PubMed:18227125
Annnotations
Glycan-Motif
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 25-36 | https://glytoucan.org/Structures/Glycans/G43702JT | denotes | chondroitin |
| T2 | 463-474 | https://glytoucan.org/Structures/Glycans/G43702JT | denotes | chondroitin |
| T3 | 532-543 | https://glytoucan.org/Structures/Glycans/G43702JT | denotes | chondroitin |
| T4 | 913-924 | https://glytoucan.org/Structures/Glycans/G43702JT | denotes | chondroitin |
| T5 | 959-970 | https://glytoucan.org/Structures/Glycans/G43702JT | denotes | chondroitin |
GlyCosmos6-Glycan-Motif-Image
| Id | Subject | Object | Predicate | Lexical cue | image |
|---|---|---|---|---|---|
| T1 | 25-36 | Glycan_Motif | denotes | chondroitin | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G43702JT |
| T2 | 463-474 | Glycan_Motif | denotes | chondroitin | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G43702JT |
| T3 | 532-543 | Glycan_Motif | denotes | chondroitin | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G43702JT |
| T4 | 913-924 | Glycan_Motif | denotes | chondroitin | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G43702JT |
| T5 | 959-970 | Glycan_Motif | denotes | chondroitin | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G43702JT |
GlyCosmos6-Glycan-Motif-Structure
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 25-36 | https://glytoucan.org/Structures/Glycans/G43702JT | denotes | chondroitin |
| T2 | 463-474 | https://glytoucan.org/Structures/Glycans/G43702JT | denotes | chondroitin |
| T3 | 532-543 | https://glytoucan.org/Structures/Glycans/G43702JT | denotes | chondroitin |
| T4 | 913-924 | https://glytoucan.org/Structures/Glycans/G43702JT | denotes | chondroitin |
| T5 | 959-970 | https://glytoucan.org/Structures/Glycans/G43702JT | denotes | chondroitin |
Glycosmos6-GlycoEpitope
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 25-36 | http://www.glycoepitope.jp/epitopes/EP0081 | denotes | chondroitin |
| T2 | 463-474 | http://www.glycoepitope.jp/epitopes/EP0081 | denotes | chondroitin |
| T3 | 532-543 | http://www.glycoepitope.jp/epitopes/EP0081 | denotes | chondroitin |
| T4 | 913-924 | http://www.glycoepitope.jp/epitopes/EP0081 | denotes | chondroitin |
| T5 | 959-970 | http://www.glycoepitope.jp/epitopes/EP0081 | denotes | chondroitin |
uniprot-human
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 553-555 | http://www.uniprot.org/uniprot/O75390 | denotes | CS |
| T2 | 652-654 | http://www.uniprot.org/uniprot/O75390 | denotes | CS |
| T3 | 909-911 | http://www.uniprot.org/uniprot/O75390 | denotes | CS |
| T4 | 1266-1268 | http://www.uniprot.org/uniprot/O75390 | denotes | CS |
| T5 | 1670-1672 | http://www.uniprot.org/uniprot/O75390 | denotes | CS |
| T6 | 579-581 | http://www.uniprot.org/uniprot/P49366 | denotes | DS |
| T7 | 685-687 | http://www.uniprot.org/uniprot/P49366 | denotes | DS |
| T8 | 955-957 | http://www.uniprot.org/uniprot/P49366 | denotes | DS |
| T9 | 1293-1295 | http://www.uniprot.org/uniprot/P49366 | denotes | DS |
| T10 | 1659-1661 | http://www.uniprot.org/uniprot/P49366 | denotes | DS |
| T11 | 932-934 | http://www.uniprot.org/uniprot/Q13510 | denotes | AC |
| T12 | 1160-1162 | http://www.uniprot.org/uniprot/Q13510 | denotes | AC |
| T13 | 1072-1086 | http://www.uniprot.org/uniprot/P34059 | denotes | chondroitinase |
| T14 | 1145-1159 | http://www.uniprot.org/uniprot/P34059 | denotes | chondroitinase |
| T15 | 1389-1403 | http://www.uniprot.org/uniprot/P34059 | denotes | chondroitinase |
uniprot-mouse
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 932-934 | http://www.uniprot.org/uniprot/Q9WV54 | denotes | AC |
| T2 | 1160-1162 | http://www.uniprot.org/uniprot/Q9WV54 | denotes | AC |
| T3 | 1072-1086 | http://www.uniprot.org/uniprot/Q571E4 | denotes | chondroitinase |
| T4 | 1145-1159 | http://www.uniprot.org/uniprot/Q571E4 | denotes | chondroitinase |
| T5 | 1389-1403 | http://www.uniprot.org/uniprot/Q571E4 | denotes | chondroitinase |
| T6 | 1192-1195 | http://www.uniprot.org/uniprot/P11344 | denotes | Tyr |
| T7 | 1819-1826 | http://www.uniprot.org/uniprot/Q9EQE5 | denotes | spatial |
GlycoBiology-NCBITAXON
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 694-698 | http://purl.bioontology.org/ontology/NCBITAXON/158455 | denotes | beta |
| T2 | 694-698 | http://purl.bioontology.org/ontology/NCBITAXON/3554 | denotes | beta |
| T3 | 711-720 | http://purl.bioontology.org/ontology/NCBITAXON/127244 | denotes | mechanism |
| T4 | 766-772 | http://purl.bioontology.org/ontology/NCBITAXON/429025 | denotes | proton |
| T5 | 940-944 | http://purl.bioontology.org/ontology/NCBITAXON/3554 | denotes | beta |
| T6 | 940-944 | http://purl.bioontology.org/ontology/NCBITAXON/158455 | denotes | beta |
| T7 | 945-950 | http://purl.bioontology.org/ontology/NCBITAXON/6534 | denotes | helix |
| T8 | 998-1008 | http://purl.bioontology.org/ontology/NCBITAXON/127244 | denotes | mechanisms |
| T9 | 1096-1103 | http://purl.bioontology.org/ontology/NCBITAXON/210425 | denotes | Proteus |
| T10 | 1252-1261 | http://purl.bioontology.org/ontology/NCBITAXON/127244 | denotes | mechanism |
