| Structural highlights
Function
LCB1_YEAST Component of serine palmitoyltransferase (SPT), which catalyzes the committed step in the synthesis of sphingolipids, the condensation of serine with palmitoyl CoA to form the long chain base 3-ketosphinganine.[1] [2] LCB1_ARATH Serine palmitoyltransferase (SPT). The heterodimer formed with LCB2 constitutes the catalytic core. Involved in the regulation of the programmed cell death (PCD) signaling pathway. Plays an important role during male gametogenesis and embryogenesis.[3] [4] [5]
References
- ↑ Gable K, Han G, Monaghan E, Bacikova D, Natarajan M, Williams R, Dunn TM. Mutations in the yeast LCB1 and LCB2 genes, including those corresponding to the hereditary sensory neuropathy type I mutations, dominantly inactivate serine palmitoyltransferase. J Biol Chem. 2002 Mar 22;277(12):10194-200. PMID:11781309 doi:10.1074/jbc.M107873200
- ↑ Nagiec MM, Baltisberger JA, Wells GB, Lester RL, Dickson RC. The LCB2 gene of Saccharomyces and the related LCB1 gene encode subunits of serine palmitoyltransferase, the initial enzyme in sphingolipid synthesis. Proc Natl Acad Sci U S A. 1994 Aug 16;91(17):7899-902. PMID:8058731 doi:10.1073/pnas.91.17.7899
- ↑ Chen M, Han G, Dietrich CR, Dunn TM, Cahoon EB. The essential nature of sphingolipids in plants as revealed by the functional identification and characterization of the Arabidopsis LCB1 subunit of serine palmitoyltransferase. Plant Cell. 2006 Dec;18(12):3576-93. PMID:17194770 doi:10.1105/tpc.105.040774
- ↑ Shi L, Bielawski J, Mu J, Dong H, Teng C, Zhang J, Yang X, Tomishige N, Hanada K, Hannun YA, Zuo J. Involvement of sphingoid bases in mediating reactive oxygen intermediate production and programmed cell death in Arabidopsis. Cell Res. 2007 Dec;17(12):1030-40. PMID:18059378 doi:10.1038/cr.2007.100
- ↑ Teng C, Dong H, Shi L, Deng Y, Mu J, Zhang J, Yang X, Zuo J. Serine palmitoyltransferase, a key enzyme for de novo synthesis of sphingolipids, is essential for male gametophyte development in Arabidopsis. Plant Physiol. 2008 Mar;146(3):1322-32. PMID:18218968 doi:10.1104/pp.107.113506
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