PubMed:10814825 JSONTXT

Annnotations TAB JSON ListView MergeView

    Oryza-OGER

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7-O-methyltransferase involved in the biosynthesis of the flavanone phytoalexin sakuranetin from rice (Oryza sativa L.).\nAn inducible S-adenosyl-L-methionine:naringenin 7-O-methyltransferase (NOMT) catalyzing the methylation of naringenin to sakuranetin, a major rice phytoalexin was purified approximately 985-fold from ultraviolet (UV)-irradiated rice leaves. The enzyme is not found in healthy tissues and was purified to a nearly homogeneous preparation in one step using adenosine-agarose affinity chromatography, with 1 g rice leaves (UV-irradiated) as starting material. Gel filtration chromatography resulted in an almost pure enzyme, as evidenced by a major band migrating to a position corresponding to a molecular mass of approximately 41 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified NOMT was strongly inhibited by Mn(2+), Ni(2+), Cu(2+), Zn(2+), Hg(2+), and Cd(2+), and to a low degree by Co(2+), Mg(2+), Ba(2+), Ca(2+) and ethylenediamine tetraacetic acid. The amino acid sequence of a NOMT cyanogen bromide (CNBr)-cleavage peptide was highly homologous to that of a caffeic acid 3-O-methyltransferase from maize, and about 70% of the amino acid sequence was obtained after sequencing the peptides generated by CNBr and/or formic acid hydrolysis. NOMT was also shown to be induced in a time-dependent manner, and purified from rice leaves treated with jasmonic acid and copper chloride."}

    OryzaGP_2021_v2

    {"project":"OryzaGP_2021_v2","denotations":[{"id":"T1","span":{"begin":203,"end":207},"obj":"http://identifiers.org/oryzabase.gene/10420"},{"id":"T2","span":{"begin":806,"end":809},"obj":"http://identifiers.org/oryzabase.gene/2454"},{"id":"T3","span":{"begin":840,"end":844},"obj":"http://identifiers.org/oryzabase.gene/10420"},{"id":"T4","span":{"begin":903,"end":905},"obj":"http://identifiers.org/oryzabase.gene/546"},{"id":"T5","span":{"begin":1044,"end":1048},"obj":"http://identifiers.org/oryzabase.gene/10420"},{"id":"T6","span":{"begin":1305,"end":1309},"obj":"http://identifiers.org/oryzabase.gene/10420"},{"id":"T55594","span":{"begin":203,"end":207},"obj":"http://identifiers.org/rapdb.locus/Os12g0240900"},{"id":"T92965","span":{"begin":840,"end":844},"obj":"http://identifiers.org/rapdb.locus/Os12g0240900"},{"id":"T95111","span":{"begin":1044,"end":1048},"obj":"http://identifiers.org/rapdb.locus/Os12g0240900"},{"id":"T27468","span":{"begin":1305,"end":1309},"obj":"http://identifiers.org/rapdb.locus/Os12g0240900"}],"text":"Naringenin 7-O-methyltransferase involved in the biosynthesis of the flavanone phytoalexin sakuranetin from rice (Oryza sativa L.).\nAn inducible S-adenosyl-L-methionine:naringenin 7-O-methyltransferase (NOMT) catalyzing the methylation of naringenin to sakuranetin, a major rice phytoalexin was purified approximately 985-fold from ultraviolet (UV)-irradiated rice leaves. The enzyme is not found in healthy tissues and was purified to a nearly homogeneous preparation in one step using adenosine-agarose affinity chromatography, with 1 g rice leaves (UV-irradiated) as starting material. Gel filtration chromatography resulted in an almost pure enzyme, as evidenced by a major band migrating to a position corresponding to a molecular mass of approximately 41 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified NOMT was strongly inhibited by Mn(2+), Ni(2+), Cu(2+), Zn(2+), Hg(2+), and Cd(2+), and to a low degree by Co(2+), Mg(2+), Ba(2+), Ca(2+) and ethylenediamine tetraacetic acid. The amino acid sequence of a NOMT cyanogen bromide (CNBr)-cleavage peptide was highly homologous to that of a caffeic acid 3-O-methyltransferase from maize, and about 70% of the amino acid sequence was obtained after sequencing the peptides generated by CNBr and/or formic acid hydrolysis. NOMT was also shown to be induced in a time-dependent manner, and purified from rice leaves treated with jasmonic acid and copper chloride."}

