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

Ashley E Beattie; David J Clarke; John M Wadsworth; Jonathan Lowther; Ho-Lam Sin; Dominic J Campopiano

doi:10.1039/c3cc43001d

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

Ashley E Beattie, David J Clarke, John M Wadsworth, Jonathan Lowther, Ho-Lam Sin, Dominic J Campopiano

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	7058-60
Number of pages	3
Journal	Chemical Communications
Volume	49
Issue number	63
Early online date	24 Jun 2013
DOIs	https://doi.org/10.1039/c3cc43001d
Publication status	Published - 14 Aug 2013

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

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.",

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publisher = "Royal Society of Chemistry",

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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. / Beattie, Ashley E; Clarke, David J; Wadsworth, John M et al.
In: Chemical Communications, Vol. 49, No. 63, 14.08.2013, p. 7058-60.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Reconstitution of the pyridoxal 5'-phosphate (PLP) dependent enzyme serine palmitoyltransferase (SPT) with pyridoxal reveals a crucial role for the phosphate during catalysis

AU - Beattie, Ashley E

AU - Clarke, David J

AU - Wadsworth, John M

AU - Lowther, Jonathan

AU - Sin, Ho-Lam

AU - Campopiano, Dominic J

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AB - 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.

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DO - 10.1039/c3cc43001d

M3 - Article

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SN - 1359-7345

VL - 49

SP - 7058

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JO - Chemical Communications

JF - Chemical Communications

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ER -

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

Abstract

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