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MetaCyc Pathway: ceramide degradation
Inferred from experiment

Enzyme View:

Pathway diagram: ceramide degradation

This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Superclasses: Degradation/Utilization/AssimilationFatty Acid and Lipids Degradation

Some taxa known to possess this pathway include : Arabidopsis thaliana col, Oryza sativa Japonica Group cultivar Nipponbare

Expected Taxonomic Range: Opisthokonta, Viridiplantae

General Background

Sphingolipids are ubiquitous cell components present in eukaryotes and bacteria. A sphingolipid molecule is typically composed of a long-chain base (LCB, also known as sphingoid base), an amide linked fatty acyl chain, and a polar head. Ceramides (without a polar head group), glycosylceramides, and glycosylinositolphosphoceramides (GIPCs) are the predominant plant sphingolipids. Sphingomyelin, with phosphocholine as the polar head group, is the major sphingolipid in animals. Yeast contains predominantly inositolphosphoceramides (reviewed in [Lynch04, Pata10].

Some physiological roles of sphingolipids have been determined. Ceramides have been well known as inducers of programmed cell death in animal cells, and the same role was evidenced in plants (reviewed in [Pata10]). In plants, GIPCs are involved in maintaining Golgi and ER integrity, in symbiosis, and function as GPI anchors for proteins (reviewed in [Pata10]). Glycosylsphingolipids play roles in increasing plasma membrane stability, reducing ion permeability and pathogenesis. They were also implicated in chilling and freezing tolerance, as well as drought tolerance in plants (reviewed in [Pata10]). Free LCBs (sphingoids) and phosphorylated LCBs (LCB-Ps, sphingoid 1-phosphates) were implicated as mediators of cellular responses. Like ceramides, LCBs were shown to promote programmed cell death in mammalian and plant cells. LCB-Ps were shown to be signaling intermediates in various cellular responses such as proliferation, differentiation, and cytoskeleton organization (reviewed in [Pata10]).

About This Pathway

Ceramides are degraded by ceramidases. Ceramidases hydrolyze the N-acyl linkage between the long chain bases and the fatty acyl moieties. Ceramidases have been well characterized from human, yeast and a number of other organisms. The only characterized plant ceramidase is a rice ceramidase which however did not act with any of the predominant plant ceramides in vitro [Pata08]. Expressing the rice ceramidase in a yeast mutant increased the yeast endogenous phytoceramide level, which indicated a reverse ceramidase activity of the rice enzyme. The in planta role of this plant ceramidase is unclear. Free long chain bases liberated from ceramides are further degraded into corresponding aldehydes and a phosphorylethanolamine via the intermediate long chain base 1-phosphates.

Created 09-Apr-2010 by Zhang P, TAIR


Lynch04: Lynch, Daniel V, Dunn, Teresa M (2004). "An introduction to plant sphingolipids and areview of recent advances in understanding their metabolism and function." New Phytologist, 161:677-702.

Pata08: Pata MO, Wu BX, Bielawski J, Xiong TC, Hannun YA, Ng CK (2008). "Molecular cloning and characterization of OsCDase, a ceramidase enzyme from rice." Plant J 55(6);1000-9. PMID: 18547394

Pata10: Pata MO, Hannun YA, Ng CK (2010). "Plant sphingolipids: decoding the enigma of the Sphinx." New Phytol 185(3);611-30. PMID: 20028469

Tsegaye07: Tsegaye Y, Richardson CG, Bravo JE, Mulcahy BJ, Lynch DV, Markham JE, Jaworski JG, Chen M, Cahoon EB, Dunn TM (2007). "Arabidopsis mutants lacking long chain base phosphate lyase are fumonisin-sensitive and accumulate trihydroxy-18:1 long chain base phosphate." J Biol Chem 282(38);28195-206. PMID: 17635905

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Worrall08: Worrall D, Liang YK, Alvarez S, Holroyd GH, Spiegel S, Panagopulos M, Gray JE, Hetherington AM (2008). "Involvement of sphingosine kinase in plant cell signalling." Plant J 56(1);64-72. PMID: 18557834

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Wed May 4, 2016, biocyc13.