Reconstitution of the pyridoxal 5'-phosphate (PLP) dependent enzyme serine palmitoyltransferase (SPT) with pyridoxal reveals a crucial role for the phosphate during catalysis

The pyridoxal 5'-phosphate (PLP)-dependent enzyme serine palmitoyltransferase (SPT) is required for de novo sphingolipid biosynthesis. A previous study revealed a novel and unexpected interaction between the hydroxyl group of the l-serine substrate and the 5'-phosphate group of PLP. By usi...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2013-08, Vol.49 (63), p.7058-7060
Hauptverfasser: Beattie, Ashley E, Clarke, David J, Wadsworth, John M, Lowther, Jonathan, Sin, Ho-Lam, Campopiano, Dominic J
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Sprache:eng
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Zusammenfassung:The pyridoxal 5'-phosphate (PLP)-dependent enzyme serine palmitoyltransferase (SPT) is required for de novo sphingolipid biosynthesis. A previous study revealed a novel and unexpected interaction between the hydroxyl group of the l-serine substrate and the 5'-phosphate group of PLP. By using pyridoxal (PL), the dephosphorylated analogue of vitamin B6, we show here that this interaction is important for substrate specificity and optimal catalytic efficiency.
ISSN:1359-7345
1364-548X
DOI:10.1039/c3cc43001d