| T11 | 1352-1359 | http://purl.bioontology.org/ontology/NCBITAXON/353209 | denotes | related |
| T12 | 1360-1371 | http://purl.bioontology.org/ontology/NCBITAXON/200643 | denotes | Bacteroides |
| T13 | 1360-1371 | http://purl.bioontology.org/ontology/NCBITAXON/816 | denotes | Bacteroides |
| T14 | 1360-1388 | http://purl.bioontology.org/ontology/NCBITAXON/818 | denotes | Bacteroides thetaiotaomicron |
GO-BP
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 25-46 | http://purl.obolibrary.org/obo/GO_0047486 | denotes | chondroitin lyase ABC |
| T2 | 463-485 | http://purl.obolibrary.org/obo/GO_0047486 | denotes | chondroitin lyases ABC |
| T3 | 519-526 | http://purl.obolibrary.org/obo/GO_0009056 | denotes | degrade |
| T4 | 1269-1280 | http://purl.obolibrary.org/obo/GO_0009056 | denotes | degradation |
| T5 | 1296-1307 | http://purl.obolibrary.org/obo/GO_0009056 | denotes | degradation |
| T6 | 544-551 | http://purl.obolibrary.org/obo/GO_0051923 | denotes | sulfate |
| T7 | 570-577 | http://purl.obolibrary.org/obo/GO_0051923 | denotes | sulfate |
| T8 | 913-934 | http://purl.obolibrary.org/obo/GO_0030341 | denotes | chondroitin lyases AC |
| T9 | 932-934 | http://purl.obolibrary.org/obo/GO_0003987 | denotes | AC |
| T10 | 932-934 | http://purl.obolibrary.org/obo/GO_0043884 | denotes | AC |
| T11 | 1160-1162 | http://purl.obolibrary.org/obo/GO_0003987 | denotes | AC |
| T12 | 1160-1162 | http://purl.obolibrary.org/obo/GO_0043884 | denotes | AC |
| T13 | 959-979 | http://purl.obolibrary.org/obo/GO_0033999 | denotes | chondroitin lyases B |
| T14 | 1072-1086 | http://purl.obolibrary.org/obo/GO_0043890 | denotes | chondroitinase |
| T15 | 1145-1159 | http://purl.obolibrary.org/obo/GO_0043890 | denotes | chondroitinase |
| T16 | 1389-1403 | http://purl.obolibrary.org/obo/GO_0043890 | denotes | chondroitinase |
| T17 | 1145-1162 | http://purl.obolibrary.org/obo/GO_0030341 | denotes | chondroitinase AC |
GO-MF
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 1713-1720 | http://purl.obolibrary.org/obo/GO_0070026 | denotes | binding |
| T2 | 1713-1720 | http://purl.obolibrary.org/obo/GO_0003680 | denotes | binding |
| T3 | 1713-1720 | http://purl.obolibrary.org/obo/GO_0017091 | denotes | binding |
| T4 | 1713-1720 | http://purl.obolibrary.org/obo/GO_0005488 | denotes | binding |
UBERON-AE
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 945-950 | http://purl.obolibrary.org/obo/UBERON_0002488 | denotes | helix |
sentences
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| TextSentencer_T1 | 0-85 | Sentence | denotes | Composite active site of chondroitin lyase ABC accepting both epimers of uronic acid. |
| TextSentencer_T2 | 86-159 | Sentence | denotes | Enzymes have evolved as catalysts with high degrees of stereospecificity. |
| TextSentencer_T3 | 160-302 | Sentence | denotes | When both enantiomers are biologically important, enzymes with two different folds usually catalyze reactions with the individual enantiomers. |
| TextSentencer_T4 | 303-438 | Sentence | denotes | In rare cases a single enzyme can process both enantiomers efficiently, but no molecular basis for such catalysis has been established. |
| TextSentencer_T5 | 439-509 | Sentence | denotes | The family of bacterial chondroitin lyases ABC comprises such enzymes. |
| TextSentencer_T6 | 510-794 | Sentence | denotes | They can degrade both chondroitin sulfate (CS) and dermatan sulfate (DS) glycosaminoglycans at the nonreducing end of either glucuronic acid (CS) or its epimer iduronic acid (DS) by a beta-elimination mechanism, which commences with the removal of the C-5 proton from the uronic acid. |
| TextSentencer_T7 | 795-1054 | Sentence | denotes | Two other structural folds evolved to perform these reactions in an epimer-specific fashion: (alpha/alpha)(5) for CS (chondroitin lyases AC) and beta-helix for DS (chondroitin lyases B); their catalytic mechanisms have been established at the molecular level. |
| TextSentencer_T8 | 1055-1308 | Sentence | denotes | The structure of chondroitinase ABC from Proteus vulgaris showed surprising similarity to chondroitinase AC, including the presence of a Tyr-His-Glu-Arg catalytic tetrad, which provided a possible mechanism for CS degradation but not for DS degradation. |
| TextSentencer_T9 | 1309-1497 | Sentence | denotes | We determined the structure of a distantly related Bacteroides thetaiotaomicron chondroitinase ABC to identify additional structurally conserved residues potentially involved in catalysis. |
| TextSentencer_T10 | 1498-1580 | Sentence | denotes | We found a conserved cluster located approximately 12 A from the catalytic tetrad. |
| TextSentencer_T11 | 1581-1673 | Sentence | denotes | We demonstrate that a histidine in this cluster is essential for catalysis of DS but not CS. |
| TextSentencer_T12 | 1674-1814 | Sentence | denotes | The enzyme utilizes a single substrate-binding site while having two partially overlapping active sites catalyzing the respective reactions. |
