Journal
BIOPOLYMERS
Volume 93, Issue 9, Pages 811-822Publisher
WILEY
DOI: 10.1002/bip.21482
Keywords
sphingolipids; Sphingomonas; serine palmitoyltransferase; pyridoxal phosphate; acyl carrier protein
Categories
Funding
- BBSRC [BBS/B/14434]
- EPSRC [EP/C543289/1]
- EaStChem [BBS/B/14434, BBF0085031, BB/S/014450]
- Biotechnology and Biological Sciences Research Council [BBS/B/14434, BB/F008503/1] Funding Source: researchfish
- Medical Research Council [G0500367] Funding Source: researchfish
- BBSRC [BB/F008503/1] Funding Source: UKRI
- MRC [G0500367] Funding Source: UKRI
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Serine palmitoyltransferase (SPT) catalyses the first step in the de novo biosynthesis of sphingolipids (SLs). It uses a decarboxylative Claisen-like condensation reaction to couple L-serine with palmitoyl-CoA to generate a long-chain base product, 3-ketodihydrosphingosine. SLs are produced by mammals, plants, yeast, and some bacteria, and we have exploited the complete genome sequence of Sphingomonas wittichii to begin a complete analysis of bacterial sphingolipid biosynthesis. Here, we describe the enzymatic characterization of the SPY from this organism and present its high-resolution x-ray structure. Moreover, we identified an open reading frame with high sequence homology to acyl carrier proteins (ACPs) that are common to fatty acid biosynthetic pathways. This small protein was co-expressed with the SPY and we isolated and characterised the apo- and bob-forms of the ACP. Our studies suggest a link between fatty acid and sphingolipid metabolism. (C) 2010. Wiley Periodicals, Inc. Biopolymers 93: 811-822, 2010.
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