Pegg M S, von Itzstein M
School of Pharmaceutical Chemistry, Victorian College of Pharmacy, Monash University, Parkville, Australia.
Biochem Mol Biol Int. 1994 Apr;32(5):851-8.
Sialidase from influenza virus A (Tokyo/3/67, N2) is inhibited in slow-binding fashion by 2,3-didehydro-2,4-dideoxy-4-guanidino-N-acetyl-D-neuraminic acid. The Ki observed for the tightly-bound form at steady-state is 3 x 10(-11) M. Slow-binding, which is a consequence of the guanidinyl moiety of the inhibitor, is observed only for influenza virus A sialidase and not for influenza virus B or any other viral, bacterial, or mammalian sialidase investigated. The different results obtained for sialidases from influenza virus A and B, whose active sites are conserved, point to the involvement of the expulsion of a structural water molecule in the slow-binding mechanism.
来自甲型流感病毒（东京/3/67，N2）的唾液酸酶被2,3 - 二脱氢 - 2,4 - 二脱氧 - 4 - 胍基 - N - 乙酰 - D - 神经氨酸以慢结合方式抑制。在稳态下观察到的紧密结合形式的Ki为3×10⁻¹¹ M。慢结合是抑制剂胍基部分的结果，仅在甲型流感病毒唾液酸酶中观察到，而在乙型流感病毒或任何其他研究的病毒、细菌或哺乳动物唾液酸酶中未观察到。来自甲型和乙型流感病毒的唾液酸酶，其活性位点是保守的，但得到了不同的结果，这表明在慢结合机制中涉及到一个结构水分子的排出。