| TextSentencer_T13 | 1815-1981 | Sentence | denotes | The spatial separation of the two sets of residues suggests a substrate-induced conformational change that brings all catalytically essential residues close together. |
| T1 | 0-85 | Sentence | denotes | Composite active site of chondroitin lyase ABC accepting both epimers of uronic acid. |
| T2 | 86-159 | Sentence | denotes | Enzymes have evolved as catalysts with high degrees of stereospecificity. |
| T3 | 160-302 | Sentence | denotes | When both enantiomers are biologically important, enzymes with two different folds usually catalyze reactions with the individual enantiomers. |
| T4 | 303-438 | Sentence | denotes | In rare cases a single enzyme can process both enantiomers efficiently, but no molecular basis for such catalysis has been established. |
| T5 | 439-509 | Sentence | denotes | The family of bacterial chondroitin lyases ABC comprises such enzymes. |
| T6 | 510-794 | Sentence | denotes | They can degrade both chondroitin sulfate (CS) and dermatan sulfate (DS) glycosaminoglycans at the nonreducing end of either glucuronic acid (CS) or its epimer iduronic acid (DS) by a beta-elimination mechanism, which commences with the removal of the C-5 proton from the uronic acid. |
| T7 | 795-1054 | Sentence | denotes | Two other structural folds evolved to perform these reactions in an epimer-specific fashion: (alpha/alpha)(5) for CS (chondroitin lyases AC) and beta-helix for DS (chondroitin lyases B); their catalytic mechanisms have been established at the molecular level. |
| T8 | 1055-1308 | Sentence | denotes | The structure of chondroitinase ABC from Proteus vulgaris showed surprising similarity to chondroitinase AC, including the presence of a Tyr-His-Glu-Arg catalytic tetrad, which provided a possible mechanism for CS degradation but not for DS degradation. |
| T9 | 1309-1497 | Sentence | denotes | We determined the structure of a distantly related Bacteroides thetaiotaomicron chondroitinase ABC to identify additional structurally conserved residues potentially involved in catalysis. |
| T10 | 1498-1580 | Sentence | denotes | We found a conserved cluster located approximately 12 A from the catalytic tetrad. |
| T11 | 1581-1673 | Sentence | denotes | We demonstrate that a histidine in this cluster is essential for catalysis of DS but not CS. |
| T12 | 1674-1814 | Sentence | denotes | The enzyme utilizes a single substrate-binding site while having two partially overlapping active sites catalyzing the respective reactions. |
| T13 | 1815-1981 | Sentence | denotes | The spatial separation of the two sets of residues suggests a substrate-induced conformational change that brings all catalytically essential residues close together. |
| T1 | 0-85 | Sentence | denotes | Composite active site of chondroitin lyase ABC accepting both epimers of uronic acid. |
| T2 | 86-159 | Sentence | denotes | Enzymes have evolved as catalysts with high degrees of stereospecificity. |
| T3 | 160-302 | Sentence | denotes | When both enantiomers are biologically important, enzymes with two different folds usually catalyze reactions with the individual enantiomers. |
| T4 | 303-438 | Sentence | denotes | In rare cases a single enzyme can process both enantiomers efficiently, but no molecular basis for such catalysis has been established. |
| T5 | 439-509 | Sentence | denotes | The family of bacterial chondroitin lyases ABC comprises such enzymes. |
| T6 | 510-794 | Sentence | denotes | They can degrade both chondroitin sulfate (CS) and dermatan sulfate (DS) glycosaminoglycans at the nonreducing end of either glucuronic acid (CS) or its epimer iduronic acid (DS) by a beta-elimination mechanism, which commences with the removal of the C-5 proton from the uronic acid. |
| T7 | 795-1054 | Sentence | denotes | Two other structural folds evolved to perform these reactions in an epimer-specific fashion: (alpha/alpha)(5) for CS (chondroitin lyases AC) and beta-helix for DS (chondroitin lyases B); their catalytic mechanisms have been established at the molecular level. |
| T8 | 1055-1308 | Sentence | denotes | The structure of chondroitinase ABC from Proteus vulgaris showed surprising similarity to chondroitinase AC, including the presence of a Tyr-His-Glu-Arg catalytic tetrad, which provided a possible mechanism for CS degradation but not for DS degradation. |
| T9 | 1309-1497 | Sentence | denotes | We determined the structure of a distantly related Bacteroides thetaiotaomicron chondroitinase ABC to identify additional structurally conserved residues potentially involved in catalysis. |
| T10 | 1498-1580 | Sentence | denotes | We found a conserved cluster located approximately 12 A from the catalytic tetrad. |
| T11 | 1581-1673 | Sentence | denotes | We demonstrate that a histidine in this cluster is essential for catalysis of DS but not CS. |
| T12 | 1674-1814 | Sentence | denotes | The enzyme utilizes a single substrate-binding site while having two partially overlapping active sites catalyzing the respective reactions. |
| T13 | 1815-1981 | Sentence | denotes | The spatial separation of the two sets of residues suggests a substrate-induced conformational change that brings all catalytically essential residues close together. |
