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Originally published In Press as doi:10.1074/jbc.M010371200 on February 5, 2001

J. Biol. Chem., Vol. 276, Issue 19, 15696-15703, May 11, 2001
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Differential Biosynthesis of Polysialic or Disialic Acid Structure by ST8Sia II and ST8Sia IV*

Shinobu Kitazume-KawaguchiDagger §, Sanae Kabata||, and Masanobu Arita

From the Dagger  Glycobiology Research Group, Frontier Research Program, Institute of Physical and Chemical Research (RIKEN), Wako, Saitama 351-0198 and  Department of Food and Nutrition, Faculty of Home Economics, Tokyo Kasei University, Tokyo 173-0003, Japan

ST8Sia II (STX) and ST8Sia IV (PST) are polysialic acid (polySia) synthases that catalyze polySia formation of neural cell adhesion molecule (NCAM) in vivo and in vitro. It still remains unclear how these structurally similar enzymes act differently in vivo. In the present study, we performed the enzymatic characterization of ST8Sia II and IV; both ST8Sia II and IV have pH optima of 5.8-6.1 and have no requirement of metal ions. Because the pH dependence of ST8Sia II and IV enzyme activities and the pK profile of His residues are similar, we hypothesized that a histidine residue would be involved in their catalytic activity. There is a conserved His residue (cf. His348 in ST8Sia II and His331 in ST8Sia IV, respectively) within the sialyl motif VS in all sialyltransferase genes cloned to date. Mutant ST8Sia II and IV enzymes in which this His residue was changed to Lys showed no detectable enzyme activity, even though they were folded correctly and could bind to CDP-hexanolamine, suggesting the importance of the His residue for their catalytic activity. Next, the degrees of polymerization of polySia in NCAM catalyzed by ST8Sia II and IV were compared. ST8Sia IV catalyzed larger polySia formation of NCAM than ST8Sia II. We also analyzed the (auto)polysialylated enzymes themselves. Interestingly, when ST8Sia II or IV itself was sialylated under conditions for polysialylation, the disialylated compound was the major product, even though polysialylated compounds were also observed. These results suggested that both ST8Sia II and IV catalyze polySia synthesis toward preferred acceptor substrates such as NCAM, whereas they mainly catalyze disialylation, similarly to ST8Sia III, toward unfavorable substrates such as enzyme themselves.

* This work was supported by Grant-in-aid for Encouragement of Young Scientists 11780435 from the Ministry of Education of Japan.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Present address: Glyco-chain Function, Frontier Research Program, Institute of Physical and Chemical Research (RIKEN), Wako, Saitama 351-0198, Japan. To whom correspondence should be addressed. Tel.: 81-48-467-9616; Fax: 81-48-467-9617; E-mail: shinobuk@postman.riken.go.jp.

|| Present address: Graduate School of Biological Sciences, Nara Institute of Science and Technology, Nara, 630-0101, Japan.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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