Guldan, Harald and Sterner, Reinhard and Babinger, Patrick (2008) Identification and characterization of a bacterial glycerol-1-phosphate dehydrogenase: Ni2+-dependent AraM from Bacillus subtilis. BIOCHEMISTRY, 47 (28). pp. 7376-7384. ISSN 0006-2960,
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The exclusive presence of glycerol-1-phosphate dehydrogenases (G1PDH) has been postulated to be a key feature that distinguishes archaea from bacteria. However, homologues of G1PDH genes can be found in several bacterial species, among them the hitherto uncharacterized open reading frame araM from Bacillus subtilis. We produced recombinant AraM in Escherichia coli and demonstrate that the purified protein forms a homodimer that reversibly reduces dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. AraM, which constitutes the first identified G1PDH from bacteria, has a similar catalytic efficiency as its archaeal homologues, but its activity is dependent on the presence of Ni2+ instead of Zn2+. On the basis of these findings and the analysis of an araM knockout mutant, we propose that AraM generates GIP for the synthesis of phosphoglycerolipids in Gram-positive bacterial species.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | SN-GLYCEROL-1-PHOSPHATE DEHYDROGENASE; LIPOTEICHOIC ACID; HYPERTHERMOPHILIC ARCHAEON; LIPID BIOSYNTHESIS; BINDING-PROPERTIES; NADH; SEQUENCE; ENZYME; CELLS; FLUORESCENCE; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 28 Oct 2020 08:04 |
| Last Modified: | 28 Oct 2020 08:04 |
| URI: | https://pred.uni-regensburg.de/id/eprint/30614 |
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