التفاصيل البيبلوغرافية
| العنوان: |
Headgroup hydroxylation by OlsE occurs at the C4 position of ornithine lipid and is widespread in proteobacteria and bacteroidetes. |
| المؤلفون: |
Hölzl, Georg1, Sohlenkamp, Christian2 chsohlen@ccg.unam.mx, Vences-Guzmán, Miguel Angel2, Gisch, Nicolas3 |
| المصدر: |
Chemistry & Physics of Lipids. Jul2018, Vol. 213, p32-38. 7p. |
| مصطلحات موضوعية: |
*GENE expression, *ESCHERICHIA coli, *ORNITHINE, *FATTY acids, *AMINO acids |
| مستخلص: |
Amino acid-containing acyloxyacyl lipids are composed of a 3-hydroxy fatty acid amide-bound to the α-amino group of an amino acid. A second fatty acid is ester-linked to the 3-hydroxy group of the first fatty acid. Most commonly, ornithine is the headgroup of these lipids, but glycine, serineglycine, glutamine and lysine have also been described in bacteria. Ornithine lipids (OL) can be synthesized by about 50% of the sequenced bacterial species, and several covalent modifications of its basic structure have been described. The OL hydroxylase OlsE is widespread in Rhizobium and Agrobacterium species and is responsible for introducing a hydroxyl group at a hence unknown position within the ornithine headgroup causing the formation of the OL named S2. Using NMR on purified OL S2, we show that the OlsE-mediated hydroxylation takes place at the C-4 position of the ornithine headgroup. Furthermore, we identify a hydroxylase in the genome of Pseudopedobacter saltans , distantly related to OlsE from α-proteobacteria, able to hydroxylate the headgroup of both ornithine lipids and lysine lipids. A homology search with the amino acid sequence of this hydroxylase allows us to predict that OL headgroup hydroxylation is not restricted to a few α-proteobacteria, but is apparently also common in many genera belonging to the Cytophaga-Flavobacterium-Bacteroidetes (CFB) group of bacteria. [ABSTRACT FROM AUTHOR] |
| قاعدة البيانات: |
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