Biological context of palmitaldehyde

  • During fasting conditions, however, rates of FFA uptake across the leg were negatively correlated with visceral adiposity as were activities of muscle carnitine palmitoyl transferase and citrate synthase [15].
  • Molecular genetics of palmitoyl-protein thioesterase deficiency in the U.S [16].
  • Transfection of human embryonic kidney 293 cells with the complementary DNA (cDNA) for eNOS and 23 cDNA clones encoding the Asp-His-His-Cys motif (DHHC) palmitoyl transferase family members showed that five clones (2, 3, 7, 8, and 21) enhanced incorporation of [3H]-palmitate into eNOS [17].
  • The ras oncogene products require membrane localization for their function, and this is thought to be accomplished by the addition of a palmitoyl group to a cysteine residue near the carboxyl terminus of the nascent chain [18].
  • The acylation of alpha- and beta-chains appears to involve attachment of palmitoyl groups via an ester linkage sensitive to alkaline hydrolysis [19].

Anatomical context of palmitaldehyde

  • Mean total activity in SLS fibroblasts (n = 5) was 13% of that in normal fibroblasts, and palmitoyl CoA-inhibitable activity was 1% of normal [20].
  • RESULTS: DEAEH accumulated in mitochondria and inhibited carnitine palmitoyl transferase I and acyl-coenzyme A dehydrogenases; it decreased beta-oxidation and caused lipid deposits in hepatocytes [21].
  • Like most metazoan Ras proteins, yeast Ras is post-translationally modified by addition of a farnesyl and a palmitoyl moiety, and these modifications are required for targeting the protein to the cytoplasmic face of the plasma membrane and for biological activity of the protein [22].
  • Palmitoyl and decanoyl analogues of 1-phenyl-2-acylamino-3-morpholino-1-propanol inhibit the enzyme activity in infected erythrocytes [23].
  • These data support a role for palmitoyl-protein thioesterase in the lysosomal degradation of S-acylated proteins and define a major new pathway for the catabolism of acylated proteins in the lysosome [1].

Associations of palmitaldehyde with other chemical compounds

  • The enzymes that mediate palmitoyl acyl transfer to PSD-95 have not yet been identified; however, proteins containing a DHHC cysteine-rich domain mediate palmitoyl acyl transferase activity in yeast [24].
  • Incubation with synthetic LPC (palmitoyl), but not with synthetic phosphatidylcholine (dipalmitoyl), suppressed ET-1-LI secretion by the endothelial cells [25].
  • This effect requires the cholesterol but not palmitoyl modification on Hh, and expands the zone of full-length Ci expression [26].
  • Transient expression of a PPT2 cDNA led to the production of a glycosylated lysosomal protein with palmitoyl-CoA hydrolase activity comparable with palmitoyl-protein thioesterase [27].
  • We show that COS cells take up exogenously supplied palmitoyl-protein thioesterase intracellularly and that the cellular uptake is blocked by mannose 6-phosphate, a hallmark of lysosomal enzyme trafficking [28].

Gene context of palmitaldehyde

  • A conformational change may facilitate palmitoyl extrusion from BET3 and allow the fatty acid chain to engage in intermolecular hydrophobic interactions [29].
  • Two homologues of TIP1 in yeast (Saccharomyces cerevisiae) and human (Homo sapiens) have been shown to have S-acyl transferase (also known as palmitoyl transferase) activity [30].
  • The genes CLN1 and CLN2 encode lysosomal palmitoyl protein thioesterase and tripeptidyl peptidase 1 [31].
  • In the current study, we describe the cloning and expression of a second lysosomal thioesterase, palmitoyl-protein thioesterase 2 (PPT2), that shares an 18% identity with palmitoyl-protein thioesterase [27].
  • The Saccharomyces cerevisiae OLE1 gene encodes the delta-9 fatty acid desaturase, an enzyme which forms the monounsaturated palmitoleic (16:1) and oleic (18:1) fatty acids from palmitoyl (16:0) or stearoyl (18:0) CoA [32].

Analytical, diagnostic and therapeutic context of palmitaldehyde

  • Vaccination of Black C57, BALB/c, and NORBA mice with the synthetic Abeta(1-16) sequence modified by covalently attaching two palmitoyl residues at each end of the peptide, subsequently reconstituted in liposomes-Lipid A elicited titers of 1:5,000 of anti-Abeta(1-16) antibodies within 10 weeks after the first inoculation [33].
  • Furthermore, palmitoyl-protein thioesterase cosediments with lysosomal enzyme markers by Percoll density gradient centrifugation [28].
  • Analysis by fast atom bombardment mass spectrometry with negative ion monitoring and by the complementary technique of collision-induced dissociation revealed molecular and daughter ions that indicated a plasmanylinositol with a palmitoyl group on an inositol hydroxyl [34].
  • Molecular cloning and expression of palmitoyl-protein thioesterase 2 (PPT2), a homolog of lysosomal palmitoyl-protein thioesterase with a distinct substrate specificity [27].
  • Analysis of inhibition of palmitoylation by flow cytometry revealed that this fluorescent lipopeptide substrate represents a highly sensitive molecular probe of palmitoyl acyltransferase activity that enables unprecedented high-throughput assays of protein palmitoylation [35].


