N-acyl amino acid biosynthesis in marine bacterium, Deleya marina.
We reported previously that the marine bacterium, Deleya marina (ATCC 25374), produced N-acyl leucine and isoleucine, in which nonhydroxy fatty acid was linked to alpha-amino group of amino acid. Further analysis of bacterium lipids revealed the additional production of N-acyl ornithine. The N-acyl ornithine had a 3-hydroxy fatty acid linked by an amide bond to a-amino group of ornithine and a nonhydroxy fatty acid esterified to the hydroxy group of the 3-hydroxy fatty acid. N-acyl ornithine was located in the cell membrane and N-acyl leucine and isoleucine in cytoplasm. N-acyl ornithine is thought to be a functional analogue of phosphatidylethanolamine (PE) because of their similar structure. PE replacement into N-acyl ornithine in the cell membrane under phosphate-limited conditions was observed with other bacteria, so we anticipated the nonbiosynthesis of N-acyl ornithine under phosphate-sufficient conditions. We did not anticipate that N-acyl leucine and isoleucine in cytoplasm, whose structure is dissimilar to that of PE, would be replaced into PE in the cell membrane. Neither N-acyl leucine, N-acyl isoleucine, nor N-acyl ornithine was biosynthesized under phosphate-sufficient condition. Thus, we report here for the first time that N-acyl amino acids in cytoplasm were not biosynthesized under phosphate-sufficient conditions.
Yagi
H
H
National Institute of Bioscience and Human Technology, Tsukuba, Ibaraki, Japan. hyagi@ccmail.nibh.go.jp
Corzo
G
G
Nakahara
T
T
D001419:Bacteria / Q000378:metabolism*; D008386:Marine Biology; D009952:Ornithine / Q000031:analogs & derivatives / Q000096:biosynthesis* / Q000737:chemistry; D011487:Protein Conformation; D012623:Seawater
D009952:Ornithine