    21k_plant_trait_mention

    {"project":"21k_plant_trait_mention","denotations":[{"id":"M_28","span":{"begin":108,"end":112},"obj":"hunflair:NA:Species"},{"id":"M_29","span":{"begin":274,"end":278},"obj":"hunflair:NA:Species"},{"id":"M_30","span":{"begin":360,"end":364},"obj":"hunflair:NA:Species"},{"id":"M_31","span":{"begin":539,"end":543},"obj":"hunflair:NA:Species"},{"id":"M_32","span":{"begin":1385,"end":1389},"obj":"hunflair:NA:Species"},{"id":"M_0","span":{"begin":1410,"end":1418},"obj":"funRiceGene:9"},{"id":"M_1","span":{"begin":1428,"end":1434},"obj":"funRiceGene:192"},{"id":"M_2","span":{"begin":1410,"end":1423},"obj":"funRiceGene:387, 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7-O-methyltransferase involved in the biosynthesis of the flavanone phytoalexin sakuranetin from rice (Oryza sativa L.).\nAn inducible S-adenosyl-L-methionine:naringenin 7-O-methyltransferase (NOMT) catalyzing the methylation of naringenin to sakuranetin, a major rice phytoalexin was purified approximately 985-fold from ultraviolet (UV)-irradiated rice leaves. The enzyme is not found in healthy tissues and was purified to a nearly homogeneous preparation in one step using adenosine-agarose affinity chromatography, with 1 g rice leaves (UV-irradiated) as starting material. Gel filtration chromatography resulted in an almost pure enzyme, as evidenced by a major band migrating to a position corresponding to a molecular mass of approximately 41 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified NOMT was strongly inhibited by Mn(2+), Ni(2+), Cu(2+), Zn(2+), Hg(2+), and Cd(2+), and to a low degree by Co(2+), Mg(2+), Ba(2+), Ca(2+) and ethylenediamine tetraacetic acid. The amino acid sequence of a NOMT cyanogen bromide (CNBr)-cleavage peptide was highly homologous to that of a caffeic acid 3-O-methyltransferase from maize, and about 70% of the amino acid sequence was obtained after sequencing the peptides generated by CNBr and/or formic acid hydrolysis. NOMT was also shown to be induced in a time-dependent manner, and purified from rice leaves treated with jasmonic acid and copper chloride."}

