Open AccessCatalytic preference of Salmonella typhimurium LT2 sialidase for N ‐acetylneuraminic acid residues over N ‐glycolylneuraminic acid residues
Author(s) -
Minami Akira,
Ishibashi Sayaka,
Ikeda Kiyoshi,
Ishitsubo Erika,
Hori Takanori,
Tokiwa Hiroaki,
Taguchi Risa,
Ieno Daisuke,
Otsubo Tadamune,
Matsuda Yukino,
Sai Saki,
Inada Mari,
Suzuki Takashi
Publication year - 2013
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1016/j.fob.2013.05.002
Subject(s) - sialidase , cleave , sialic acid , n acetylneuraminic acid , chemistry , enzyme , neuraminidase , salmonella , neuraminic acid , biochemistry , stereochemistry , bacteria , biology , genetics
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 k cat / K m 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 α2‐3‐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 kcal/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 α2‐3‐linked sialic acids.