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Serine palmitoyltransferase small subunit B is a protein-coding component of the SPT heterotrimer, which regulates the initial and rate-limiting step of sphingolipid biosynthesis by condensing L-serine and a fatty acyl-CoA to generate long-chain bases, the backbone of sphingolipids. The SPT complex is composed of larger catalytic subunits (SPTLC1 and SPTLC2 or SPTLC3) and a small regulatory subunit, either SPTSSA or SPTSSB. SPTSSB increases the catalytic activity and acyl-CoA chain-length preference of SPT, influencing the composition of sphingolipids and thus membrane structure and cellular signaling. Mutations affecting SPTSSB or its regulation are implicated in hereditary neuropathies and neurodegenerative disease due to aberrant sphingolipid production and axonal degeneration.
Most potential drugs would act as enzyme inhibitors of SPT; modulation would alter sphingolipid production, affecting cell signaling and membrane properties
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