Kiefelt M J, Wilson J C, Bennett S, Gredley M, von Itzstein M
Department of Medicinal Chemistry, Monash University, Parkville, Victoria, Australia.
Bioorg Med Chem. 2000 Mar;8(3):657-64. doi: 10.1016/s0968-0896(99)00325-9.
Several C-9 modified N-acetylneuraminic acid derivatives have been synthesised and evaluated as substrates of N-acetylneuraminic acid aldolase. Simple C-9 acyl or ether modified derivatives of N-acetylneuraminic acid were found to be accepted as substrates by the enzyme, albeit being transformed more slowly than Neu5Ac itself. 1H NMR spectroscopy was used to evaluate the extent of the enzyme catalysed transformation of these compounds. Interestingly, the chain-extended Neu5Ac derivative 16 is not a substrate for N-acetylneuraminate lyase and behaves as an inhibitor of the enzyme.
已经合成了几种C-9修饰的N-乙酰神经氨酸衍生物，并将其作为N-乙酰神经氨酸醛缩酶的底物进行了评估。发现N-乙酰神经氨酸的简单C-9酰基或醚修饰衍生物可被该酶接受为底物，尽管其转化速度比Neu5Ac本身慢。使用1H NMR光谱来评估这些化合物的酶催化转化程度。有趣的是，链延长的Neu5Ac衍生物16不是N-乙酰神经氨酸裂解酶的底物，而是该酶的抑制剂。
