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On the Specificity of Sialidase. Synthesis and Properties of N 5 -Acetyl-β-D-neuraminoylpeptides – AcNeu-Gly-OH, AcNeu-Glu-OH, AcNeu-Phe-OH — and the corresponding α-Ketosides

1983; De Gruyter; Volume: 364; Issue: 2 Linguagem: Inglês

10.1515/bchm2.1983.364.2.1411

0018-4888

Volker Eschenfelder, Reinhard Brossmer, Margot Wachter,

Natural Antidiabetic Agents Studies

By means of the mixed anhydride procedure the benzyl alpha-ketoside of N5-acetyl-D-neuraminic acid was linked to L-glycine, L-glutamic acid and L-phenylalanine. Hydrogenolytic cleavage of the benzyl group resulted in the corresponding free N5-acetyl-beta-D-neuraminoylpeptides. This new class of compounds is no substrate for Vibrio cholerae sialidase. The enzyme does not split the benzyl alpha-ketosides of N5-acetyl-D-neuraminoylpeptides nor is its activity inhibited by these compounds. The results strongly support the assumption that in sialidase substrates the carboxy group must be located close to the ketosidic oxygen. N-(N5-acetyl-beta-D-neuraminoyl)-L-phenylalanine was readily hydrolysed by carboxypeptidase A from bovine pancreas.