    OryzaGP_2021

    {"project":"OryzaGP_2021","denotations":[{"id":"T1","span":{"begin":0,"end":32},"obj":"http://identifiers.org/oryzabase.gene/10420"},{"id":"T2","span":{"begin":182,"end":201},"obj":"http://identifiers.org/oryzabase.gene/20481"},{"id":"T3","span":{"begin":182,"end":201},"obj":"http://identifiers.org/oryzabase.gene/18240"},{"id":"T4","span":{"begin":182,"end":201},"obj":"http://identifiers.org/oryzabase.gene/16788"},{"id":"T5","span":{"begin":203,"end":207},"obj":"http://identifiers.org/oryzabase.gene/10420"},{"id":"T6","span":{"begin":806,"end":809},"obj":"http://identifiers.org/oryzabase.gene/2454"},{"id":"T7","span":{"begin":840,"end":844},"obj":"http://identifiers.org/oryzabase.gene/10420"},{"id":"T8","span":{"begin":887,"end":889},"obj":"http://identifiers.org/oryzabase.gene/9457"},{"id":"T9","span":{"begin":903,"end":905},"obj":"http://identifiers.org/oryzabase.gene/546"},{"id":"T10","span":{"begin":1044,"end":1048},"obj":"http://identifiers.org/oryzabase.gene/10420"},{"id":"T11","span":{"begin":1125,"end":1159},"obj":"http://identifiers.org/oryzabase.gene/7324"},{"id":"T12","span":{"begin":1305,"end":1309},"obj":"http://identifiers.org/oryzabase.gene/10420"},{"id":"T33162","span":{"begin":0,"end":32},"obj":"http://identifiers.org/ricegap/LOC_Os12g13810"},{"id":"T2022","span":{"begin":0,"end":32},"obj":"http://identifiers.org/ricegap/LOC_Os12g13800"},{"id":"T35839","span":{"begin":182,"end":201},"obj":"http://identifiers.org/ricegap/LOC_Os11g19840"},{"id":"T82955","span":{"begin":182,"end":201},"obj":"http://identifiers.org/ricegap/LOC_Os09g17560"},{"id":"T38396","span":{"begin":182,"end":201},"obj":"http://identifiers.org/ricegap/LOC_Os04g11970"},{"id":"T66521","span":{"begin":203,"end":207},"obj":"http://identifiers.org/ricegap/LOC_Os12g13810"},{"id":"T24038","span":{"begin":203,"end":207},"obj":"http://identifiers.org/ricegap/LOC_Os12g13800"},{"id":"T33251","span":{"begin":840,"end":844},"obj":"http://identifiers.org/ricegap/LOC_Os12g13810"},{"id":"T13563","span":{"begin":840,"end":844},"obj":"http://identifiers.org/ricegap/LOC_Os12g13800"},{"id":"T9415","span":{"begin":887,"end":889},"obj":"http://identifiers.org/ricegap/LOC_Os07g46990"},{"id":"T55235","span":{"begin":1044,"end":1048},"obj":"http://identifiers.org/ricegap/LOC_Os12g13810"},{"id":"T3978","span":{"begin":1044,"end":1048},"obj":"http://identifiers.org/ricegap/LOC_Os12g13800"},{"id":"T13","span":{"begin":1125,"end":1159},"obj":"http://identifiers.org/ricegap/LOC_Os08g06100"},{"id":"T14","span":{"begin":1305,"end":1309},"obj":"http://identifiers.org/ricegap/LOC_Os12g13810"},{"id":"T15","span":{"begin":1305,"end":1309},"obj":"http://identifiers.org/ricegap/LOC_Os12g13800"},{"id":"T43768","span":{"begin":0,"end":32},"obj":"http://identifiers.org/rapdb.locus/Os12g0240900"},{"id":"T96412","span":{"begin":182,"end":201},"obj":"http://identifiers.org/rapdb.locus/Os11g0303600"},{"id":"T56490","span":{"begin":182,"end":201},"obj":"http://identifiers.org/rapdb.locus/Os09g0344500"},{"id":"T96356","span":{"begin":182,"end":201},"obj":"http://identifiers.org/rapdb.locus/Os04g0196200"},{"id":"T57707","span":{"begin":203,"end":207},"obj":"http://identifiers.org/rapdb.locus/Os12g0240900"},{"id":"T76864","span":{