N-acyl amino acid biosynthesis in marine bacterium, Deleya marina

• Published in: Biochimica et biophysica acta 1997-07, Vol.1336 (1), p.28-32
• Main Authors: Yagi, Hisaaki, Corzo, Gerardo, Nakahara, Toro
• Format: Article
• Language: English
• Subjects: Bacteria - metabolism; Deleya marina; Marine Biology; N-acyl isoleucine; N-acyl leucine; N-acyl ornithine; Ornithine - analogs & derivatives; Ornithine - biosynthesis; Ornithine - chemistry; Protein Conformation; Seawater
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/S0304-4165(97)00009-3

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 α-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 α-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.