PubMed:22418094 JSONTXT

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    OryzaGP_2021

    {"project":"OryzaGP_2021","denotations":[{"id":"T1","span":{"begin":5,"end":10},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T2","span":{"begin":122,"end":127},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T3","span":{"begin":611,"end":616},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T4","span":{"begin":809,"end":814},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T5","span":{"begin":856,"end":861},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T6","span":{"begin":1010,"end":1015},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T7","span":{"begin":1022,"end":1027},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T8","span":{"begin":1966,"end":1971},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T51362","span":{"begin":5,"end":10},"obj":"http://identifiers.org/ricegap/LOC_Os03g49600"},{"id":"T64297","span":{"begin":122,"end":127},"obj":"http://identifiers.org/ricegap/LOC_Os03g49600"},{"id":"T54381","span":{"begin":611,"end":616},"obj":"http://identifiers.org/ricegap/LOC_Os03g49600"},{"id":"T13491","span":{"begin":809,"end":814},"obj":"http://identifiers.org/ricegap/LOC_Os03g49600"},{"id":"T42588","span":{"begin":856,"end":861},"obj":"http://identifiers.org/ricegap/LOC_Os03g49600"},{"id":"T59195","span":{"begin":1010,"end":1015},"obj":"http://identifiers.org/ricegap/LOC_Os03g49600"},{"id":"T85201","span":{"begin":1022,"end":1027},"obj":"http://identifiers.org/ricegap/LOC_Os03g49600"},{"id":"T69044","span":{"begin":1966,"end":1971},"obj":"http://identifiers.org/ricegap/LOC_Os03g49600"},{"id":"T22731","span":{"begin":5,"end":10},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T60932","span":{"begin":122,"end":127},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T63517","span":{"begin":611,"end":616},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T89176","span":{"begin":809,"end":814},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T51058","span":{"begin":856,"end":861},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T34076","span":{"begin":1010,"end":1015},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T84135","span":{"begin":1022,"end":1027},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T70694","span":{"begin":1966,"end":1971},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T48399","span":{"begin":5,"end":10},"obj":"http://identifiers.org/uniprot/Q75I93"},{"id":"T61073","span":{"begin":122,"end":127},"obj":"http://identifiers.org/uniprot/Q75I93"},{"id":"T36009","span":{"begin":611,"end":616},"obj":"http://identifiers.org/uniprot/Q75I93"},{"id":"T72053","span":{"begin":809,"end":814},"obj":"http://identifiers.org/uniprot/Q75I93"},{"id":"T81949","span":{"begin":856,"end":861},"obj":"http://identifiers.org/uniprot/Q75I93"},{"id":"T69830","span":{"begin":1010,"end":1015},"obj":"http://identifiers.org/uniprot/Q75I93"},{"id":"T35305","span":{"begin":1022,"end":1027},"obj":"http://identifiers.org/uniprot/Q75I93"},{"id":"T90337","span":{"begin":1966,"end":1971},"obj":"http://identifiers.org/uniprot/Q75I93"},{"id":"M_0","span":{"begin":247,"end":274},"obj":"hunflair:NA:Chemical"},{"id":"M_1","span":{"begin":1471,"end":1490},"obj":"hunflair:NA:Chemical"},{"id":"M_2","span":{"begin":86,"end":100},"obj":"hunflair:NA:Chemical"},{"id":"M_3","span":{"begin":912,"end":926},"obj":"hunflair:NA:Chemical"},{"id":"M_4","span":{"begin":345,"end":360},"obj":"hunflair:NA:Chemical"},{"id":"M_5","span":{"begin":531,"end":538},"obj":"hunflair:NA:Chemical"},{"id":"M_6","span":{"begin":671,"end":678},"obj":"hunflair:NA:Chemical"},{"id":"M_7","span":{"begin":700,"end":707},"obj":"hunflair:NA:Chemical"},{"id":"M_8","span":{"begin":721,"end":728},"obj":"hunflair:NA:Chemical"},{"id":"M_9","span":{"begin":758,"end":765},"obj":"hunflair:NA:Chemical"},{"id":"M_10","span":{"begin":1678,"end":1685},"obj":"hunflair:NA:Chemical"},{"id":"M_11","span":{"begin":1326,"end":1347},"obj":"hunflair:NA:Chemical"},{"id":"M_12","span":{"begin":688,"end":707},"obj":"hunflair:NA:Chemical"},{"id":"M_13","span":{"begin":1353,"end":1373},"obj":"hunflair:NA:Chemical"},{"id":"M_14","span":{"begin":220,"end":241},"obj":"hunflair:NA:Chemical"},{"id":"M_15","span":{"begin":1657,"end":1667},"obj":"hunflair:NA:Chemical"},{"id":"M_16","span":{"begin":1254,"end":1277},"obj":"hunflair:NA:Chemical"},{"id":"M_17","span":{"begin":507,"end":529},"obj":"hunflair:NA:Chemical"},{"id":"M_18","span":{"begin":1542,"end":1573},"obj":"hunflair:NA:Chemical"},{"id":"M_19","span":{"begin":1687,"end":1712},"obj":"hunflair:NA:Chemical"},{"id":"M_20","span":{"begin":292,"end":305},"obj":"hunflair:NA:Chemical"},{"id":"M_21","span":{"begin":1301,"end":1324},"obj":"hunflair:NA:Chemical"},{"id":"M_22","span":{"begin":1718,"end":1740},"obj":"hunflair:NA:Chemical"},{"id":"M_23","span":{"