PubMed:10460837 JSONTXT

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":809,"end":826},"obj":"FMAID:196810"},{"id":"_T2","span":{"begin":809,"end":826},"obj":"FMAID:82815"},{"id":"_T3","span":{"begin":809,"end":826},"obj":"FMAID:82811"},{"id":"_T4","span":{"begin":809,"end":826},"obj":"FMAID:196806"},{"id":"_T5","span":{"begin":809,"end":826},"obj":"FMAID:196809"},{"id":"_T6","span":{"begin":809,"end":826},"obj":"FMAID:82814"},{"id":"_T7","span":{"begin":809,"end":826},"obj":"FMAID:196812"},{"id":"_T8","span":{"begin":809,"end":826},"obj":"FMAID:82817"},{"id":"_T9","span":{"begin":809,"end":826},"obj":"FMAID:196807"},{"id":"_T10","span":{"begin":809,"end":826},"obj":"FMAID:82813"},{"id":"_T11","span":{"begin":809,"end":826},"obj":"FMAID:196808"},{"id":"_T12","span":{"begin":809,"end":826},"obj":"FMAID:196814"},{"id":"_T13","span":{"begin":809,"end":826},"obj":"FMAID:82819"},{"id":"_T14","span":{"begin":809,"end":826},"obj":"FMAID:196815"},{"id":"_T15","span":{"begin":809,"end":826},"obj":"FMAID:196813"},{"id":"_T16","span":{"begin":809,"end":826},"obj":"FMAID:82818"},{"id":"_T17","span":{"begin":809,"end":826},"obj":"FMAID:82812"},{"id":"_T18","span":{"begin":1136,"end":1142},"obj":"FMAID:165145"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Requirement for a different hydrophobic moiety and reliable chromogenic substrate for endo-type glycosylceramidases.\nA 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. Km of the chromogenic lactoside for CGase and Rhodococcus EGCase were 28 microM and 2.9 mM, respectively."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":321,"end":329},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/2"},{"id":"T2","span":{"begin":321,"end":329},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/629395"},{"id":"T3","span":{"begin":498,"end":502},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T4","span":{"begin":498,"end":502},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T5","span":{"begin":602,"end":606},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/3554"},{"id":"T6","span":{"begin":602,"end":606},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/158455"},{"id":"T7","span":{"begin":764,"end":769},"obj":"http://purl.bioontology.org/ontology/STY/T096"},{"id":"T8","span":{"begin":1109,"end":1120},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/37919"}],"text":"Requirement for a different hydrophobic moiety and reliable chromogenic substrate for endo-type glycosylceramidases.\nA 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. Km of the chromogenic lactoside for CGase and Rhodococcus EGCase were 28 microM and 2.9 mM, respectively."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":116},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":117,"end":285},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":286,"end":410},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":411,"end":479},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":480,"end":705},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":706,"end":853},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":854,"end":1062},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1063,"end":1168},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":116},"obj":"Sentence"},{"id":"T2","span":{"begin":117,"end":285},"obj":"Sentence"},{"id":"T3","span":{"begin":286,"end":410},"obj":"Sentence"},{"id":"T4","span":{"begin":411,"end":479},"obj":"Sentence"},{"id":"T5","span":{"begin":480,"end":705},"obj":"Sentence"},{"id":"T6","span":{"begin":706,"end":853},"obj":"Sentence"},{"id":"T7","span":{"begin":854,"end":1062},"obj":"Sentence"},{"id":"T8","span":{"begin":1063,"end":1168},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":116},"obj":"Sentence"},{"id":"T2","span":{"begin":117,"end":285},"obj":"Sentence"},{"id":"T3","span":{"begin":286,"end":410},"obj":"Sentence"},{"id":"T4","span":{"begin":411,"end":479},"obj":"Sentence"},{"id":"T5","span":{"begin":480,"end":705},"obj":"Sentence"},{"id":"T6","span":{"begin":706,"end":853},"obj":"Sentence"},{"id":"T7","span":{"begin":854,"end":1062},"obj":"Sentence"},{"id":"T8","span":{"begin":1063,"end":1168},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Requirement for a different hydrophobic moiety and reliable chromogenic substrate for endo-type glycosylceramidases.\nA 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. Km of the chromogenic lactoside for CGase and Rhodococcus EGCase were 28 microM and 2.9 mM, respectively."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":922,"end":930},"obj":"http://purl.obolibrary.org/obo/GO_0009056"},{"id":"T2","span":{"begin":1034,"end":1061},"obj":"http://purl.obolibrary.org/obo/GO_0017042"}],"text":"Requirement for a different hydrophobic moiety and reliable chromogenic substrate for endo-type glycosylceramidases.\nA 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. Km of the chromogenic lactoside for CGase and Rhodococcus EGCase were 28 microM and 2.9 mM, respectively."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":193,"end":202},"obj":"http://edamontology.org/data_0883"},{"id":"T2","span":{"begin":369,"end":378},"obj":"http://edamontology.org/data_0883"},{"id":"T3","span":{"begin":635,"end":642},"obj":"http://edamontology.org/data_1756"},{"id":"T4","span":{"begin":841,"end":852},"obj":"http://edamontology.org/operation_2423"},{"id":"T5","span":{"begin":1063,"end":1065},"obj":"http://edamontology.org/data_0910"}],"text":"Requirement for a different hydrophobic moiety and reliable chromogenic substrate for endo-type glycosylceramidases.\nA 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. Km of the chromogenic lactoside for CGase and Rhodococcus EGCase were 28 microM and 2.9 mM, respectively."}

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":1133,"end":1135},"obj":"http://www.glycoepitope.jp/epitopes/AN0746"}],"text":"Requirement for a different hydrophobic moiety and reliable chromogenic substrate for endo-type glycosylceramidases.\nA 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. Km of the chromogenic lactoside for CGase and Rhodococcus EGCase were 28 microM and 2.9 mM, respectively."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":321,"end":329},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1109,"end":1120},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"2"},{"id":"A2","pred":"db_id","subj":"T1","obj":"629395"},{"id":"A3","pred":"db_id","subj":"T3","obj":"1661425"},{"id":"A4","pred":"db_id","subj":"T3","obj":"1827"}],"text":"Requirement for a different hydrophobic moiety and reliable chromogenic substrate for endo-type glycosylceramidases.\nA 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. Km of the chromogenic lactoside for CGase and Rhodococcus EGCase were 28 microM and 2.9 mM, respectively."}