The Pyridoxal 5′-Phosphate (PLP)-Dependent Enzyme Serine Palmitoyltransferase (SPT): Effects of the Small Subunits and Insights from Bacterial Mimics of Human hLCB2a HSAN1 Mutations

<table>High resolution structure of <i>Sp </i>SPT homodimer PLP-L-serine external aldimine showing the position of the three hLCB2a HSAN1 related mutations (PDB:2W8J). Each monomer is coloured (red and yellow). Sequence alignment of bacterial <i>Sp</i> SPT (Uniprot code: Q93UV0) with bacterial <i>Sw </i>SPT (Uniprot code: A5VD79) and human hLCB2a (Uniprot code: O15270). The key catalytic lysine residue (K265) involved in the formation of the internal aldimine is coloured red, and the HSAN1 mutant mimics (V246M, G268V, and G385F) are coloured cyan.</table>

BioMed Research International

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Figure 2: The Pyridoxal 5′-Phosphate (PLP)-Dependent Enzyme Serine Palmitoyltransferase (SPT): Effects of the Small Subunits and Insights from Bacterial Mimics of Human hLCB2a HSAN1 Mutations 

Figure 2 | The Pyridoxal 5′-Phosphate (PLP)-Dependent Enzyme Serine Palmitoyltransferase (SPT): Effects of the Small Subunits and Insights from Bacterial Mimics of Human hLCB2a HSAN1 Mutations 