begin":0,"end":4},"obj":"hunflair:NA:Species"},{"id":"M_24","span":{"begin":1017,"end":1021},"obj":"hunflair:NA:Species"},{"id":"M_25","span":{"begin":611,"end":630},"obj":"hunflair:NA:Gene"},{"id":"M_26","span":{"begin":856,"end":875},"obj":"hunflair:NA:Gene"},{"id":"M_27","span":{"begin":1017,"end":1035},"obj":"hunflair:NA:Gene"},{"id":"M_28","span":{"begin":312,"end":324},"obj":"hunflair:NA:Chemical"},{"id":"M_29","span":{"begin":117,"end":121},"obj":"hunflair:NA:Species"},{"id":"M_30","span":{"begin":5,"end":10},"obj":"hunflair:NA:Gene"},{"id":"M_31","span":{"begin":122,"end":127},"obj":"hunflair:NA:Gene"},{"id":"M_32","span":{"begin":611,"end":616},"obj":"hunflair:NA:Gene"},{"id":"M_33","span":{"begin":809,"end":814},"obj":"hunflair:NA:Gene"},{"id":"M_34","span":{"begin":856,"end":861},"obj":"hunflair:NA:Gene"},{"id":"M_35","span":{"begin":1010,"end":1015},"obj":"hunflair:NA:Gene"},{"id":"M_36","span":{"begin":1022,"end":1027},"obj":"hunflair:NA:Gene"},{"id":"M_37","span":{"begin":1966,"end":1971},"obj":"hunflair:NA:Gene"},{"id":"M_38","span":{"begin":494,"end":501},"obj":"hunflair:NA:Chemical"},{"id":"M_39","span":{"begin":1669,"end":1676},"obj":"hunflair:NA:Chemical"},{"id":"M_40","span":{"begin":1976,"end":1991},"obj":"hunflair:NA:Gene"},{"id":"M_41","span":{"begin":1028,"end":1035},"obj":"hunflair:NA:Gene"},{"id":"M_42","span":{"begin":1195,"end":1202},"obj":"hunflair:NA:Gene"},{"id":"M_43","span":{"begin":307,"end":310},"obj":"hunflair:NA:Chemical"},{"id":"M_44","span":{"begin":331,"end":334},"obj":"hunflair:NA:Chemical"},{"id":"M_45","span":{"begin":469,"end":472},"obj":"hunflair:NA:Chemical"},{"id":"M_46","span":{"begin":498,"end":501},"obj":"hunflair:NA:Chemical"},{"id":"M_47","span":{"begin":507,"end":510},"obj":"hunflair:NA:Chemical"},{"id":"M_48","span":{"begin":535,"end":538},"obj":"hunflair:NA:Chemical"},{"id":"M_49","span":{"begin":543,"end":546},"obj":"hunflair:NA:Chemical"},{"id":"M_50","span":{"begin":675,"end":678},"obj":"hunflair:NA:Chemical"},{"id":"M_51","span":{"begin":704,"end":707},"obj":"hunflair:NA:Chemical"},{"id":"M_52","span":{"begin":725,"end":728},"obj":"hunflair:NA:Chemical"},{"id":"M_53","span":{"begin":762,"end":765},"obj":"hunflair:NA:Chemical"},{"id":"M_54","span":{"begin":1389,"end":1392},"obj":"hunflair:NA:Chemical"},{"id":"M_55","span":{"begin":1673,"end":1676},"obj":"hunflair:NA:Chemical"},{"id":"M_56","span":{"begin":1682,"end":1685},"obj":"hunflair:NA:Chemical"},{"id":"M_57","span":{"begin":1687,"end":1690},"obj":"hunflair:NA:Chemical"},{"id":"M_58","span":{"begin":1718,"end":1721},"obj":"hunflair:NA:Chemical"},{"id":"M_59","span":{"begin":1766,"end":1769},"obj":"hunflair:NA:Chemical"},{"id":"M_60","span":{"begin":469,"end":492},"obj":"hunflair:NA:Chemical"},{"id":"M_61","span":{"begin":442,"end":448},"obj":"hunflair:NA:Gene"},{"id":"M_62","span":{"begin":1812,"end":1828},"obj":"hunflair:NA:Chemical"},{"id":"M_63","span":{"begin":734,"end":765},"obj":"hunflair:NA:Chemical"},{"id":"M_64","span":{"begin":563,"end":569},"obj":"hunflair:NA:Chemical"},{"id":"M_65","span":{"begin":326,"end":334},"obj":"hunflair:NA:Chemical"},{"id":"M_66","span":{"begin":1384,"end":1392},"obj":"hunflair:NA:Chemical"},{"id":"M_67","span":{"begin":709,"end":728},"obj":"hunflair:NA:Chemical"},{"id":"M_68","span":{"begin":746,"end":765},"obj":"hunflair:NA:Chemical"},{"id":"M_69","span":{"begin":122,"end":143},"obj":"hunflair:NA:Gene"},{"id":"M_70","span":{"begin":1448,"end":1466},"obj":"hunflair:NA:Chemical"},{"id":"M_71","span":{"begin":11,"end":24},"obj":"hunflair:NA:Gene"},{"id":"M_72","span":{"begin":174,"end":187},"obj":"hunflair:NA:Gene"},{"id":"M_73","span":{"begin":823,"end":836},"obj":"hunflair:NA:Gene"},{"id":"M_74","span":{"begin":952,"end":965},"obj":"hunflair:NA:Gene"},{"id":"M_75","span":{"begin":1111,"end":1124},"obj":"hunflair:NA:Gene"},{"id":"M_76","span":{"begin":1595,"end":1608},"obj":"hunflair:NA:Gene"},{"id":"M_77","span":{"begin":1978,"end":1991},"obj":"hunflair:NA:Gene"},{"id":"M_78","span":{"begin":276,"end":280},"obj":"hunflair:NA:Chemical"},{"id":"M_79","span":{"begin":662,"end":666},"obj":"hunflair:NA:Chemical"},{"id":"M_80","span":{"begin":1248,"end":1252},"obj":"hunflair:NA:Chemical"},{"id":"M_81","span":{"begin":1634,"end":1638},"obj":"hunflair:NA:Chemical"},{"id":"M_82","span":{"begin":1225,"end":1242},"obj":"hunflair:NA:Chemical"},{"id":"M_83","span":{"begin":551,"end":558},"obj":"hunflair:NA:Chemical"},{"id":"M_84","span":{"begin":1621,"end":1628},"obj":"hunflair:NA:Chemical"},{"id":"M_85","span":{"begin":1648,"end":1655},"obj":"hunflair:NA:Chemical"},{"id":"M_86","span":{"begin":1279,"end":1299},"obj":"hunflair:NA:Chemical"},{"id":"M_87","span":{"begin":1766,"end":1789},"obj":"hunflair:NA:Chemical"},{"id":"M_88","span":{"begin":0,"end":24},"obj":"hunflair:NA:Gene"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    OryzaGP_2021_v2