  1. Lipid thioesters derived from acylated proteins accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase. Lu, J.Y., Verkruyse, L.A., Hofmann, S.L. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  2. CLN3P, the Batten's disease protein, is a novel palmitoyl-protein Delta-9 desaturase. Narayan, S.B., Rakheja, D., Tan, L., Pastor, J.V., Bennett, M.J. Ann. Neurol. (2006) [Pubmed]
  3. Dissemination of lipid A deacylases (pagL) among gram-negative bacteria: identification of active-site histidine and serine residues. Geurtsen, J., Steeghs, L., Hove, J.T., van der Ley, P., Tommassen, J. J. Biol. Chem. (2005) [Pubmed]
  4. Bordetella bronchiseptica PagP is a Bvg-regulated lipid A palmitoyl transferase that is required for persistent colonization of the mouse respiratory tract. Preston, A., Maxim, E., Toland, E., Pishko, E.J., Harvill, E.T., Caroff, M., Maskell, D.J. Mol. Microbiol. (2003) [Pubmed]
  5. Novel lipid modifications of secreted protein signals. Mann, R.K., Beachy, P.A. Annu. Rev. Biochem. (2004) [Pubmed]
  6. A palmitoylation switch mechanism in the regulation of the visual cycle. Xue, L., Gollapalli, D.R., Maiti, P., Jahng, W.J., Rando, R.R. Cell (2004) [Pubmed]
  7. Lysosomal ceroid depletion by drugs: therapeutic implications for a hereditary neurodegenerative disease of childhood. Zhang, Z., Butler, J.D., Levin, S.W., Wisniewski, K.E., Brooks, S.S., Mukherjee, A.B. Nat. Med. (2001) [Pubmed]
  8. Differential regulation of AMPA receptor subunit trafficking by palmitoylation of two distinct sites. Hayashi, T., Rumbaugh, G., Huganir, R.L. Neuron (2005) [Pubmed]
  9. Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins. Huang, K., Yanai, A., Kang, R., Arstikaitis, P., Singaraja, R.R., Metzler, M., Mullard, A., Haigh, B., Gauthier-Campbell, C., Gutekunst, C.A., Hayden, M.R., El-Husseini, A. Neuron (2004) [Pubmed]
  10. The crystal structure of palmitoyl protein thioesterase 1 and the molecular basis of infantile neuronal ceroid lipofuscinosis. Bellizzi, J.J., Widom, J., Kemp, C., Lu, J.Y., Das, A.K., Hofmann, S.L., Clardy, J. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  11. Biosynthesis of lipid A precursors in Escherichia coli. A membrane-bound enzyme that transfers a palmitoyl residue from a glycerophospholipid to lipid X. Brozek, K.A., Bulawa, C.E., Raetz, C.R. J. Biol. Chem. (1987) [Pubmed]
  12. Characterization of an ovarian cancer activating factor in ascites from ovarian cancer patients. Xu, Y., Gaudette, D.C., Boynton, J.D., Frankel, A., Fang, X.J., Sharma, A., Hurteau, J., Casey, G., Goodbody, A., Mellors, A. Clin. Cancer Res. (1995) [Pubmed]
  13. Potential anti-AIDS naphthalenesulfonic acid derivatives. Synthesis and inhibition of HIV-1 induced cytopathogenesis and HIV-1 and HIV-2 reverse transcriptase activities. Tan, G.T., Wickramasinghe, A., Verma, S., Singh, R., Hughes, S.H., Pezzuto, J.M., Baba, M., Mohan, P. J. Med. Chem. (1992) [Pubmed]
  14. A new spectrophotometric assay for citrate synthase and its use to assess the inhibitory effects of palmitoyl thioesters. Else, A.J., Barnes, S.J., Danson, M.J., Weitzman, P.D. Biochem. J. (1988) [Pubmed]
  15. Skeletal muscle utilization of free fatty acids in women with visceral obesity. Colberg, S.R., Simoneau, J.A., Thaete, F.L., Kelley, D.E. J. Clin. Invest. (1995) [Pubmed]
  16. Molecular genetics of palmitoyl-protein thioesterase deficiency in the U.S. Das, A.K., Becerra, C.H., Yi, W., Lu, J.Y., Siakotos, A.N., Wisniewski, K.E., Hofmann, S.L. J. Clin. Invest. (1998) [Pubmed]
  17. Identification of Golgi-localized acyl transferases that palmitoylate and regulate endothelial nitric oxide synthase. Fernández-Hernando, C., Fukata, M., Bernatchez, P.N., Fukata, Y., Lin, M.I., Bredt, D.S., Sessa, W.C. J. Cell Biol. (2006) [Pubmed]
