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Journal of Biochemistry 2006 139(3):535-541; doi:10.1093/jb/mvj056
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© 2006 The Japanese Biochemical Society.

Regular Paper

Acceptor Specificity of 4-{alpha}-Glucanotransferases of Mammalian Glycogen Debranching Enzymes

Yasushi Makino and Kaoru Omichi*

Department of Chemistry, Graduate School of Science, Osaka Prefecture University, Sakai, Osaka 590-0035

* To whom correspondence should be addressed. Fax: +81-72-222-4791, E-mail: komichi{at}c.s.osakafu-u.ac.jp

Glycogen debranching enzyme (GDE) has two distinct active sites for its 4-{alpha}-glucanotransferase and amylo-{alpha}-1,6-glucosidase activities. The GDE 4-{alpha}-glucanotransferases of mammals show stringent donor specificity; only {alpha}-glucans with an {alpha}-1,6–linked maltotetraosyl or maltotriosyl branch function as donors of a maltotriosyl or maltosyl residue. In this study, we investigated the acceptor specificity of the 4-{alpha}-glucanotransferases using methyl {alpha}-maltooligosides, p-nitrophenyl {alpha}-maltooligosides, and pyridylaminated maltooligosaccharides of various sizes as the acceptor substrates, and phosphorylase limit dextrin as the donor substrate. High-performance liquid chromatography analysis of the transfer products indicated that maltotriosyl and maltosyl residues were specifically transferred from phosphorylase limit dextrin to acceptors with a maltopentaosyl residue comprising a nonreducing-end. These results suggest that the acceptor binding sites in the active sites of mammalian GDE 4-{alpha}-glucanotransferases are composed of tandem subsites that are geometrically complementary to five glucose residues.


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