    {"project":"OryzaGP_2021_v2","denotations":[{"id":"T1","span":{"begin":5,"end":10},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T2","span":{"begin":122,"end":127},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T3","span":{"begin":611,"end":616},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T4","span":{"begin":809,"end":814},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T5","span":{"begin":856,"end":861},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T6","span":{"begin":1010,"end":1015},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T7","span":{"begin":1022,"end":1027},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T8","span":{"begin":1966,"end":1971},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T318","span":{"begin":5,"end":10},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T46596","span":{"begin":122,"end":127},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T43560","span":{"begin":611,"end":616},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T91385","span":{"begin":809,"end":814},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T35465","span":{"begin":856,"end":861},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T59900","span":{"begin":1010,"end":1015},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T33665","span":{"begin":1022,"end":1027},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T14517","span":{"begin":1966,"end":1971},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    OryzaGP_2022

    {"project":"OryzaGP_2022","denotations":[{"id":"T1","span":{"begin":695,"end":696},"obj":"http://identifiers.org/oryzabase.gene/11216"},{"id":"T2","span":{"begin":716,"end":717},"obj":"http://identifiers.org/oryzabase.gene/11216"},{"id":"T3","span":{"begin":741,"end":742},"obj":"http://identifiers.org/oryzabase.gene/11216"},{"id":"T4","span":{"begin":753,"end":754},"obj":"http://identifiers.org/oryzabase.gene/11216"},{"id":"T5","span":{"begin":1545,"end":1546},"obj":"http://identifiers.org/oryzabase.gene/11216"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    GlyCosmos6-Glycan-Motif-Image

    {"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":551,"end":558},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":563,"end":569},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":1621,"end":1628},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":1648,"end":1655},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G15021LG"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G82576YO"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G15021LG"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G15021LG"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    GlyCosmos6-Glycan-Motif-Structure

    {"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":551,"end":558},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"},{"id":"T2","span":{"begin":563,"end":569},"obj":"https://glytoucan.org/Structures/Glycans/G82576YO"},{"id":"T3","span":{"begin":1621,"end":1628},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"},{"id":"T4","span":{"begin":1648,"end":1655},"obj":"https://glytoucan.org/Structures/Glycans/G15021LG"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    OryzaGP_2021_FLAIR

