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Regulation of capsular polysialic acid biosynthesis by N ‐acetyl‐ d ‐mannosamine, an intermediate of sialic acid metabolism
Author(s) -
Revilla-Nuin Beatriz,
Rodriguez-Aparicio Leandro B,
Ferrero Miguel A,
Reglero Angel
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00339-1
Subject(s) - polysialic acid , sialic acid , biochemistry , escherichia coli , chemistry , biosynthesis , enzyme , lyase , metabolism , cell adhesion , gene , cell , neural cell adhesion molecule
N ‐Acetyl‐ d ‐mannosamine (ManNAc) is a specific substrate for the synthesis of N ‐acetylneuraminic acid, the essential precursor of bacterial capsular polysialic acid (PA). When Escherichia coli K92 used ManNAc as a carbon source, we observed a dramatic reduction (up to 90%) in in vivo PA production. Experiments in which the carbon source was changed revealed that the maximal inhibitory effect occurred when this sugar was present in the medium before the logarithmic phase of bacterial growth had started. Enzymatic analysis revealed that high concentrations of ManNAc‐6‐phosphate inhibit NeuAc lyase, the enzyme that synthesizes NeuAc for PA biosynthesis in E. coli . These results indicate that ManNAc‐6‐phosphate is able to regulate NeuAc lyase activity and modulate the PA synthesis.