2000
DOI: 10.1046/j.1432-1327.2000.01414.x
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Novel processive and nonprocessive glycosyltransferases from Staphylococcus aureus and Arabidopsis thaliana synthesize glycoglycerolipids, glycophospholipids, glycosphingolipids and glycosylsterols

Abstract: A processive diacylglycerol glucosyltransferase has recently been identified from Bacillus subtilis [Jorasch, P., Wolter, F.P., Za Èhringer, U., and Heinz, E. (1998) Mol. Microbiol. 29, 419±430]. Now we report the cloning and characterization of two other genes coding for diacylglycerol glycosyltransferases from Staphylococcus aureus and Arabidopsis thaliana; only the S. aureus enzyme shows processivity similar to the B. subtilis enzyme. Both glycosyltransferases characterized in this work show unexpected acce… Show more

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Cited by 78 publications
(55 citation statements)
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“…4 shows that the human GCS expressed in P. pastoris synthesized an additional glycolipid, which was identified as 1,2-diacyl-3-[O-␤-D-glucopyranosyl]-sn-glycerol, also known from our previous study on diacylglycerol glucosyltransferases (31). The formation of this new glycolipid as a consequence of GCS expression may be ascribed to the structural similarity of 1,2-diacyl-sn-glycerol and ceramide as discussed before (31). It results in the use of both acceptors by diacylglycerol and ceramide glycosyltransferases, which normally prefer only one of the two substrates.…”
Section: Expression Of Glucosylceramide Synthases In P Pastoris Resumentioning
confidence: 77%
See 1 more Smart Citation
“…4 shows that the human GCS expressed in P. pastoris synthesized an additional glycolipid, which was identified as 1,2-diacyl-3-[O-␤-D-glucopyranosyl]-sn-glycerol, also known from our previous study on diacylglycerol glucosyltransferases (31). The formation of this new glycolipid as a consequence of GCS expression may be ascribed to the structural similarity of 1,2-diacyl-sn-glycerol and ceramide as discussed before (31). It results in the use of both acceptors by diacylglycerol and ceramide glycosyltransferases, which normally prefer only one of the two substrates.…”
Section: Expression Of Glucosylceramide Synthases In P Pastoris Resumentioning
confidence: 77%
“…Fatty acid and sugar analysis by gas-liquid chromatography/mass spectrometry was performed as described previously (31). Peracetylated derivatives of GlcCer and glycosyldiacylglycerols were analyzed by mass spectrometry on an HP 5989A instrument (Hewlett-Packard) using the direct insertion probe mode and heating the sample by a temperature gradient starting from 80°C (3 min) 3 325°C at 30°/min.…”
Section: Combined Gas-liquid Chromatography/mass Spectrometry Analysismentioning
confidence: 99%
“…1). For this purpose, glycosyltransferases were selected from bacterial origin that had previously been characterized by heterologous expression in prokaryotic or eukaryotic hosts (Escherichia coli, Pichia pastoris, Saccharomyces cerevisiae, and Synechococcus) and subsequent analysis of newly formed glycolipids (20)(21)(22)(23)(24)(25)(26). Additional putative glycosyltransferases were identified in bacteria based on sequence similarity to known genes (Table 1) (26), and by this 20 bacterial genes were selected for expression in plants.…”
Section: Resultsmentioning
confidence: 99%
“…The best studied glycosyltransferases include the MGD/MGlcD and DGD synthases from plants and cyanobacteria (15)(16)(17)(18), the MGlcD and DGlcD synthases from Acholeplasma (7,19), and the processive glycosyltransferases from the Gram-positive bacteria Staphylococcus or Bacillus (20,21). There are only a few glycosyltransferases characterized as promiscuous enzymes, such as Pgt from Agrobacterium or Mesorhizobium, or the processive glycosyltransferases from the human pathogens Mycoplasma pneumoniae and Mycoplasma genitalum using UDP-Glc and UDP-galactose (UDP-Gal) as sugar donors (11,22,23).…”
Section: Discussionmentioning
confidence: 99%