Serine palmitoyltransferase (SPT) catalyzes the first unique reaction of de novo sphingolipid biosynthesis. It is a member of the γ-oxoamine synthase family that utilizes pyridoxal 5′-phosphate as a co-factor. Many factors - such as cytokines, irradiation and stress - alter SPT activity, and in some cases mRNA, and increased ceramide production has been proposed to modulate diverse cell behaviours, including programmed cell death. Normal SPT function is critical because missense mutations in the human SPTLC1 gene cause hereditary sensory neuropathy type I, and complete knockout of SPT is embryonic lethal; however, the SPT inhibitor myriocin has been found to decrease atherosclerotic lesions in apo-E deficient mice. SPT is clearly involved in critical cell functions and disease, and much remains to be learned about its regulation. © Springer-Verlag Tokyo 2006. All rights reserved.
CITATION STYLE
Wei, J., Yerokun, T., Liepelt, M., Momin, A., Wang, E., Hanada, K., & Merrill, A. H. (2006). Serine palmitoyltransferase. In Sphingolipid Biology (pp. 25–47). Springer Japan. https://doi.org/10.1007/4-431-34200-1_2
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