Catalytic preference of Salmonella typhimurium LT2 sialidase for N-acetylneuraminic acid residues over N-glycolylneuraminic acid residues
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- 作者：Akira Minami ; Sayaka Ishibashi ; Kiyoshi Ikeda ; Erika Ishitsubo ; Takanori Hori ; Hiroaki Tokiwa ; Risa Taguchi ; Daisuke Ieno ; Tadamune Otsubo ; Yukino Matsuda ; Saki Sai ; Mari Inada ; Takashi Suzuki
- 关键词：Salmonella typhimurium LT2 sialidase ; Sialic acid ; N-glycolylneuraminic acid ; 4MU-Neu5Gc ; Docking simulations ; Substrate specificity
- 刊名：FEBS Open Bio
- 出版年：2013
- 年：2013
- 卷：3
- 期：Complete
- 页码：231-236
- 全文大小：930 K
文摘
In a comparison of sialidase activities toward N-acetylneuraminic acid (Neu5Ac) and N-glycolylneuraminic acid (Neu5Gc), we found that Salmonella typhimurium LT2 sialidase (STSA) hardly cleaved 4-methylumbelliferyl Neu5Gc (4MU-Neu5Gc). The kcat/Km value of STSA for 4MU-Neu5Gc was found to be 110 times lower than that for 4-methylumbelliferyl Neu5Ac (4MU-Neu5Ac). Additionally, STSA had remarkably weak ability to cleave 伪2-3-linked-Neu5Gc contained in gangliosides and equine erythrocytes. In silico analysis based on first-principle calculations with transition-state analogues suggested that the binding affinity of Neu5Gc2en is 14.3鈥塳cal/mol more unstable than that of Neu5Ac2en. The results indicated that STSA preferentially cleaves Neu5Ac residues rather than Neu5Gc residues, which is important for anyone using this enzyme to cleave 伪2-3-linked sialic acids.