"begin":840,"end":844},"obj":"http://identifiers.org/rapdb.locus/Os12g0240900"},{"id":"T2463","span":{"begin":887,"end":889},"obj":"http://identifiers.org/rapdb.locus/Os07g0665200"},{"id":"T67677","span":{"begin":1044,"end":1048},"obj":"http://identifiers.org/rapdb.locus/Os12g0240900"},{"id":"T25103","span":{"begin":1125,"end":1159},"obj":"http://identifiers.org/rapdb.locus/Os08g0157500"},{"id":"T6508","span":{"begin":1305,"end":1309},"obj":"http://identifiers.org/rapdb.locus/Os12g0240900"},{"id":"T20893","span":{"begin":0,"end":32},"obj":"http://identifiers.org/uniprot/Q0IP69"},{"id":"T87519","span":{"begin":0,"end":32},"obj":"http://identifiers.org/uniprot/I2FFE9"},{"id":"T49438","span":{"begin":182,"end":201},"obj":"http://identifiers.org/uniprot/Q53QK5"},{"id":"T5445","span":{"begin":182,"end":201},"obj":"http://identifiers.org/uniprot/Q01MZ9"},{"id":"T10050","span":{"begin":182,"end":201},"obj":"http://identifiers.org/uniprot/B4FLE0"},{"id":"T46095","span":{"begin":203,"end":207},"obj":"http://identifiers.org/uniprot/Q0IP69"},{"id":"T86046","span":{"begin":203,"end":207},"obj":"http://identifiers.org/uniprot/I2FFE9"},{"id":"T47751","span":{"begin":840,"end":844},"obj":"http://identifiers.org/uniprot/Q0IP69"},{"id":"T43469","span":{"begin":840,"end":844},"obj":"http://identifiers.org/uniprot/I2FFE9"},{"id":"T21318","span":{"begin":887,"end":889},"obj":"http://identifiers.org/uniprot/P28757"},{"id":"T99668","span":{"begin":1044,"end":1048},"obj":"http://identifiers.org/uniprot/Q0IP69"},{"id":"T23826","span":{"begin":1044,"end":1048},"obj":"http://identifiers.org/uniprot/I2FFE9"},{"id":"T55348","span":{"begin":1125,"end":1159},"obj":"http://identifiers.org/uniprot/Q6ZD89"},{"id":"T25766","span":{"begin":1305,"end":1309},"obj":"http://identifier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7-O-methyltransferase involved in the biosynthesis of the flavanone phytoalexin sakuranetin from rice (Oryza sativa L.).\nAn inducible S-adenosyl-L-methionine:naringenin 7-O-methyltransferase (NOMT) catalyzing the methylation of naringenin to sakuranetin, a major rice phytoalexin was purified approximately 985-fold from ultraviolet (UV)-irradiated rice leaves. The enzyme is not found in healthy tissues and was purified to a nearly homogeneous preparation in one step using adenosine-agarose affinity chromatography, with 1 g rice leaves (UV-irradiated) as starting material. Gel filtration chromatography resulted in an almost pure enzyme, as evidenced by a major band migrating to a position corresponding to a molecular mass of approximately 41 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified NOMT was strongly inhibited by Mn(2+), Ni(2+), Cu(2+), Zn(2+), Hg(2+), and Cd(2+), and to a low degree by Co(2+), Mg(2+), Ba(2+), Ca(2+) and ethylenediamine tetraacetic acid. The amino acid sequence of a NOMT cyanogen bromide (CNBr)-cleavage peptide was highly homologous to that of a caffeic acid 3-O-methyltransferase from maize, and about 70% of the amino acid sequence was obtained after sequencing the peptides generated by CNBr and/or formic acid hydrolysis. NOMT was also shown to be induced in a time-dependent manner, and purified from rice leaves treated with jasmonic acid and copper chloride."}

