2007
DOI: 10.1128/jb.00194-07
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Molecular Characterization of Membrane-Associated Soluble Serine Palmitoyltransferases from Sphingobacterium multivorum and Bdellovibrio stolpii

Abstract: ). This enzyme is suitable for the detailed mechanistic studies of SPT, although single crystals appropriate for high-resolution crystallography have not yet been obtained. We have now isolated three novel SPT genes from Sphingobacterium multivorum, Sphingobacterium spiritivorum, and Bdellovibrio stolpii, respectively. Each gene product exhibits an ϳ30% sequence identity to both eukaryotic subunits, and the putative catalytic amino acid residues are conserved. All bacterial SPTs were successfully overproduced … Show more

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Cited by 32 publications
(44 citation statements)
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“…(267,268) These have supported the general mechanism shown in Figure 5. As for many PLP-dependent enzymes,(269) the amino acid substrate is covalently bound to PLP as a Schiff base 24 (which is often referred to as the “external aldimine” versus the “internal aldimine” that is produced by the enzyme-Lys-PLP Schiff base).…”
Section: Sphingolipid Metabolic Pathwayssupporting
confidence: 77%
“…(267,268) These have supported the general mechanism shown in Figure 5. As for many PLP-dependent enzymes,(269) the amino acid substrate is covalently bound to PLP as a Schiff base 24 (which is often referred to as the “external aldimine” versus the “internal aldimine” that is produced by the enzyme-Lys-PLP Schiff base).…”
Section: Sphingolipid Metabolic Pathwayssupporting
confidence: 77%
“…gov]. In addition, SPT orthologs have been reported in several other sphingolipid-producing bacteria (19,20) and are well conserved in Bacteroides and related species (Table S1). In the following steps, 3-ketosphinganine is converted to sphinganine by 3-ketosphinganine reductase, and sphinganine is further transformed to dihydroceramide by ceramide synthase.…”
Section: Resultsmentioning
confidence: 99%
“…The hits against the Sphingobacteriales are particularly intriguing as members of this order are characterized by the presence of cellular lipid components that are comprised of high concentrations of sphingophospholipids [79]. The rate limiting step in sphingolipid biosynthesis in S. multivorum is serine palmitoyltransferase (SPT) [80], as in the E. huxleyi —virus system [81]. Although the EhV SPT is more similar to the host gene (as indicated above), the closest crystal structure in the PDB database to the EhV SPT is Sphingobacterium multivorum [67].…”
Section: Resultsmentioning
confidence: 99%