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Serine palmitoyltransferase, long chain base subunit 1, also known as SPTLC1, is a protein which in humans is encoded by the SPTLC1gene.[1][2]
Serine palmitoyltransferase, which consists of two different subunits, is the initial enzyme in sphingolipid biosynthesis. It converts L-serine and palmitoyl CoA to 3-oxosphinganine with pyridoxal 5'-phosphate as a cofactor. The product of this gene is the long chain base subunit 1 of serine palmitoyltransferase. Mutations in this gene were identified in patients with hereditary sensory neuropathy type 1. Alternatively spliced variants encoding different isoforms have been identified.[1]
↑Weiss B, Stoffel W (October 1997). "Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis". Eur. J. Biochem. 249 (1): 239–47. doi:10.1111/j.1432-1033.1997.00239.x. PMID9363775.
Further reading
Weiss B, Stoffel W (1997). "Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis". Eur. J. Biochem. 249 (1): 239–47. doi:10.1111/j.1432-1033.1997.00239.x. PMID9363775.
Gable K, Slife H, Bacikova D, et al. (2000). "Tsc3p is an 80-amino acid protein associated with serine palmitoyltransferase and required for optimal enzyme activity". J. Biol. Chem. 275 (11): 7597–603. doi:10.1074/jbc.275.11.7597. PMID10713067.
Hanada K, Hara T, Nishijima M (2000). "Purification of the serine palmitoyltransferase complex responsible for sphingoid base synthesis by using affinity peptide chromatography techniques". J. Biol. Chem. 275 (12): 8409–15. doi:10.1074/jbc.275.12.8409. PMID10722674.
Perry DK, Carton J, Shah AK, et al. (2000). "Serine palmitoyltransferase regulates de novo ceramide generation during etoposide-induced apoptosis". J. Biol. Chem. 275 (12): 9078–84. doi:10.1074/jbc.275.12.9078. PMID10722759.
Bejaoui K, Wu C, Scheffler MD, et al. (2001). "SPTLC1 is mutated in hereditary sensory neuropathy, type 1". Nat. Genet. 27 (3): 261–2. doi:10.1038/85817. PMID11242106.
Dawkins JL, Hulme DJ, Brahmbhatt SB, et al. (2001). "Mutations in SPTLC1, encoding serine palmitoyltransferase, long chain base subunit-1, cause hereditary sensory neuropathy type I.". Nat. Genet. 27 (3): 309–12. doi:10.1038/85879. PMID11242114.
Stachowitz S, Alessandrini F, Abeck D, et al. (2003). "Permeability barrier disruption increases the level of serine palmitoyltransferase in human epidermis". J. Invest. Dermatol. 119 (5): 1048–52. doi:10.1046/j.1523-1747.2002.19524.x. PMID12445191.
CAMPBELL AM, HOFFMAN HL (1996). "SENSORY RADICULAR NEUROPATHY ASSOCIATED WITH MUSCLE WASTING IN TWO CASES". Brain. 87: 67–74. doi:10.1093/brain/87.1.67. PMID14152213.
Verhoeven K, Coen K, De Vriendt E, et al. (2004). "SPTLC1 mutation in twin sisters with hereditary sensory neuropathy type I.". Neurology. 62 (6): 1001–2. doi:10.1212/01.wnl.0000115388.10828.5c. PMID15037712.
Dedov VN, Dedova IV, Nicholson GA (2006). "Hypoxia causes aggregation of serine palmitoyltransferase followed by non-apoptotic death of human lymphocytes". Cell Cycle. 3 (10): 1271–7. doi:10.4161/cc.3.10.1163. PMID15467453.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID16189514.
McCampbell A, Truong D, Broom DC, et al. (2006). "Mutant SPTLC1 dominantly inhibits serine palmitoyltransferase activity in vivo and confers an age-dependent neuropathy". Hum. Mol. Genet. 14 (22): 3507–21. doi:10.1093/hmg/ddi380. PMID16210380.