PubMed:22341501 JSON TXT

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OryzaGP_2022

{"project":"OryzaGP_2022","denotations":[{"id":"T1","span":{"begin":196,"end":197},"obj":"http://identifiers.org/oryzabase.gene/11216"},{"id":"T2","span":{"begin":371,"end":372},"obj":"http://identifiers.org/oryzabase.gene/11216"}],"text":"Exchanging a single amino acid residue generates or weakens a +2 cellooligosaccharide binding subsite in rice β-glucosidases.\nOs3BGlu6, Os3BGlu7, and Os4BGlu12 are rice glycoside hydrolase family 1 β-glucosidases, the structures of which have been solved by X-ray crystallography. In complex structures, Os3BGlu7 residue Asn245 hydrogen bonds to the second sugar in the +1 subsite for laminaribiose and the third sugar in the +2 subsite for cellotetraose and cellopentaose. The corresponding Os3BGlu6 residue, Met251, appears to block the binding of cellooligosaccharides at the +2 subsite, whereas His252 in this position in Os4BGlu12 could hydrogen bond to oligosaccharides. Mutation of Os3BGlu6 Met251 to Asn resulted in a 15-fold increased k(cat)/K(m) value for hydrolysis of laminaribiose compared to wild type Os3BGlu6 and 9 to 24-fold increases for cellooligosaccharides with degrees of polymerization (DP) of 2-5. On the other hand, mutation of Os3BGlu7 Asn245 to Met decreased the k(cat)/K(m) of hydrolysis by 6.5-fold for laminaribiose and 17 to 30-fold for cellooligosaccharides with DP \u003e2, while mutation of Os4BGlu12 His252 to Met decreased the corresponding k(cat)/K(m) values 2 to 6-fold."}

sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":125},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":126,"end":280},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":281,"end":473},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":474,"end":676},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":677,"end":921},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":922,"end":1203},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":125},"obj":"Sentence"},{"id":"T2","span":{"begin":126,"end":280},"obj":"Sentence"},{"id":"T3","span":{"begin":281,"end":473},"obj":"Sentence"},{"id":"T4","span":{"begin":474,"end":676},"obj":"Sentence"},{"id":"T5","span":{"begin":677,"end":921},"obj":"Sentence"},{"id":"T6","span":{"begin":922,"end":1203},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Exchanging a single amino acid residue generates or weakens a +2 cellooligosaccharide binding subsite in rice β-glucosidases.\nOs3BGlu6, Os3BGlu7, and Os4BGlu12 are rice glycoside hydrolase family 1 β-glucosidases, the structures of which have been solved by X-ray crystallography. In complex structures, Os3BGlu7 residue Asn245 hydrogen bonds to the second sugar in the +1 subsite for laminaribiose and the third sugar in the +2 subsite for cellotetraose and cellopentaose. The corresponding Os3BGlu6 residue, Met251, appears to block the binding of cellooligosaccharides at the +2 subsite, whereas His252 in this position in Os4BGlu12 could hydrogen bond to oligosaccharides. Mutation of Os3BGlu6 Met251 to Asn resulted in a 15-fold increased k(cat)/K(m) value for hydrolysis of laminaribiose compared to wild type Os3BGlu6 and 9 to 24-fold increases for cellooligosaccharides with degrees of polymerization (DP) of 2-5. On the other hand, mutation of Os3BGlu7 Asn245 to Met decreased the k(cat)/K(m) of hydrolysis by 6.5-fold for laminaribiose and 17 to 30-fold for cellooligosaccharides with DP \u003e2, while mutation of Os4BGlu12 His252 to Met decreased the corresponding k(cat)/K(m) values 2 to 6-fold."}

Glycosmos6-MAT

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":935,"end":939},"obj":"http://purl.obolibrary.org/obo/MAT_0000091"}],"text":"Exchanging a single amino acid residue generates or weakens a +2 cellooligosaccharide binding subsite in rice β-glucosidases.\nOs3BGlu6, Os3BGlu7, and Os4BGlu12 are rice glycoside hydrolase family 1 β-glucosidases, the structures of which have been solved by X-ray crystallography. In complex structures, Os3BGlu7 residue Asn245 hydrogen bonds to the second sugar in the +1 subsite for laminaribiose and the third sugar in the +2 subsite for cellotetraose and cellopentaose. The corresponding Os3BGlu6 residue, Met251, appears to block the binding of cellooligosaccharides at the +2 subsite, whereas His252 in this position in Os4BGlu12 could hydrogen bond to oligosaccharides. Mutation of Os3BGlu6 Met251 to Asn resulted in a 15-fold increased k(cat)/K(m) value for hydrolysis of laminaribiose compared to wild type Os3BGlu6 and 9 to 24-fold increases for cellooligosaccharides with degrees of polymerization (DP) of 2-5. On the other hand, mutation of Os3BGlu7 Asn245 to Met decreased the k(cat)/K(m) of hydrolysis by 6.5-fold for laminaribiose and 17 to 30-fold for cellooligosaccharides with DP \u003e2, while mutation of Os4BGlu12 His252 to Met decreased the corresponding k(cat)/K(m) values 2 to 6-fold."}