GlyTouCan-IUPAC
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| GlycanIUPAC_T1 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G41652MJ" | denotes | all |
| GlycanIUPAC_T2 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G20761YC" | denotes | all |
| GlycanIUPAC_T3 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G19807HM" | denotes | all |
| GlycanIUPAC_T4 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G20351TE" | denotes | all |
| GlycanIUPAC_T5 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G71957MR" | denotes | all |
| GlycanIUPAC_T6 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G59040AE" | denotes | all |
| GlycanIUPAC_T7 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G14987PW" | denotes | all |
| GlycanIUPAC_T8 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G95064PC" | denotes | all |
| GlycanIUPAC_T9 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G39143AQ" | denotes | all |
| GlycanIUPAC_T10 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G65149OO" | denotes | all |
| GlycanIUPAC_T11 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G02766SY" | denotes | all |
| GlycanIUPAC_T12 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G26019KJ" | denotes | all |
| GlycanIUPAC_T13 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G36429CZ" | denotes | all |
| GlycanIUPAC_T14 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G89633TP" | denotes | all |
| GlycanIUPAC_T15 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G28494FO" | denotes | all |
| GlycanIUPAC_T16 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G06219CP" | denotes | all |
| GlycanIUPAC_T17 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G44237SM" | denotes | all |
| GlycanIUPAC_T18 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G57948RL" | denotes | all |
| GlycanIUPAC_T19 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G64016DN" | denotes | all |
| GlycanIUPAC_T20 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G14536PC" | denotes | all |
| GlycanIUPAC_T21 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G14356FW" | denotes | all |
| GlycanIUPAC_T22 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G34565UO" | denotes | all |
| GlycanIUPAC_T23 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G67124MW" | denotes | all |
| GlycanIUPAC_T24 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G71457ZU" | denotes | all |
| GlycanIUPAC_T25 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G55228VZ" | denotes | all |
| GlycanIUPAC_T26 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G31034MJ" | denotes | all |
| GlycanIUPAC_T27 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G25776IP" | denotes | all |
| GlycanIUPAC_T28 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G64442BV" | denotes | all |
| GlycanIUPAC_T29 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G57018LE" | denotes | all |
| GlycanIUPAC_T30 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G61761GX" | denotes | all |
| GlycanIUPAC_T31 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G76318UX" | denotes | all |
| GlycanIUPAC_T32 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G61906ER" | denotes | all |
| GlycanIUPAC_T33 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G68723GR" | denotes | all |
| GlycanIUPAC_T34 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G19540LE" | denotes | all |
| GlycanIUPAC_T35 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G74944PO" | denotes | all |
| GlycanIUPAC_T36 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G89489ZJ" | denotes | all |
| GlycanIUPAC_T37 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G04434YU" | denotes | all |
| GlycanIUPAC_T38 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G21450PB" | denotes | all |
| GlycanIUPAC_T39 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G93629QY" | denotes | all |
| GlycanIUPAC_T40 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G02603TR" | denotes | all |
| GlycanIUPAC_T41 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G40280JP" | denotes | all |
| GlycanIUPAC_T42 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G95259IC" | denotes | all |
| GlycanIUPAC_T43 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G26900FE" | denotes | all |
| GlycanIUPAC_T44 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G21346KK" | denotes | all |
| GlycanIUPAC_T45 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G62509FF" | denotes | all |
| GlycanIUPAC_T46 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G83932AK" | denotes | all |
| GlycanIUPAC_T47 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G96978IB" | denotes | all |
| GlycanIUPAC_T48 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G34275DN" | denotes | all |
| GlycanIUPAC_T49 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G07071JF" | denotes | all |
| GlycanIUPAC_T50 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G80639QD" | denotes | all |