    {"project":"OryzaGP_2021_FLAIR","denotations":[{"id":"M_0","span":{"begin":247,"end":274},"obj":"hunflair:NA:Chemical"},{"id":"M_1","span":{"begin":1471,"end":1490},"obj":"hunflair:NA:Chemical"},{"id":"M_2","span":{"begin":86,"end":100},"obj":"hunflair:NA:Chemical"},{"id":"M_3","span":{"begin":912,"end":926},"obj":"hunflair:NA:Chemical"},{"id":"M_4","span":{"begin":345,"end":360},"obj":"hunflair:NA:Chemical"},{"id":"M_5","span":{"begin":531,"end":538},"obj":"hunflair:NA:Chemical"},{"id":"M_6","span":{"begin":671,"end":678},"obj":"hunflair:NA:Chemical"},{"id":"M_7","span":{"begin":700,"end":707},"obj":"hunflair:NA:Chemical"},{"id":"M_8","span":{"begin":721,"end":728},"obj":"hunflair:NA:Chemical"},{"id":"M_9","span":{"begin":758,"end":765},"obj":"hunflair:NA:Chemical"},{"id":"M_10","span":{"begin":1678,"end":1685},"obj":"hunflair:NA:Chemical"},{"id":"M_11","span":{"begin":1326,"end":1347},"obj":"hunflair:NA:Chemical"},{"id":"M_12","span":{"begin":688,"end":707},"obj":"hunflair:NA:Chemical"},{"id":"M_13","span":{"begin":1353,"end":1373},"obj":"hunflair:NA:Chemical"},{"id":"M_14","span":{"begin":220,"end":241},"obj":"hunflair:NA:Chemical"},{"id":"M_15","span":{"begin":1657,"end":1667},"obj":"hunflair:NA:Chemical"},{"id":"M_16","span":{"begin":1254,"end":1277},"obj":"hunflair:NA:Chemical"},{"id":"M_17","span":{"begin":507,"end":529},"obj":"hunflair:NA:Chemical"},{"id":"M_18","span":{"begin":1542,"end":1573},"obj":"hunflair:NA:Chemical"},{"id":"M_19","span":{"begin":1687,"end":1712},"obj":"hunflair:NA:Chemical"},{"id":"M_20","span":{"begin":292,"end":305},"obj":"hunflair:NA:Chemical"},{"id":"M_21","span":{"begin":1301,"end":1324},"obj":"hunflair:NA:Chemical"},{"id":"M_22","span":{"begin":1718,"end":1740},"obj":"hunflair:NA:Chemical"},{"id":"M_23","span":{"begin":0,"end":4},"obj":"hunflair:NA:Species"},{"id":"M_24","span":{"begin":1017,"end":1021},"obj":"hunflair:NA:Species"},{"id":"M_25","span":{"begin":611,"end":630},"obj":"hunflair:NA:Gene"},{"id":"M_26","span":{"begin":856,"end":875},"obj":"hunflair:NA:Gene"},{"id":"M_27","span":{"begin":1017,"end":1035},"obj":"hunflair:NA:Gene"},{"id":"M_28","span":{"begin":312,"end":324},"obj":"hunflair:NA:Chemical"},{"id":"M_29","span":{"begin":117,"end":121},"obj":"hunflair:NA:Species"},{"id":"M_30","span":{"begin":5,"end":10},"obj":"hunflair:NA:Gene"},{"id":"M_31","span":{"begin":122,"end":127},"obj":"hunflair:NA:Gene"},{"id":"M_32","span":{"begin":611,"end":616},"obj":"hunflair:NA:Gene"},{"id":"M_33","span":{"begin":809,"end":814},"obj":"hunflair:NA:Gene"},{"id":"M_34","span":{"begin":856,"end":861},"obj":"hunflair:NA:Gene"},{"id":"M_35","span":{"begin":1010,"end":1015},"obj":"hunflair:NA:Gene"},{"id":"M_36","span":{"begin":1022,"end":1027},"obj":"hunflair:NA:Gene"},{"id":"M_37","span":{"begin":1966,"end":1971},"obj":"hunflair:NA:Gene"},{"id":"M_38","span":{"begin":494,"end":501},"obj":"hunflair:NA:Chemical"},{"id":"M_39","span":{"begin":1669,"end":1676},"obj":"hunflair:NA:Chemical"},{"id":"M_40","span":{"begin":1976,"end":1991},"obj":"hunflair:NA:Gene"},{"id":"M_41","span":{"begin":1028,"end":1035},"obj":"hunflair:NA:Gene"},{"id":"M_42","span":{"begin":1195,"end":1202},"obj":"hunflair:NA:Gene"},{"id":"M_43","span":{"begin":307,"end":310},"obj":"hunflair:NA:Chemical"},{"id":"M_44","span":{"begin":331,"end":334},"obj":"hunflair