Linde, Mona and Peterhoff, David and Sterner, Reinhard and Babinger, Patrick (2016) Identification and Characterization of Heptaprenylglyceryl Phosphate Processing Enzymes in Bacillus subtilis. JOURNAL OF BIOLOGICAL CHEMISTRY, 291 (28). pp. 14861-14870. ISSN 0021-9258, 1083-351X
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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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ESCHERICHIA-COLI; ACYL MIGRATION; SUBSTRATE-SPECIFICITY; BIOSYNTHESIS; ARCHAEA; BACTERIA; MALTOSE; ACETYLTRANSFERASE; ACYLTRANSFERASES; TRANSACETYLASE; acetyl coenzyme A (acetyl-CoA); acetyltransferase; enzyme; lipid ether; phosphatase; maltose |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie III |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 02 Apr 2019 11:49 |
| Last Modified: | 02 Apr 2019 11:49 |
| URI: | https://pred.uni-regensburg.de/id/eprint/3636 |
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