| GlycanIUPAC_T51 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G99460PJ" | denotes | all |
| GlycanIUPAC_T52 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G22024BZ" | denotes | all |
| GlycanIUPAC_T53 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G74097ZY" | denotes | all |
| GlycanIUPAC_T54 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G84439YP" | denotes | all |
| GlycanIUPAC_T55 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G52207WQ" | denotes | all |
| GlycanIUPAC_T56 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G90695MS" | denotes | all |
| GlycanIUPAC_T57 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G50398QX" | denotes | all |
| GlycanIUPAC_T58 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G12166ZT" | denotes | all |
| GlycanIUPAC_T59 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G48368BR" | denotes | all |
| GlycanIUPAC_T60 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G57407RW" | denotes | all |
| GlycanIUPAC_T61 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G00386TY" | denotes | all |
| GlycanIUPAC_T62 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G18723JK" | denotes | all |
| GlycanIUPAC_T63 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G93757OR" | denotes | all |
| GlycanIUPAC_T64 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G29006SI" | denotes | all |
| GlycanIUPAC_T65 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G03099OQ" | denotes | all |
| GlycanIUPAC_T66 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G53739OW" | denotes | all |
| GlycanIUPAC_T67 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G70440ZO" | denotes | all |
| GlycanIUPAC_T68 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G29951RR" | denotes | all |
| GlycanIUPAC_T69 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G58402TI" | denotes | all |
| GlycanIUPAC_T70 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G39875TP" | denotes | all |
| GlycanIUPAC_T71 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G83439QV" | denotes | all |
| GlycanIUPAC_T72 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G41762RC" | denotes | all |
| GlycanIUPAC_T73 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G91604UI" | denotes | all |
| GlycanIUPAC_T74 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G88447WE" | denotes | all |
| GlycanIUPAC_T75 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G93634BS" | denotes | all |
| GlycanIUPAC_T76 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G02587BH" | denotes | all |
| GlycanIUPAC_T77 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G43511MX" | denotes | all |
| GlycanIUPAC_T78 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G64958DH" | denotes | all |
| GlycanIUPAC_T79 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G30384TR" | denotes | all |
| GlycanIUPAC_T80 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G15624EX" | denotes | all |
| GlycanIUPAC_T81 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G22706ST" | denotes | all |
| GlycanIUPAC_T82 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G57408PI" | denotes | all |
| GlycanIUPAC_T83 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G86403XX" | denotes | all |
| GlycanIUPAC_T84 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G78043YB" | denotes | all |
| GlycanIUPAC_T85 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G18952JK" | denotes | all |
| GlycanIUPAC_T86 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G49020ND" | denotes | all |
| GlycanIUPAC_T87 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G63590YW" | denotes | all |
| GlycanIUPAC_T88 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G22793KS" | denotes | all |
| GlycanIUPAC_T89 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G64134SS" | denotes | all |
| GlycanIUPAC_T90 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G17338HY" | denotes | all |
| GlycanIUPAC_T91 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G99745XF" | denotes | all |
| GlycanIUPAC_T92 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G27782HN" | denotes | all |
| GlycanIUPAC_T93 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G57496DC" | denotes | all |
| GlycanIUPAC_T94 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G93169WB" | denotes | all |
| GlycanIUPAC_T95 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G05518TD" | denotes | all |
| GlycanIUPAC_T96 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G62603DN" | denotes | all |
| GlycanIUPAC_T97 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G59574FS" | denotes | all |
| GlycanIUPAC_T98 | 1929-1932 | "http://rdf.glycoinfo.org/glycan/G47567WC" | denotes | all |
GlycoBiology-Motifs
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 25-36 | http://rdf.glycoinfo.org/glycan/G00018MO | denotes | chondroitin |
| T2 | 463-474 | http://rdf.glycoinfo.org/glycan/G00018MO | denotes | chondroitin |
| T3 | 532-543 | http://rdf.glycoinfo.org/glycan/G00018MO | denotes | chondroitin |
| T4 | 913-924 | http://rdf.glycoinfo.org/glycan/G00018MO | denotes | chondroitin |
