Catalytic preference of Salmonella typhimurium LT2 sialidase for N-acetylneuraminic acid residues over N-glycolylneuraminic acid residues.
Catalytic preference of Salmonella typhimurium LT2 sialidase for N-acetylneuraminic acid residues over N-glycolylneuraminic acid residues.
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鼠伤寒沙门氏菌LT2唾液酸酶的催化偏好是N-乙酰基神经氨酸酸残基而不是N-糖苷神经酰氨酸残基。
DOI：
10.1016/j.fob.2013.05.002
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发表时间：
2013
期刊：
影响因子：
2.6
通讯作者：
Suzuki T
中科院分区：
文献类型：
--
作者：
Minami A;Ishibashi S;Ikeda K;Ishitsubo E;Hori T;Tokiwa H;Taguchi R;Ieno D;Otsubo T;Matsuda Y;Sai S;Inada M;Suzuki T
在对N-乙酰神经氨酸(Neu5Ac)和N-羟基神经氨酸(Neu5Gc)唾液酸酶活性的比较中，我们发现鼠伤寒沙门氏菌LT2唾液酸酶(STSA)几乎不切割4-甲基伞形花序Neu5Gc(4MU-Neu5Gc)。4MU-Neu5Gc的Kcat/Km值比4-甲基伞形花环Neu5Ac(4MU-Neu5Ac)的Kcat/Km值低110倍。此外，短链霉菌对神经节苷脂和马红细胞中的α2-3连接的Neu5Gc的切割能力也非常弱。在过渡态类似物的第一性原理计算的计算机分析中，Neu5Gc2en的结合亲和力比Neu5Ac2en的结合亲和力更不稳定，为14.3kcal/ 。结果表明，STSA优先切割Neu5Ac残基，而不是Neu5Gc残基，这对任何使用该酶切割α2-3连接的唾液酸的人都是重要的。鼠伤寒沙门氏菌LT2唾液酸酶(STSA)几乎不能切割4MU-Neu5Gc。STSA几乎不能切割神经节苷脂和马红细胞中的Neu5Gc残基。4MU-Neu5Gc的kcat/km值比4MU-Neu5Ac的低110倍。Neu5Gc2en的结合亲和力比Neu5Ac2en更不稳定(14.3kcal/ )。识别唾液酸基和α2-3键的氨基酸残基也区分Neu5Gc和Neu5Ac。
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 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. Salmonella typhimurium LT2 sialidase (STSA) hardly cleaved 4MU-Neu5Gc. STSA hardly cleaved Neu5Gc residues in ganglioside and equine erythrocytes. The kcat/Km value of STSA for 4MU-Neu5Gc was 110 times lower than that for 4MU-Neu5Ac. Binding affinity of Neu5Gc2en is more unstable (by 14.3 kcal/mol) than that of Neu5Ac2en. Amino acid residues that recognize sialyl α2-3 linkage also discriminate Neu5Gc and Neu5Ac.
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影响因子：
2.7
作者：
HOYER, LL;ROGGENTIN, P;VIMR, ER
通讯作者：
VIMR, ER
影响因子：
2.8
作者：
Ishikawa, Takeshi;Kuwata, Kazuo
通讯作者：
Kuwata, Kazuo
影响因子：
1.8
作者：
Ikeda, Kiyoshi;Miyamoto, Keisuke;Sato, Masayuki
通讯作者：
Sato, Masayuki
影响因子：
4.1
作者：
CORFIELD, AP;VEH, RW;SCHAUER, R
通讯作者：
SCHAUER, R
影响因子：
5.7
作者：
Minami, Akira;Shimizu, Hirotaka;Suzuki, Takashi
通讯作者：
Suzuki, Takashi