The enzyme, characterized from the bacterium Rhizobium tropici, catalyses the hydroxylation of C-2 of the fatty acyl group that is ester-linked to the 3-hydroxy position of the amide-linked fatty acid.
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The expected taxonomic range for this enzyme is: Rhizobium tropici
The enzyme, characterized from the bacterium Rhizobium tropici, catalyses the hydroxylation of C-2 of the fatty acyl group that is ester-linked to the 3-hydroxy position of the amide-linked fatty acid.
hydroxylase OlsC modifies two species of ornithine-containing lipids in vivo, presumably by hydroxylation. A mutant carrying a nonpolar deletion in OlsC is symbiotically defective, whereas overexpressed OlsC in the complemented strain provokes an acid-sensitive phenotype
ornithine lipid hydroxylase OlsC introduces a hydroxyl group at the 2 position of the secondary fatty acid of ornithine lipids. Mutants deficient in OlsC cause an increase in nodule number that is reverted by the deletion of hydroxylase OlsE. OlsC is important in conferring stress resistance
ornithine lipid hydroxylase OlsC introduces a hydroxyl group at the 2 position of the secondary fatty acid of ornithine lipids. Mutants deficient in OlsC cause an increase in nodule number that is reverted by the deletion of hydroxylase OlsE. OlsC is important in conferring stress resistance
hydroxylase OlsC modifies two species of ornithine-containing lipids in vivo, presumably by hydroxylation. A mutant carrying a nonpolar deletion in OlsC is symbiotically defective, whereas overexpressed OlsC in the complemented strain provokes an acid-sensitive phenotype
A CIC chloride channel homolog and ornithine-containing membrane lipids of Rhizobium tropici CIAT899 are involved in symbiotic efficiency and acid tolerance