:NA:Chemical"},{"id":"M_45","span":{"begin":469,"end":472},"obj":"hunflair:NA:Chemical"},{"id":"M_46","span":{"begin":498,"end":501},"obj":"hunflair:NA:Chemical"},{"id":"M_47","span":{"begin":507,"end":510},"obj":"hunflair:NA:Chemical"},{"id":"M_48","span":{"begin":535,"end":538},"obj":"hunflair:NA:Chemical"},{"id":"M_49","span":{"begin":543,"end":546},"obj":"hunflair:NA:Chemical"},{"id":"M_50","span":{"begin":675,"end":678},"obj":"hunflair:NA:Chemical"},{"id":"M_51","span":{"begin":704,"end":707},"obj":"hunflair:NA:Chemical"},{"id":"M_52","span":{"begin":725,"end":728},"obj":"hunflair:NA:Chemical"},{"id":"M_53","span":{"begin":762,"end":765},"obj":"hunflair:NA:Chemical"},{"id":"M_54","span":{"begin":1389,"end":1392},"obj":"hunflair:NA:Chemical"},{"id":"M_55","span":{"begin":1673,"end":1676},"obj":"hunflair:NA:Chemical"},{"id":"M_56","span":{"begin":1682,"end":1685},"obj":"hunflair:NA:Chemical"},{"id":"M_57","span":{"begin":1687,"end":1690},"obj":"hunflair:NA:Chemical"},{"id":"M_58","span":{"begin":1718,"end":1721},"obj":"hunflair:NA:Chemical"},{"id":"M_59","span":{"begin":1766,"end":1769},"obj":"hunflair:NA:Chemical"},{"id":"M_60","span":{"begin":469,"end":492},"obj":"hunflair:NA:Chemical"},{"id":"M_61","span":{"begin":442,"end":448},"obj":"hunflair:NA:Gene"},{"id":"M_62","span":{"begin":1812,"end":1828},"obj":"hunflair:NA:Chemical"},{"id":"M_63","span":{"begin":734,"end":765},"obj":"hunflair:NA:Chemical"},{"id":"M_64","span":{"begin":563,"end":569},"obj":"hunflair:NA:Chemical"},{"id":"M_65","span":{"begin":326,"end":334},"obj":"hunflair:NA:Chemical"},{"id":"M_66","span":{"begin":1384,"end":1392},"obj":"hunflair:NA:Chemical"},{"id":"M_67","span":{"begin":709,"end":728},"obj":"hunflair:NA:Chemical"},{"id":"M_68","span":{"begin":746,"end":765},"obj":"hunflair:NA:Chemical"},{"id":"M_69","span":{"begin":122,"end":143},"obj":"hunflair:NA:Gene"},{"id":"M_70","span":{"begin":1448,"end":1466},"obj":"hunflair:NA:Chemical"},{"id":"M_71","span":{"begin":11,"end":24},"obj":"hunflair:NA:Gene"},{"id":"M_72","span":{"begin":174,"end":187},"obj":"hunflair:NA:Gene"},{"id":"M_73","span":{"begin":823,"end":836},"obj":"hunflair:NA:Gene"},{"id":"M_74","span":{"begin":952,"end":965},"obj":"hunflair:NA:Gene"},{"id":"M_75","span":{"begin":1111,"end":1124},"obj":"hunflair:NA:Gene"},{"id":"M_76","span":{"begin":1595,"end":1608},"obj":"hunflair:NA:Gene"},{"id":"M_77","span":{"begin":1978,"end":1991},"obj":"hunflair:NA:Gene"},{"id":"M_78","span":{"begin":276,"end":280},"obj":"hunflair:NA:Chemical"},{"id":"M_79","span":{"begin":662,"end":666},"obj":"hunflair:NA:Chemical"},{"id":"M_80","span":{"begin":1248,"end":1252},"obj":"hunflair:NA:Chemical"},{"id":"M_81","span":{"begin":1634,"end":1638},"obj":"hunflair:NA:Chemical"},{"id":"M_82","span":{"begin":1225,"end":1242},"obj":"hunflair:NA:Chemical"},{"id":"M_83","span":{"begin":551,"end":558},"obj":"hunflair:NA:Chemical"},{"id":"M_84","span":{"begin":1621,"end":1628},"obj":"hunflair:NA:Chemical"},{"id":"M_85","span":{"begin":1648,"end":1655},"obj":"hunflair:NA:Chemical"},{"id":"M_86","span":{"begin":1279,"end":1299},"obj":"hunflair:NA:Chemical"},{"id":"M_87","span":{"begin":1766,"end":1789},"obj":"hunflair:NA:Chemical"},{"id":"M_88","span":{"begin":0,"end":24},"obj":"hunflair:NA:Gene"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    Allie

