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

Yoshiaki Miura, Tsutomu Arai, Atsuko Ohtake, Makoto Ito, Kenji Yamamoto, Tatsuya Yamagata

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


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 β-lactosides and n-alkyl lactosides were substrates for both EGCase and CGase, but N-acylaminobutyl β-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 μM and 2.9 mM, respectively.

Original languageEnglish
Pages (from-to)957-960
Number of pages4
Issue number9
Publication statusPublished - Sept 1999

All Science Journal Classification (ASJC) codes

  • Biochemistry


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