    OryzaGP_2022

    {"project":"OryzaGP_2022","denotations":[{"id":"T1","span":{"begin":0,"end":32},"obj":"http://identifiers.org/oryzabase.gene/10420"},{"id":"T2","span":{"begin":182,"end":201},"obj":"http://identifiers.org/oryzabase.gene/18240"},{"id":"T3","span":{"begin":182,"end":201},"obj":"http://identifiers.org/oryzabase.gene/16788"},{"id":"T4","span":{"begin":535,"end":536},"obj":"http://identifiers.org/oryzabase.gene/11216"},{"id":"T5","span":{"begin":1140,"end":1159},"obj":"http://identifiers.org/oryzabase.gene/18240"},{"id":"T6","span":{"begin":1140,"end":1159},"obj":"http://identifiers.org/oryzabase.gene/16788"}],"text":"Naringenin 7-O-methyltransferase involved in the biosynthesis of the flavanone phytoalexin sakuranetin from rice (Oryza sativa L.).\nAn inducible S-adenosyl-L-methionine:naringenin 7-O-methyltransferase (NOMT) catalyzing the methylation of naringenin to sakuranetin, a major rice phytoalexin was purified approximately 985-fold from ultraviolet (UV)-irradiated rice leaves. The enzyme is not found in healthy tissues and was purified to a nearly homogeneous preparation in one step using adenosine-agarose affinity chromatography, with 1 g rice leaves (UV-irradiated) as starting material. Gel filtration chromatography resulted in an almost pure enzyme, as evidenced by a major band migrating to a position corresponding to a molecular mass of approximately 41 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified NOMT was strongly inhibited by Mn(2+), Ni(2+), Cu(2+), Zn(2+), Hg(2+), and Cd(2+), and to a low degree by Co(2+), Mg(2+), Ba(2+), Ca(2+) and ethylenediamine tetraacetic acid. The amino acid sequence of a NOMT cyanogen bromide (CNBr)-cleavage peptide was highly homologous to that of a caffeic acid 3-O-methyltransferase from maize, and about 70% of the amino acid sequence was obtained after sequencing the peptides generated by CNBr and/or formic acid hydrolysis. NOMT was also shown to be induced in a time-dependent manner, and purified from rice leaves treated with jasmonic acid and copper chloride."}

    pqqtest_sentence

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7-O-methyltransferase involved in the biosynthesis of the flavanone phytoalexin sakuranetin from rice (Oryza sativa L.).\nAn inducible S-adenosyl-L-methionine:naringenin 7-O-methyltransferase (NOMT) catalyzing the methylation of naringenin to sakuranetin, a major rice phytoalexin was purified approximately 985-fold from ultraviolet (UV)-irradiated rice leaves. The enzyme is not found in healthy tissues and was purified to a nearly homogeneous preparation in one step using adenosine-agarose affinity chromatography, with 1 g rice leaves (UV-irradiated) as starting material. Gel filtration chromatography resulted in an almost pure enzyme, as evidenced by a major band migrating to a position corresponding to a molecular mass of approximately 41 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified NOMT was strongly inhibited by Mn(2+), Ni(2+), Cu(2+), Zn(2+), Hg(2+), and Cd(2+), and to a low degree by Co(2+), Mg(2+), Ba(2+), Ca(2+) and ethylenediamine tetraacetic acid. The amino acid sequence of a NOMT cyanogen bromide (CNBr)-cleavage peptide was highly homologous to that of a caffeic acid 3-O-methyltransferase from maize, and about 70% of the amino acid sequence was obtained after sequencing the peptides generated by CNBr and/or formic acid hydrolysis. NOMT was also shown to be induced in a time-dependent manner, and purified from rice leaves treated with jasmonic acid and copper chloride."}

    OryzaGP_2021_FLAIR

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The enzyme is not found in healthy tissues and was purified to a nearly homogeneous preparation in one step using adenosine-agarose affinity chromatography, with 1 g rice leaves (UV-irradiated) as starting material. Gel filtration chromatography resulted in an almost pure enzyme, as evidenced by a major band migrating to a position corresponding to a molecular mass of approximately 41 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The purified NOMT was strongly inhibited by Mn(2+), Ni(2+), Cu(2+), Zn(2+), Hg(2+), and Cd(2+), and to a low degree by Co(2+), Mg(2+), Ba(2+), Ca(2+) and ethylenediamine tetraacetic acid. The amino acid sequence of a NOMT cyanogen bromide (CNBr)-cleavage peptide was highly homologous to that of a caffeic acid 3-O-methyltransferase from maize, and about 70% of the amino acid sequence was obtained after sequencing the peptides generated by CNBr and/or formic acid hydrolysis. NOMT was also shown to be induced in a time-dependent manner, and purified from rice leaves treated with jasmonic acid and copper chloride."}