    {"project":"Allie","denotations":[{"id":"SS1_22418094_1_0","span":{"begin":247,"end":274},"obj":"expanded"},{"id":"SS2_22418094_1_0","span":{"begin":276,"end":280},"obj":"abbr"},{"id":"SS1_22418094_1_1","span":{"begin":292,"end":305},"obj":"expanded"},{"id":"SS2_22418094_1_1","span":{"begin":307,"end":310},"obj":"abbr"},{"id":"SS1_22418094_2_0","span":{"begin":469,"end":492},"obj":"expanded"},{"id":"SS2_22418094_2_0","span":{"begin":494,"end":501},"obj":"abbr"},{"id":"SS1_22418094_2_1","span":{"begin":507,"end":529},"obj":"expanded"},{"id":"SS2_22418094_2_1","span":{"begin":531,"end":538},"obj":"abbr"}],"relations":[{"id":"AE1_22418094_1_0","pred":"abbreviatedTo","subj":"SS1_22418094_1_0","obj":"SS2_22418094_1_0"},{"id":"AE1_22418094_1_1","pred":"abbreviatedTo","subj":"SS1_22418094_1_1","obj":"SS2_22418094_1_1"},{"id":"AE1_22418094_2_0","pred":"abbreviatedTo","subj":"SS1_22418094_2_0","obj":"SS2_22418094_2_0"},{"id":"AE1_22418094_2_1","pred":"abbreviatedTo","subj":"SS1_22418094_2_1","obj":"SS2_22418094_2_1"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    sentences

