Biochem Biophys Res Commun 1994 Nov 30;2051:893-8. doi: 10.1006/bbrc.1994.2748.

Differential reactivity of two types of N-glycolyneuraminic acid dimers toward enzymatic and nonenzymatic hydrolysis of their interketosidic linkages.

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The kinetics of acid- and sialidase-catalyzed hydrolysis of the interketosidic linkages of two different disialic acids, Neu5Gc alpha 2-->5-OglycolylNeu5Gc and Neu5Gc alpha 2-->8Neu5Gc, were studied. The former sequence was recently identified in the polysialic acid chains of a sialic acid-rich glycoprotein isolated from the egg jelly coat of two different species of sea urchins, and the latter was previously found in the cortical alveolar-derived polysialoglycoprotein from rainbow trout eggs. At pH values < 3.8, the rate of hydrolysis of Neu5Gc alpha 2-->5-OglycolylNeu5Gc was greater than that of Neu5Gc alpha 2-->8Neu5Gc. Paradoxically, however, Neu5Gc alpha 2-->5-OglycolylNeu5Gc was more stable than Neu5Gc alpha 2-->8Neu5Gc at pH values > 3.8. These findings indicate a greater contribution of intramolecular general acid catalysis to the lability of the alpha 2-->5-ketosidic linkage. Neu5Gc alpha 2-->5-OglycolylNeu5Gc was a poor substrate for Arthrobacter ureafaciens, Clostridium perfringens, and Vibrio cholerae sialidases, in contrast to Neu5Gc alpha 2-->8Neu5Gc. Neu5Gc alpha 2-->5-OglycolylNeu5Gc was essentially resistant to hydrolysis by A. ureafaciens sialidase.

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Genes referenced: LOC100887844