title: Identification and Characterization of Heptaprenylglyceryl Phosphate Processing Enzymes in Bacillus subtilis.
abstract: In Archaea, ether lipids play an essential role as the main building blocks of the cellular membrane. Recently, ether lipids have also been discovered in the domain of Bacteria, and the key enzymes that catalyze their synthesis, glycerol-1-phosphate dehydrogenase and heptaprenylglyceryl phosphate synthase, have been described. In Bacillales, heptaprenylglyceryl phosphate does not become linked to a second polyprenyl moiety like ether lipids in Archaea but is dephosphorylated and acetylated. Here, we report on the enzymes that catalyze these reactions. We enriched the phosphatase activity from a B. subtilis cell extract and suppose that dephosphorylation is catalyzed by the phosphatase PhoB or by any other phosphatase in an unspecific manner. By screening a B. subtilis knock-out library for deficiency in acetylation, the yvoF gene product was identified to be the acetyltransferase. The acetyl-CoA-dependent enzyme YvoF is a close relative of maltose O-acetyltransferase (MAT). Its catalytic properties were analyzed and compared with MAT. YvoF and MAT partially overlap in substrate and product range in vitro, but MAT is not able to complement the yvoF knock-out in vivo.
authors.affiliation: From the Institute of Biophysics and Physical Biochemistry, University of Regensburg, 93040 Regensburg, Germany.
authors.forename: Mona
authors.initials: M
authors.lastname: Linde
authors.affiliation: From the Institute of Biophysics and Physical Biochemistry, University of Regensburg, 93040 Regensburg, Germany.
authors.forename: David
authors.initials: D
authors.lastname: Peterhoff
authors.affiliation: From the Institute of Biophysics and Physical Biochemistry, University of Regensburg, 93040 Regensburg, Germany.
authors.forename: Reinhard
authors.initials: R
authors.lastname: Sterner
authors.affiliation: From the Institute of Biophysics and Physical Biochemistry, University of Regensburg, 93040 Regensburg, Germany patrick.babinger@ur.de.
authors.forename: Patrick
authors.initials: P
authors.lastname: Babinger
mesh_terms: D000123:Acetyltransferases / Q000378:metabolism; D001412:Bacillus subtilis / Q000201:enzymology*; D055162:Biocatalysis; D005993:Glycerolphosphate Dehydrogenase / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation
chemical_list: D005993:Glycerolphosphate Dehydrogenase; C098215:glycerol-1-phosphate dehydrogenase; D000123:Acetyltransferases
keywords: acetyl coenzyme A (acetyl-CoA); acetyltransferase; enzyme; lipid ether; maltose; phosphatase