    {"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":112},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":113,"end":371},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":372,"end":631},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":632,"end":837},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":838,"end":1016},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1017,"end":1194},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1195,"end":1402},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1403,"end":1574},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1575,"end":1790},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1791,"end":1888},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1889,"end":2012},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":112},"obj":"Sentence"},{"id":"T2","span":{"begin":113,"end":371},"obj":"Sentence"},{"id":"T3","span":{"begin":372,"end":631},"obj":"Sentence"},{"id":"T4","span":{"begin":632,"end":837},"obj":"Sentence"},{"id":"T5","span":{"begin":838,"end":1016},"obj":"Sentence"},{"id":"T6","span":{"begin":1017,"end":1194},"obj":"Sentence"},{"id":"T7","span":{"begin":1195,"end":1402},"obj":"Sentence"},{"id":"T8","span":{"begin":1403,"end":1574},"obj":"Sentence"},{"id":"T9","span":{"begin":1575,"end":1790},"obj":"Sentence"},{"id":"T10","span":{"begin":1791,"end":1888},"obj":"Sentence"},{"id":"T11","span":{"begin":1889,"end":2012},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    mondo_disease

    {"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":339,"end":344},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0013662"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    Glycan-GlyCosmos

    {"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":1657,"end":1667},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G55560AP"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G55560AP"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    GlyCosmos15-MONDO

    {"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":339,"end":344},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0013662"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    GlyCosmos15-NCBITAXON

    {"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":0,"end":4},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":117,"end":121},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1017,"end":1021},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"4530"},{"id":"A2","pred":"db_id","subj":"T2","obj":"4530"},{"id":"A3","pred":"db_id","subj":"T3","obj":"4530"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    GlyCosmos15-UBERON

    {"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":1089,"end":1093},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0001137"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    sentences

    {"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":112},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":113,"end":371},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":372,"end":631},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":632,"end":837},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":838,"end":1016},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1017,"end":1194},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1195,"end":1402},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1403,"end":1574},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1575,"end":1790},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1791,"end":1888},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1889,"end":2012},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":112},"obj":"Sentence"},{"id":"T2","span":{"begin":113,"end":371},"obj":"Sentence"},{"id":"T3","span":{"begin":372,"end":631},"obj":"Sentence"},{"id":"T4","span":{"begin":632,"end":837},"obj":"Sentence"},{"id":"T5","span":{"begin":838,"end":1016},"obj":"Sentence"},{"id":"T6","span":{"begin":1017,"end":1194},"obj":"Sentence"},{"id":"T7","span":{"begin":1195,"end":1402},"obj":"Sentence"},{"id":"T8","span":{"begin":1403,"end":1574},"obj":"Sentence"},{"id":"T9","span":{"begin":1575,"end":1790},"obj":"Sentence"},{"id":"T10","span":{"begin":1791,"end":1888},"obj":"Sentence"},{"id":"T11","span":{"begin":1889,"end":2012},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    GlyCosmos15-Sentences