| T5 | 959-970 | http://rdf.glycoinfo.org/glycan/G00018MO | denotes | chondroitin |
| T6 | 532-551 | http://rdf.glycoinfo.org/glycan/G00018MO | denotes | chondroitin sulfate |
| T7 | 561-577 | http://rdf.glycoinfo.org/glycan/G00019MO | denotes | dermatan sulfate |
GlycoBiology-Epitope
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| PD-GlycoEpitope-B_T1 | 25-36 | http://www.glycoepitope.jp/epitopes/EP0081 | denotes | chondroitin |
| PD-GlycoEpitope-B_T2 | 463-474 | http://www.glycoepitope.jp/epitopes/EP0081 | denotes | chondroitin |
| PD-GlycoEpitope-B_T3 | 532-543 | http://www.glycoepitope.jp/epitopes/EP0081 | denotes | chondroitin |
| PD-GlycoEpitope-B_T4 | 913-924 | http://www.glycoepitope.jp/epitopes/EP0081 | denotes | chondroitin |
| PD-GlycoEpitope-B_T5 | 959-970 | http://www.glycoepitope.jp/epitopes/EP0081 | denotes | chondroitin |
performance-test
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| PD-UBERON-AE-B_T1 | 945-950 | http://purl.obolibrary.org/obo/UBERON_0002488 | denotes | helix |
Glycan-GlyCosmos
| Id | Subject | Object | Predicate | Lexical cue | image |
|---|---|---|---|---|---|
| T1 | 25-36 | Glycan | denotes | chondroitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT |
| T2 | 463-474 | Glycan | denotes | chondroitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT |
| T3 | 532-543 | Glycan | denotes | chondroitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT |
| T4 | 913-924 | Glycan | denotes | chondroitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT |
| T5 | 959-970 | Glycan | denotes | chondroitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT |
GlyCosmos15-UBERON
| Id | Subject | Object | Predicate | Lexical cue | uberon_id |
|---|---|---|---|---|---|
| T1 | 945-950 | Body_part | denotes | helix | http://purl.obolibrary.org/obo/UBERON_0002488 |
sentences
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| TextSentencer_T1 | 0-85 | Sentence | denotes | Composite active site of chondroitin lyase ABC accepting both epimers of uronic acid. |
| TextSentencer_T2 | 86-159 | Sentence | denotes | Enzymes have evolved as catalysts with high degrees of stereospecificity. |
| TextSentencer_T3 | 160-302 | Sentence | denotes | When both enantiomers are biologically important, enzymes with two different folds usually catalyze reactions with the individual enantiomers. |
| TextSentencer_T4 | 303-438 | Sentence | denotes | In rare cases a single enzyme can process both enantiomers efficiently, but no molecular basis for such catalysis has been established. |
| TextSentencer_T5 | 439-509 | Sentence | denotes | The family of bacterial chondroitin lyases ABC comprises such enzymes. |
| TextSentencer_T6 | 510-794 | Sentence | denotes | They can degrade both chondroitin sulfate (CS) and dermatan sulfate (DS) glycosaminoglycans at the nonreducing end of either glucuronic acid (CS) or its epimer iduronic acid (DS) by a beta-elimination mechanism, which commences with the removal of the C-5 proton from the uronic acid. |
| TextSentencer_T7 | 795-1054 | Sentence | denotes | Two other structural folds evolved to perform these reactions in an epimer-specific fashion: (alpha/alpha)(5) for CS (chondroitin lyases AC) and beta-helix for DS (chondroitin lyases B); their catalytic mechanisms have been established at the molecular level. |
| TextSentencer_T8 | 1055-1308 | Sentence | denotes | The structure of chondroitinase ABC from Proteus vulgaris showed surprising similarity to chondroitinase AC, including the presence of a Tyr-His-Glu-Arg catalytic tetrad, which provided a possible mechanism for CS degradation but not for DS degradation. |
| TextSentencer_T9 | 1309-1497 | Sentence | denotes | We determined the structure of a distantly related Bacteroides thetaiotaomicron chondroitinase ABC to identify additional structurally conserved residues potentially involved in catalysis. |
| TextSentencer_T10 | 1498-1580 | Sentence | denotes | We found a conserved cluster located approximately 12 A from the catalytic tetrad. |
| TextSentencer_T11 | 1581-1673 | Sentence | denotes | We demonstrate that a histidine in this cluster is essential for catalysis of DS but not CS. |
| TextSentencer_T12 | 1674-1814 | Sentence | denotes | The enzyme utilizes a single substrate-binding site while having two partially overlapping active sites catalyzing the respective reactions. |
| TextSentencer_T13 | 1815-1981 | Sentence | denotes | The spatial separation of the two sets of residues suggests a substrate-induced conformational change that brings all catalytically essential residues close together. |
| T1 | 0-85 | Sentence | denotes | Composite active site of chondroitin lyase ABC accepting both epimers of uronic acid. |
| T2 | 86-159 | Sentence | denotes | Enzymes have evolved as catalysts with high degrees of stereospecificity. |
| T3 | 160-302 | Sentence | denotes | When both enantiomers are biologically important, enzymes with two different folds usually catalyze reactions with the individual enantiomers. |