  18. Posttranslational modification of the Ha-ras oncogene protein: evidence for a third class of protein carboxyl methyltransferases. Clarke, S., Vogel, J.P., Deschenes, R.J., Stock, J. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  19. Fatty acylation of murine Ia alpha, beta, and invariant chains. Simonis, S., Cullen, S.E. J. Immunol. (1986) [Pubmed]
  20. Sjögren-Larsson syndrome. Impaired fatty alcohol oxidation in cultured fibroblasts due to deficient fatty alcohol:nicotinamide adenine dinucleotide oxidoreductase activity. Rizzo, W.B., Dammann, A.L., Craft, D.A. J. Clin. Invest. (1988) [Pubmed]
  21. Steatohepatitis-inducing drugs cause mitochondrial dysfunction and lipid peroxidation in rat hepatocytes. Berson, A., De Beco, V., Lettéron, P., Robin, M.A., Moreau, C., El Kahwaji, J., Verthier, N., Feldmann, G., Fromenty, B., Pessayre, D. Gastroenterology (1998) [Pubmed]
  22. Ras membrane targeting is essential for glucose signaling but not for viability in yeast. Bhattacharya, S., Chen, L., Broach, J.R., Powers, S. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  23. Sphingolipid synthesis as a target for chemotherapy against malaria parasites. Lauer, S.A., Ghori, N., Haldar, K. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  24. Identification of PSD-95 palmitoylating enzymes. Fukata, M., Fukata, Y., Adesnik, H., Nicoll, R.A., Bredt, D.S. Neuron (2004) [Pubmed]
  25. Suppression of endothelin-1 secretion by lysophosphatidylcholine in oxidized low density lipoprotein in cultured vascular endothelial cells. Jougasaki, M., Kugiyama, K., Saito, Y., Nakao, K., Imura, H., Yasue, H. Circ. Res. (1992) [Pubmed]
  26. Splitting the Hedgehog signal: sex and patterning in Drosophila. Horabin, J.I. Development (2005) [Pubmed]
  27. Molecular cloning and expression of palmitoyl-protein thioesterase 2 (PPT2), a homolog of lysosomal palmitoyl-protein thioesterase with a distinct substrate specificity. Soyombo, A.A., Hofmann, S.L. J. Biol. Chem. (1997) [Pubmed]
  28. Lysosomal targeting of palmitoyl-protein thioesterase. Verkruyse, L.A., Hofmann, S.L. J. Biol. Chem. (1996) [Pubmed]
  29. Structure of palmitoylated BET3: insights into TRAPP complex assembly and membrane localization. Turnbull, A.P., Kümmel, D., Prinz, B., Holz, C., Schultchen, J., Lang, C., Niesen, F.H., Hofmann, K.P., Delbrück, H., Behlke, J., Müller, E.C., Jarosch, E., Sommer, T., Heinemann, U. EMBO J. (2005) [Pubmed]
  30. The TIP GROWTH DEFECTIVE1 S-acyl transferase regulates plant cell growth in Arabidopsis. Hemsley, P.A., Kemp, A.C., Grierson, C.S. Plant Cell (2005) [Pubmed]
  31. Current state of clinical and morphological features in human NCL. Goebel, H.H., Wisniewski, K.E. Brain Pathol. (2004) [Pubmed]
  32. Specificity of unsaturated fatty acid-regulated expression of the Saccharomyces cerevisiae OLE1 gene. McDonough, V.M., Stukey, J.E., Martin, C.E. J. Biol. Chem. (1992) [Pubmed]
  33. A liposome-based therapeutic vaccine against beta -amyloid plaques on the pancreas of transgenic NORBA mice. Nicolau, C., Greferath, R., Balaban, T.S., Lazarte, J.E., Hopkins, R.J. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  34. Structural characterization of the glycoinositol phospholipid membrane anchor of human erythrocyte acetylcholinesterase by fast atom bombardment mass spectrometry. Roberts, W.L., Santikarn, S., Reinhold, V.N., Rosenberry, T.L. J. Biol. Chem. (1988) [Pubmed]
  35. Sensitive and rapid analysis of protein palmitoylation with a synthetic cell-permeable mimic of SRC oncoproteins. Creaser, S.P., Peterson, B.R. J. Am. Chem. Soc. (2002) [Pubmed]
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