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Glycobiology, Vol 9, 957-960, Copyright © 1999 by Oxford University Press

ORIGINAL ARTICLES

Requirement for a different hydrophobic moiety and reliable chromogenic substrate for endo-type glycosylceramidases

Y Miura, T Arai, A Ohtake, M Ito, K Yamamoto and T Yamagata3
Department of Biomolecular Engineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midoriku, Yokohama 226-8501, Japan, Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Higashiku, Fukuoka 812- 8581, Japan, Department.

A series of synthetic lactosides with aglycones that differed in length and structure were used to determine the substrate specificity of endo - type glycosylceramidases. Endoglycoceramidases (EGCase) from bacteria preferred lactosides with an acylamide structure over simple n -alkyl lactosides. While ceramide glycanase (CGase) from leech did not show preference. N -Acylaminoethyl beta-lactosides and n -alkyl lactosides were substrates for both EGCase and CGase, but N -acylaminobutyl beta- lactosides, whose acylamide residue differs from that in ceramide, were not hydrolyzed by EGCases. Thus, EGCases, but not CGase, appear to require an N -acyl group at the same position as that of intact glycosphingolipid for substrate recognition. A p -nitrophenyl lactoside derivative possessing an N -acyl chain was degraded by both EGCases and CGase and this chromogenic substrate may be an alternative substrate for endo -type glycosylceramidase activity. K m of the chromogenic lactoside for CGase and Rhodococcus EGCase were 28 &mgr;M and 2.9 mM, respectively.
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