Zane W Taylor1, Haley A Brown2, Tamari Narindoshvili3, Cory Q Wenzel4, Christine M Szymanski4,5, Hazel M Holden2, Frank M Raushel1,3. 1. Department of Biochemistry & Biophysics, Texas A&M University , College Station, Texas 77843, United States. 2. Department of Biochemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States. 3. Department of Chemistry, Texas A&M University , College Station, Texas 77843, United States. 4. Department of Biological Sciences, University of Alberta , Edmonton, Alberta Canada , T6G 2E9. 5. Department of Microbiology and Complex Carbohydrate Research Center, University of Georgia , Athens, Georgia 30602, United States.
Abstract
Bacterial capsular polysaccharides (CPS) are complex carbohydrate structures that play a role in the overall fitness of the organism. Campylobacter jejuni, known for being a major cause of bacterial gastroenteritis worldwide, produces a CPS with a unique O-methyl phosphoramidate (MeOPN) modification on specific sugar residues. The formation of P-N bonds in nature is relatively rare, and the pathway for the assembly of the phosphoramidate moiety in the CPS of C. jejuni is unknown. In this investigation we discovered that the initial transformation in the biosynthetic pathway for the MeOPN modification of the CPS involves the direct phosphorylation of the amide nitrogen of l-glutamine with ATP by the catalytic activity of Cj1418. The other two products are AMP and inorganic phosphate. The l-glutamine-phosphate product was characterized using 31P NMR spectroscopy and mass spectrometry. We suggest that this newly discovered enzyme be named l-glutamine kinase.
Bacterial capsular pan class="Chemical">polysaccharides (pan class="Chemical">CPS) are complex carbohydrate structures that play a role in the overall fitness of the organism. Campylobacter jejuni, known for being a major cause of bacterial gastroenteritis worldwide, produces a CPS with a unique O-methyl phosphoramidate (MeOPN) modification on specific sugar residues. The formation of P-N bonds in nature is relatively rare, and the pathway for the assembly of the phosphoramidate moiety in the CPS of C. jejuni is unknown. In this investigation we discovered that the initial transformation in the biosynthetic pathway for the MeOPN modification of the CPS involves the direct phosphorylation of the amidenitrogen of l-glutamine with ATP by the catalytic activity of Cj1418. The other two products are AMP and inorganic phosphate. The l-glutamine-phosphate product was characterized using 31P NMR spectroscopy and mass spectrometry. We suggest that this newly discovered enzyme be named l-glutamine kinase.
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