Regulation of capsular polysialic acid biosynthesis by N‐acetyl‐d‐mannosamine, an intermediate of sialic acid metabolism

FEBS Letters

Ferrero, Miguel A¹  Rodriguez-Aparicio, Leandro B¹  Revilla-Nuin, Beatriz¹  Reglero, Angel¹ 

[1] Departamento de Bioquímica y Biología Molecular, Universidad de León, Campus de Vegazana, 24007 León, Spain

关键词: N-Acetyl-d-mannosamine;    Polysialic acid;    Capsular polysaccharide;    PA;    polysialic acid;    NeuAc or sialic acid;    N-acetyl-d-neuraminic acid;    N-CAM;    cell adhesion molecule;    ManNAc;    N-acetyl-d-mannosamine;    GlcNAc;    N-acetyl-d-glucosamine;    CTP;    cytidine 5′-triphosphate;    CMP-NeuAc;    cytidine 5′-monophospho-N-acetylneuraminic acid;    DTT;    dithiothreitol;    Pyr;    pyruvate;    BSA;    bovine serum albumin;   

DOI  :  10.1016/S0014-5793(98)00339-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown