PubMed:26582607
Annnotations
Glycan-Motif
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 363-369 | https://glytoucan.org/Structures/Glycans/G82576YO | denotes | fucose |
GlyCosmos6-Glycan-Motif-Image
Id | Subject | Object | Predicate | Lexical cue | image |
---|---|---|---|---|---|
T1 | 363-369 | Glycan_Motif | denotes | fucose | https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G82576YO |
GlyCosmos6-Glycan-Motif-Structure
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 363-369 | https://glytoucan.org/Structures/Glycans/G82576YO | denotes | fucose |
sentences
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
TextSentencer_T1 | 0-71 | Sentence | denotes | Design of an α-l-transfucosidase for the synthesis of fucosylated HMOs. |
TextSentencer_T2 | 72-172 | Sentence | denotes | Human milk oligosaccharides (HMOs) are recognized as benefiting breast-fed infants in multiple ways. |
TextSentencer_T3 | 173-271 | Sentence | denotes | As a result, there is growing interest in the synthesis of HMOs mimicking their natural diversity. |
TextSentencer_T4 | 272-408 | Sentence | denotes | Most HMOs are fucosylated oligosaccharides. α-l-Fucosidases catalyze the hydrolysis of α-l-fucose from the non-reducing end of a glucan. |
TextSentencer_T5 | 409-471 | Sentence | denotes | They fall into the glycoside hydrolase GH29 and GH95 families. |
TextSentencer_T6 | 472-591 | Sentence | denotes | The GH29 family fucosidases display a classic retaining mechanism and are good candidates for transfucosidase activity. |
TextSentencer_T7 | 592-782 | Sentence | denotes | We recently demonstrated that the α-l-fucosidase from Thermotoga maritima (TmαFuc) from the GH29 family can be evolved into an efficient transfucosidase by directed evolution ( Osanjo et al. |
TextSentencer_T8 | 783-789 | Sentence | denotes | 2007). |
TextSentencer_T9 | 790-991 | Sentence | denotes | In this work, we developed semi-rational approaches to design an α-l-transfucosidase starting with the α-l-fucosidase from commensal bacteria Bifidobacterium longum subsp. infantis (BiAfcB, Blon_2336). |
TextSentencer_T10 | 992-1215 | Sentence | denotes | Efficient fucosylation was obtained with enzyme mutants (L321P-BiAfcB and F34I/L321P-BiAfcB) enabling in vitro synthesis of lactodifucotetraose, lacto-N-fucopentaose II, lacto-N-fucopentaose III and lacto-N-difucohexaose I. |
TextSentencer_T11 | 1216-1393 | Sentence | denotes | The enzymes also generated more complex HMOs like fucosylated para-lacto-N-neohexaose (F-p-LNnH) and mono- or difucosylated lacto-N-neohexaose (F-LNnH-I, F-LNnH-II and DF-LNnH). |
TextSentencer_T12 | 1394-1619 | Sentence | denotes | It is worth noting that mutation at these two positions did not result in a strong decrease in the overall activity of the enzyme, which makes these variants interesting candidates for large-scale transfucosylation reactions. |
TextSentencer_T13 | 1620-1736 | Sentence | denotes | For the first time, this work provides an efficient enzymatic method to synthesize the majority of fucosylated HMOs. |
T1 | 0-71 | Sentence | denotes | Design of an α-l-transfucosidase for the synthesis of fucosylated HMOs. |
T2 | 72-172 | Sentence | denotes | Human milk oligosaccharides (HMOs) are recognized as benefiting breast-fed infants in multiple ways. |
T3 | 173-271 | Sentence | denotes | As a result, there is growing interest in the synthesis of HMOs mimicking their natural diversity. |
T4 | 272-408 | Sentence | denotes | Most HMOs are fucosylated oligosaccharides. α-l-Fucosidases catalyze the hydrolysis of α-l-fucose from the non-reducing end of a glucan. |
T5 | 409-471 | Sentence | denotes | They fall into the glycoside hydrolase GH29 and GH95 families. |
T6 | 472-591 | Sentence | denotes | The GH29 family fucosidases display a classic retaining mechanism and are good candidates for transfucosidase activity. |
T7 | 592-782 | Sentence | denotes | We recently demonstrated that the α-l-fucosidase from Thermotoga maritima (TmαFuc) from the GH29 family can be evolved into an efficient transfucosidase by directed evolution ( Osanjo et al. |
T8 | 783-789 | Sentence | denotes | 2007). |
T9 | 790-991 | Sentence | denotes | In this work, we developed semi-rational approaches to design an α-l-transfucosidase starting with the α-l-fucosidase from commensal bacteria Bifidobacterium longum subsp. infantis (BiAfcB, Blon_2336). |
T10 | 992-1393 | Sentence | denotes | Efficient fucosylation was obtained with enzyme mutants (L321P-BiAfcB and F34I/L321P-BiAfcB) enabling in vitro synthesis of lactodifucotetraose, lacto-N-fucopentaose II, lacto-N-fucopentaose III and lacto-N-difucohexaose I. The enzymes also generated more complex HMOs like fucosylated para-lacto-N-neohexaose (F-p-LNnH) and mono- or difucosylated lacto-N-neohexaose (F-LNnH-I, F-LNnH-II and DF-LNnH). |
T11 | 1394-1619 | Sentence | denotes | It is worth noting that mutation at these two positions did not result in a strong decrease in the overall activity of the enzyme, which makes these variants interesting candidates for large-scale transfucosylation reactions. |
T12 | 1620-1736 | Sentence | denotes | For the first time, this work provides an efficient enzymatic method to synthesize the majority of fucosylated HMOs. |
T1 | 0-71 | Sentence | denotes | Design of an α-l-transfucosidase for the synthesis of fucosylated HMOs. |
T2 | 72-172 | Sentence | denotes | Human milk oligosaccharides (HMOs) are recognized as benefiting breast-fed infants in multiple ways. |
T3 | 173-271 | Sentence | denotes | As a result, there is growing interest in the synthesis of HMOs mimicking their natural diversity. |
T4 | 272-408 | Sentence | denotes | Most HMOs are fucosylated oligosaccharides. α-l-Fucosidases catalyze the hydrolysis of α-l-fucose from the non-reducing end of a glucan. |
T5 | 409-471 | Sentence | denotes | They fall into the glycoside hydrolase GH29 and GH95 families. |
T6 | 472-591 | Sentence | denotes | The GH29 family fucosidases display a classic retaining mechanism and are good candidates for transfucosidase activity. |
T7 | 592-782 | Sentence | denotes | We recently demonstrated that the α-l-fucosidase from Thermotoga maritima (TmαFuc) from the GH29 family can be evolved into an efficient transfucosidase by directed evolution ( Osanjo et al. |
T8 | 783-789 | Sentence | denotes | 2007). |
T9 | 790-991 | Sentence | denotes | In this work, we developed semi-rational approaches to design an α-l-transfucosidase starting with the α-l-fucosidase from commensal bacteria Bifidobacterium longum subsp. infantis (BiAfcB, Blon_2336). |
T10 | 992-1215 | Sentence | denotes | Efficient fucosylation was obtained with enzyme mutants (L321P-BiAfcB and F34I/L321P-BiAfcB) enabling in vitro synthesis of lactodifucotetraose, lacto-N-fucopentaose II, lacto-N-fucopentaose III and lacto-N-difucohexaose I. |
T11 | 1216-1393 | Sentence | denotes | The enzymes also generated more complex HMOs like fucosylated para-lacto-N-neohexaose (F-p-LNnH) and mono- or difucosylated lacto-N-neohexaose (F-LNnH-I, F-LNnH-II and DF-LNnH). |
T12 | 1394-1619 | Sentence | denotes | It is worth noting that mutation at these two positions did not result in a strong decrease in the overall activity of the enzyme, which makes these variants interesting candidates for large-scale transfucosylation reactions. |
T13 | 1620-1736 | Sentence | denotes | For the first time, this work provides an efficient enzymatic method to synthesize the majority of fucosylated HMOs. |
ICD10
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 414-418 | http://purl.bioontology.org/ontology/ICD10/W00-W19.9 | denotes | fall |
GlycoBiology-FMA
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
_T1 | 78-82 | FMAID:165676 | denotes | milk |
_T2 | 83-99 | FMAID:196731 | denotes | oligosaccharides |
_T3 | 83-99 | FMAID:82742 | denotes | oligosaccharides |
_T4 | 136-142 | FMAID:9601 | denotes | breast |
_T5 | 136-142 | FMAID:97486 | denotes | breast |
_T6 | 298-314 | FMAID:82742 | denotes | oligosaccharides |
_T7 | 298-314 | FMAID:196731 | denotes | oligosaccharides |
_T8 | 363-369 | FMAID:82790 | denotes | fucose |
_T9 | 363-369 | FMAID:196784 | denotes | fucose |
uniprot-human
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 1384-1386 | http://www.uniprot.org/uniprot/P00746 | denotes | DF |
GlycoBiology-NCBITAXON
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 379-382 | http://purl.bioontology.org/ontology/NCBITAXON/604139 | denotes | non |
T2 | 528-537 | http://purl.bioontology.org/ontology/NCBITAXON/127244 | denotes | mechanism |
T3 | 646-656 | http://purl.bioontology.org/ontology/NCBITAXON/2335 | denotes | Thermotoga |
T4 | 646-656 | http://purl.bioontology.org/ontology/NCBITAXON/188709 | denotes | Thermotoga |
T5 | 646-656 | http://purl.bioontology.org/ontology/NCBITAXON/188708 | denotes | Thermotoga |
T6 | 646-656 | http://purl.bioontology.org/ontology/NCBITAXON/200918 | denotes | Thermotoga |
T7 | 646-665 | http://purl.bioontology.org/ontology/NCBITAXON/2336 | denotes | Thermotoga maritima |
T8 | 923-931 | http://purl.bioontology.org/ontology/NCBITAXON/629395 | denotes | bacteria |
T9 | 923-931 | http://purl.bioontology.org/ontology/NCBITAXON/2 | denotes | bacteria |
T10 | 923-954 | http://purl.bioontology.org/ontology/NCBITAXON/767694 | denotes | bacteria Bifidobacterium longum |
T11 | 923-960 | http://purl.bioontology.org/ontology/NCBITAXON/77635 | denotes | bacteria Bifidobacterium longum subsp |
T12 | 932-947 | http://purl.bioontology.org/ontology/NCBITAXON/1685 | denotes | Bifidobacterium |
T13 | 932-947 | http://purl.bioontology.org/ontology/NCBITAXON/78448 | denotes | Bifidobacterium |
T14 | 932-947 | http://purl.bioontology.org/ontology/NCBITAXON/78345 | denotes | Bifidobacterium |
T15 | 932-947 | http://purl.bioontology.org/ontology/NCBITAXON/35760 | denotes | Bifidobacterium |
T16 | 932-947 | http://purl.bioontology.org/ontology/NCBITAXON/1691 | denotes | Bifidobacterium |
T17 | 932-947 | http://purl.bioontology.org/ontology/NCBITAXON/78344 | denotes | Bifidobacterium |
T18 | 932-947 | http://purl.bioontology.org/ontology/NCBITAXON/180216 | denotes | Bifidobacterium |
T19 | 932-947 | http://purl.bioontology.org/ontology/NCBITAXON/78342 | denotes | Bifidobacterium |
T20 | 932-947 | http://purl.bioontology.org/ontology/NCBITAXON/1689 | denotes | Bifidobacterium |
T21 | 932-947 | http://purl.bioontology.org/ontology/NCBITAXON/41200 | denotes | Bifidobacterium |
T22 | 932-947 | http://purl.bioontology.org/ontology/NCBITAXON/638617 | denotes | Bifidobacterium |
T23 | 932-947 | http://purl.bioontology.org/ontology/NCBITAXON/85004 | denotes | Bifidobacterium |
T24 | 932-947 | http://purl.bioontology.org/ontology/NCBITAXON/1683 | denotes | Bifidobacterium |
T25 | 932-947 | http://purl.bioontology.org/ontology/NCBITAXON/1681 | denotes | Bifidobacterium |
T26 | 932-947 | http://purl.bioontology.org/ontology/NCBITAXON/471511 | denotes | Bifidobacterium |
T27 | 932-954 | http://purl.bioontology.org/ontology/NCBITAXON/216816 | denotes | Bifidobacterium longum |
T28 | 1278-1282 | http://purl.bioontology.org/ontology/NCBITAXON/507091 | denotes | para |
T29 | 1278-1282 | http://purl.bioontology.org/ontology/NCBITAXON/218705 | denotes | para |
GO-BP
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 41-50 | http://purl.obolibrary.org/obo/GO_0009058 | denotes | synthesis |
T2 | 219-228 | http://purl.obolibrary.org/obo/GO_0009058 | denotes | synthesis |
T3 | 1103-1112 | http://purl.obolibrary.org/obo/GO_0009058 | denotes | synthesis |
T4 | 54-65 | http://purl.obolibrary.org/obo/GO_0036065 | denotes | fucosylated |
T5 | 286-297 | http://purl.obolibrary.org/obo/GO_0036065 | denotes | fucosylated |
T6 | 1266-1277 | http://purl.obolibrary.org/obo/GO_0036065 | denotes | fucosylated |
T7 | 1002-1014 | http://purl.obolibrary.org/obo/GO_0036065 | denotes | fucosylation |
T8 | 776-778 | http://purl.obolibrary.org/obo/GO_0004306 | denotes | et |
T9 | 807-816 | http://purl.obolibrary.org/obo/GO_0032502 | denotes | developed |
T10 | 913-922 | http://purl.obolibrary.org/obo/GO_0085031 | denotes | commensal |
T11 | 1501-1523 | http://purl.obolibrary.org/obo/GO_0003824 | denotes | activity of the enzyme |
UBERON-AE
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
T1 | 78-82 | http://purl.obolibrary.org/obo/UBERON_0001913 | denotes | milk |
T2 | 136-142 | http://purl.obolibrary.org/obo/UBERON_0000310 | denotes | breast |
T3 | 1585-1590 | http://purl.obolibrary.org/obo/UBERON_0002542 | denotes | scale |
Lectin
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
Lectin_T1 | 779-781 | https://acgg.asia/db/lfdb/LfDB0344 | denotes | al |
GlyTouCan-IUPAC
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
GlycanIUPAC_T1 | 379-382 | "http://rdf.glycoinfo.org/glycan/G02780QX" | denotes | non |
GlycanIUPAC_T2 | 379-382 | "http://rdf.glycoinfo.org/glycan/G18425DX" | denotes | non |
GlycanIUPAC_T3 | 379-382 | "http://rdf.glycoinfo.org/glycan/G18630JE" | denotes | non |
GlycanIUPAC_T4 | 379-382 | "http://rdf.glycoinfo.org/glycan/G01004IT" | denotes | non |
GlycanIUPAC_T5 | 379-382 | "http://rdf.glycoinfo.org/glycan/G87301QZ" | denotes | non |
GlycanIUPAC_T6 | 379-382 | "http://rdf.glycoinfo.org/glycan/G39790GW" | denotes | non |
GlycanIUPAC_T7 | 379-382 | "http://rdf.glycoinfo.org/glycan/G42928BB" | denotes | non |
GlycanIUPAC_T8 | 379-382 | "http://rdf.glycoinfo.org/glycan/G51134HC" | denotes | non |
GlycanIUPAC_T9 | 379-382 | "http://rdf.glycoinfo.org/glycan/G68183GR" | denotes | non |
GlycanIUPAC_T10 | 379-382 | "http://rdf.glycoinfo.org/glycan/G46883FA" | denotes | non |
GlycanIUPAC_T11 | 379-382 | "http://rdf.glycoinfo.org/glycan/G54702VY" | denotes | non |
performance-test
Id | Subject | Object | Predicate | Lexical cue |
---|---|---|---|---|
PD-UBERON-AE-B_T1 | 78-82 | http://purl.obolibrary.org/obo/UBERON_0001913 | denotes | milk |
PD-UBERON-AE-B_T2 | 136-142 | http://purl.obolibrary.org/obo/UBERON_0000310 | denotes | breast |
PD-UBERON-AE-B_T3 | 1585-1590 | http://purl.obolibrary.org/obo/UBERON_0002542 | denotes | scale |
NCBITAXON
Id | Subject | Object | Predicate | Lexical cue | db_id |
---|---|---|---|---|---|
T1 | 72-77 | OrganismTaxon | denotes | Human | 9606 |
T2 | 646-665 | OrganismTaxon | denotes | Thermotoga maritima | 2336 |
T3 | 923-931 | OrganismTaxon | denotes | bacteria | 2|629395 |
T5 | 932-970 | OrganismTaxon | denotes | Bifidobacterium longum subsp. infantis | 1682 |
Anatomy-UBERON
Id | Subject | Object | Predicate | Lexical cue | uberon_id |
---|---|---|---|---|---|
T1 | 78-82 | Body_part | denotes | milk | http://purl.obolibrary.org/obo/UBERON_0001913 |
T2 | 136-142 | Body_part | denotes | breast | http://purl.obolibrary.org/obo/UBERON_0000310 |
T3 | 1585-1590 | Body_part | denotes | scale | http://purl.obolibrary.org/obo/UBERON_0002542 |