| T4 | 303-438 | Sentence | denotes | In rare cases a single enzyme can process both enantiomers efficiently, but no molecular basis for such catalysis has been established. |
| T5 | 439-509 | Sentence | denotes | The family of bacterial chondroitin lyases ABC comprises such enzymes. |
| T6 | 510-794 | Sentence | denotes | They can degrade both chondroitin sulfate (CS) and dermatan sulfate (DS) glycosaminoglycans at the nonreducing end of either glucuronic acid (CS) or its epimer iduronic acid (DS) by a beta-elimination mechanism, which commences with the removal of the C-5 proton from the uronic acid. |
| T7 | 795-1054 | Sentence | denotes | Two other structural folds evolved to perform these reactions in an epimer-specific fashion: (alpha/alpha)(5) for CS (chondroitin lyases AC) and beta-helix for DS (chondroitin lyases B); their catalytic mechanisms have been established at the molecular level. |
| T8 | 1055-1308 | Sentence | denotes | The structure of chondroitinase ABC from Proteus vulgaris showed surprising similarity to chondroitinase AC, including the presence of a Tyr-His-Glu-Arg catalytic tetrad, which provided a possible mechanism for CS degradation but not for DS degradation. |
| T9 | 1309-1497 | Sentence | denotes | We determined the structure of a distantly related Bacteroides thetaiotaomicron chondroitinase ABC to identify additional structurally conserved residues potentially involved in catalysis. |
| T10 | 1498-1580 | Sentence | denotes | We found a conserved cluster located approximately 12 A from the catalytic tetrad. |
| T11 | 1581-1673 | Sentence | denotes | We demonstrate that a histidine in this cluster is essential for catalysis of DS but not CS. |
| T12 | 1674-1814 | Sentence | denotes | The enzyme utilizes a single substrate-binding site while having two partially overlapping active sites catalyzing the respective reactions. |
| T13 | 1815-1981 | Sentence | denotes | The spatial separation of the two sets of residues suggests a substrate-induced conformational change that brings all catalytically essential residues close together. |
| T1 | 0-85 | Sentence | denotes | Composite active site of chondroitin lyase ABC accepting both epimers of uronic acid. |
| T2 | 86-159 | Sentence | denotes | Enzymes have evolved as catalysts with high degrees of stereospecificity. |
| T3 | 160-302 | Sentence | denotes | When both enantiomers are biologically important, enzymes with two different folds usually catalyze reactions with the individual enantiomers. |
| T4 | 303-438 | Sentence | denotes | In rare cases a single enzyme can process both enantiomers efficiently, but no molecular basis for such catalysis has been established. |
| T5 | 439-509 | Sentence | denotes | The family of bacterial chondroitin lyases ABC comprises such enzymes. |
| T6 | 510-794 | Sentence | denotes | They can degrade both chondroitin sulfate (CS) and dermatan sulfate (DS) glycosaminoglycans at the nonreducing end of either glucuronic acid (CS) or its epimer iduronic acid (DS) by a beta-elimination mechanism, which commences with the removal of the C-5 proton from the uronic acid. |
| T7 | 795-1054 | Sentence | denotes | Two other structural folds evolved to perform these reactions in an epimer-specific fashion: (alpha/alpha)(5) for CS (chondroitin lyases AC) and beta-helix for DS (chondroitin lyases B); their catalytic mechanisms have been established at the molecular level. |
| T8 | 1055-1308 | Sentence | denotes | The structure of chondroitinase ABC from Proteus vulgaris showed surprising similarity to chondroitinase AC, including the presence of a Tyr-His-Glu-Arg catalytic tetrad, which provided a possible mechanism for CS degradation but not for DS degradation. |
| T9 | 1309-1497 | Sentence | denotes | We determined the structure of a distantly related Bacteroides thetaiotaomicron chondroitinase ABC to identify additional structurally conserved residues potentially involved in catalysis. |
| T10 | 1498-1580 | Sentence | denotes | We found a conserved cluster located approximately 12 A from the catalytic tetrad. |
| T11 | 1581-1673 | Sentence | denotes | We demonstrate that a histidine in this cluster is essential for catalysis of DS but not CS. |
| T12 | 1674-1814 | Sentence | denotes | The enzyme utilizes a single substrate-binding site while having two partially overlapping active sites catalyzing the respective reactions. |
| T13 | 1815-1981 | Sentence | denotes | The spatial separation of the two sets of residues suggests a substrate-induced conformational change that brings all catalytically essential residues close together. |
GlyCosmos15-Sentences
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 0-85 | Sentence | denotes | Composite active site of chondroitin lyase ABC accepting both epimers of uronic acid. |
| T2 | 86-159 | Sentence | denotes | Enzymes have evolved as catalysts with high degrees of stereospecificity. |
| T3 | 160-302 | Sentence | denotes | When both enantiomers are biologically important, enzymes with two different folds usually catalyze reactions with the individual enantiomers. |
