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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

Author:
Ashley E. Beattie, David J. Clarke, John M. Wadsworth, Jonathan Lowther, Ho-Lam Sin, Dominic J. Campopiano
Source:
Chemical communications 2013 v.49 no.63 pp. 7058-7060
ISSN:
1364-548X
Subject:
biosynthesis, catalytic activity, chemical communication, chemical reactions, moieties, phosphates, pyridoxal, pyridoxal phosphate, pyridoxine, serine, serine C-palmitoyltransferase, sphingolipids, substrate specificity
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.
Agid:
6598837