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The serine palmitoyltransferase from Sphingomonas wittichii RW1: An interesting link to an unusual acyl carrier protein
Author(s) -
Raman Marine C. C.,
Johnson Kenneth A.,
Clarke David J.,
Naismith James H.,
Campopiano Dominic J.
Publication year - 2010
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21482
Subject(s) - sphingolipid , biochemistry , serine , acyl carrier protein , chemistry , biosynthesis , enzyme , stereochemistry
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 SPT 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 SPT and we isolated and characterised the apo‐ and holo‐forms of the ACP. Our studies suggest a link between fatty acid and sphingolipid metabolism. © 2010 Wiley Periodicals, Inc. Biopolymers 93: 811–822, 2010.