    {"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":112},"obj":"Sentence"},{"id":"T2","span":{"begin":113,"end":371},"obj":"Sentence"},{"id":"T3","span":{"begin":372,"end":631},"obj":"Sentence"},{"id":"T4","span":{"begin":632,"end":837},"obj":"Sentence"},{"id":"T5","span":{"begin":838,"end":1016},"obj":"Sentence"},{"id":"T6","span":{"begin":1017,"end":1194},"obj":"Sentence"},{"id":"T7","span":{"begin":1195,"end":1402},"obj":"Sentence"},{"id":"T8","span":{"begin":1403,"end":1574},"obj":"Sentence"},{"id":"T9","span":{"begin":1575,"end":1790},"obj":"Sentence"},{"id":"T10","span":{"begin":1791,"end":1888},"obj":"Sentence"},{"id":"T11","span":{"begin":1889,"end":2012},"obj":"Sentence"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    GlyCosmos15-Glycan

    {"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":1657,"end":1667},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G55560AP"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G55560AP"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    NCBITAXON

    {"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":0,"end":4},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":117,"end":121},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1017,"end":1021},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"4530"},{"id":"A2","pred":"db_id","subj":"T2","obj":"4530"},{"id":"A3","pred":"db_id","subj":"T3","obj":"4530"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}

    Anatomy-UBERON

    {"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":1089,"end":1093},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0001137"}],"text":"Rice BGlu1 glycosynthase and wild type transglycosylation activities distinguished by cyclophellitol inhibition.\nThe rice BGlu1 β-D-glucosidase nucleophile mutant E386G is a glycosynthase that catalyzes the synthesis of cellooligosaccharides from α-d-glucopyranosyl fluoride (GlcF) donor and p-nitrophenyl (pNP) cellobioside (Glc2-pNP) or cello-oligosaccharide acceptors. When activity with other donors and acceptors was tested, the initial enzyme preparation cleaved pNP-β-D-glucopyranoside (Glc-pNP) and pNP-β-D-fucopyranoside (Fuc-pNP) to pNP and glucose and fucose, suggesting contamination with wild type BGlu1 β-glucosidase. The products from reaction of GlcF and Fuc-pNP included Fuc-β-(1→3)-Fuc-pNP, Glc-β-(1→3)-Fuc-pNP, and Fuc-β-(1→4)-Glc-β-(1→3)-Fuc-pNP, suggesting the presence of both wild type BGlu1 and its glycosynthase. Inhibition of the BGlu1 β-glucosidase activity within this preparation by cyclophellitol confirmed that the E386G glycosynthase preparation was contaminated with wild type BGlu1. Rice BGlu1 E386G-2, generated from a new construct designed to minimize back-mutation, showed glycosynthase activity without wild type hydrolytic or transglycosylation activity. E386G-2 catalyzed transfer of glycosyl residues from GlcF, α-L-arabinosyl fluoride, α-D-fucosyl fluoride, α-D-galactosyl fluoride, α-D-mannosyl fluoride, and α-D-xylosyl fluoride donors to Glc2-pNP acceptor. The synthetic products from the reactions of α-fucosyl fluoride and α-mannosyl fluoride donors were confirmed to result from addition of a β-(1→4)-linked glycosyl residue. Moreover, the E386G glycosynthase transferred glucose from GlcF donor to glucose, cellobiose, Glc-pNP, Fuc-pNP, pNP-β-D-galactopyranoside, and pNP-β-D-xylopyranoside acceptors, but little to pNP-β-D-mannopyranoside. Production of longer oligosaccharides occurred most readily on acceptors with an equatorial 4-OH. Elimination of wild type contamination thereby allowed a clear assessment of BGlu1 E386G glycosynthase catalytic abilities."}