| T4 | 303-438 | Sentence | denotes | In rare cases a single enzyme can process both enantiomers efficiently, but no molecular basis for such catalysis has been established. |
| T5 | 439-509 | Sentence | denotes | The family of bacterial chondroitin lyases ABC comprises such enzymes. |
| T6 | 510-794 | Sentence | denotes | They can degrade both chondroitin sulfate (CS) and dermatan sulfate (DS) glycosaminoglycans at the nonreducing end of either glucuronic acid (CS) or its epimer iduronic acid (DS) by a beta-elimination mechanism, which commences with the removal of the C-5 proton from the uronic acid. |
| T7 | 795-1054 | Sentence | denotes | Two other structural folds evolved to perform these reactions in an epimer-specific fashion: (alpha/alpha)(5) for CS (chondroitin lyases AC) and beta-helix for DS (chondroitin lyases B); their catalytic mechanisms have been established at the molecular level. |
| T8 | 1055-1308 | Sentence | denotes | The structure of chondroitinase ABC from Proteus vulgaris showed surprising similarity to chondroitinase AC, including the presence of a Tyr-His-Glu-Arg catalytic tetrad, which provided a possible mechanism for CS degradation but not for DS degradation. |
| T9 | 1309-1497 | Sentence | denotes | We determined the structure of a distantly related Bacteroides thetaiotaomicron chondroitinase ABC to identify additional structurally conserved residues potentially involved in catalysis. |
| T10 | 1498-1580 | Sentence | denotes | We found a conserved cluster located approximately 12 A from the catalytic tetrad. |
| T11 | 1581-1673 | Sentence | denotes | We demonstrate that a histidine in this cluster is essential for catalysis of DS but not CS. |
| T12 | 1674-1814 | Sentence | denotes | The enzyme utilizes a single substrate-binding site while having two partially overlapping active sites catalyzing the respective reactions. |
| T13 | 1815-1981 | Sentence | denotes | The spatial separation of the two sets of residues suggests a substrate-induced conformational change that brings all catalytically essential residues close together. |
GlyCosmos15-GlycoEpitope
| Id | Subject | Object | Predicate | Lexical cue | glycoepitope_id |
|---|---|---|---|---|---|
| T1 | 25-36 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | chondroitin | http://www.glycoepitope.jp/epitopes/EP0081 |
| T2 | 463-474 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | chondroitin | http://www.glycoepitope.jp/epitopes/EP0081 |
| T3 | 532-543 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | chondroitin | http://www.glycoepitope.jp/epitopes/EP0081 |
| T4 | 913-924 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | chondroitin | http://www.glycoepitope.jp/epitopes/EP0081 |
| T5 | 959-970 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | chondroitin | http://www.glycoepitope.jp/epitopes/EP0081 |
GlyCosmos15-NCBITAXON
| Id | Subject | Object | Predicate | Lexical cue | db_id |
|---|---|---|---|---|---|
| T1 | 1096-1112 | OrganismTaxon | denotes | Proteus vulgaris | 585 |
| T2 | 1360-1388 | OrganismTaxon | denotes | Bacteroides thetaiotaomicron | 818 |
GlyCosmos15-FMA
| Id | Subject | Object | Predicate | Lexical cue | db_id |
|---|---|---|---|---|---|
| T1 | 945-950 | Body_part | denotes | helix | FMA:60992 |
GlyCosmos15-Glycan
| Id | Subject | Object | Predicate | Lexical cue | image |
|---|---|---|---|---|---|
| T1 | 25-36 | Glycan | denotes | chondroitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT |
| T2 | 463-474 | Glycan | denotes | chondroitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT |
| T3 | 532-543 | Glycan | denotes | chondroitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT |
| T4 | 913-924 | Glycan | denotes | chondroitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT |
| T5 | 959-970 | Glycan | denotes | chondroitin | https://api.glycosmos.org/wurcs2image/latest/png/binary/G43702JT |
NCBITAXON
| Id | Subject | Object | Predicate | Lexical cue | db_id |
|---|---|---|---|---|---|
| T1 | 1096-1112 | OrganismTaxon | denotes | Proteus vulgaris | 585 |
| T2 | 1360-1388 | OrganismTaxon | denotes | Bacteroides thetaiotaomicron | 818 |
GlyCosmos-GlycoEpitope
| Id | Subject | Object | Predicate | Lexical cue | glycoepitope_id |
|---|---|---|---|---|---|
| T1 | 25-36 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | chondroitin | http://www.glycoepitope.jp/epitopes/EP0081 |
| T2 | 463-474 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | chondroitin | http://www.glycoepitope.jp/epitopes/EP0081 |
| T3 | 532-543 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | chondroitin | http://www.glycoepitope.jp/epitopes/EP0081 |
| T4 | 913-924 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | chondroitin | http://www.glycoepitope.jp/epitopes/EP0081 |
| T5 | 959-970 | http://purl.jp/bio/12/glyco/glycan#Glycan_epitope | denotes | chondroitin | http://www.glycoepitope.jp/epitopes/EP0081 |
Anatomy-UBERON
| Id | Subject | Object | Predicate | Lexical cue | uberon_id |
|---|---|---|---|---|---|
| T1 | 945-950 | Body_part | denotes | helix | http://purl.obolibrary.org/obo/UBERON_0002488 |