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Issue 63, 2013
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Reconstitution of the pyridoxal 5′-phosphate (PLP) dependent enzyme serine palmitoyltransferase (SPT) with pyridoxal reveals a crucial role for the phosphate during catalysis

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Abstract

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.

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

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Publication details

The article was received on 23 Apr 2013, accepted on 24 Jun 2013 and first published on 24 Jun 2013


Article type: Communication
DOI: 10.1039/C3CC43001D
Chem. Commun., 2013,49, 7058-7060

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

    A. E. Beattie, D. J. Clarke, J. M. Wadsworth, J. Lowther, H. Sin and D. J. Campopiano, Chem. Commun., 2013, 49, 7058
    DOI: 10.1039/C3CC43001D

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