OryzaGP_2021_v2

{"project":"OryzaGP_2021_v2","denotations":[{"id":"T1","span":{"begin":126,"end":134},"obj":"http://identifiers.org/oryzabase.gene/12080"},{"id":"T2","span":{"begin":136,"end":144},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T3","span":{"begin":150,"end":159},"obj":"http://identifiers.org/oryzabase.gene/12085"},{"id":"T4","span":{"begin":304,"end":312},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T5","span":{"begin":492,"end":500},"obj":"http://identifiers.org/oryzabase.gene/12080"},{"id":"T6","span":{"begin":626,"end":635},"obj":"http://identifiers.org/oryzabase.gene/12085"},{"id":"T7","span":{"begin":689,"end":697},"obj":"http://identifiers.org/oryzabase.gene/12080"},{"id":"T8","span":{"begin":816,"end":824},"obj":"http://identifiers.org/oryzabase.gene/12080"},{"id":"T9","span":{"begin":910,"end":912},"obj":"http://identifiers.org/oryzabase.gene/847"},{"id":"T10","span":{"begin":953,"end":961},"obj":"http://identifiers.org/oryzabase.gene/12081"},{"id":"T11","span":{"begin":1095,"end":1100},"obj":"http://identifiers.org/oryzabase.gene/868"},{"id":"T12","span":{"begin":1120,"end":1129},"obj":"http://identifiers.org/oryzabase.gene/12085"},{"id":"T10237","span":{"begin":126,"end":134},"obj":"http://identifiers.org/rapdb.locus/Os03g0212800"},{"id":"T47089","span":{"begin":136,"end":144},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T83828","span":{"begin":150,"end":159},"obj":"http://identifiers.org/rapdb.locus/Os04g0474800"},{"id":"T2878","span":{"begin":304,"end":312},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T87331","span":{"begin":492,"end":500},"obj":"http://identifiers.org/rapdb.locus/Os03g0212800"},{"id":"T6334","span":{"begin":626,"end":635},"obj":"http://identifiers.org/rapdb.locus/Os04g0474800"},{"id":"T7648","span":{"begin":689,"end":697},"obj":"http://identifiers.org/rapdb.locus/Os03g0212800"},{"id":"T73335","span":{"begin":816,"end":824},"obj":"http://identifiers.org/rapdb.locus/Os03g0212800"},{"id":"T96081","span":{"begin":953,"end":961},"obj":"http://identifiers.org/rapdb.locus/Os03g0703000"},{"id":"T17394","span":{"begin":1120,"end":1129},"obj":"http://identifiers.org/rapdb.locus/Os04g0474800"}],"text":"Exchanging a single amino acid residue generates or weakens a +2 cellooligosaccharide binding subsite in rice β-glucosidases.\nOs3BGlu6, Os3BGlu7, and Os4BGlu12 are rice glycoside hydrolase family 1 β-glucosidases, the structures of which have been solved by X-ray crystallography. In complex structures, Os3BGlu7 residue Asn245 hydrogen bonds to the second sugar in the +1 subsite for laminaribiose and the third sugar in the +2 subsite for cellotetraose and cellopentaose. The corresponding Os3BGlu6 residue, Met251, appears to block the binding of cellooligosaccharides at the +2 subsite, whereas His252 in this position in Os4BGlu12 could hydrogen bond to oligosaccharides. Mutation of Os3BGlu6 Met251 to Asn resulted in a 15-fold increased k(cat)/K(m) value for hydrolysis of laminaribiose compared to wild type Os3BGlu6 and 9 to 24-fold increases for cellooligosaccharides with degrees of polymerization (DP) of 2-5. On the other hand, mutation of Os3BGlu7 Asn245 to Met decreased the k(cat)/K(m) of hydrolysis by 6.5-fold for laminaribiose and 17 to 30-fold for cellooligosaccharides with DP \u003e2, while mutation of Os4BGlu12 His252 to Met decreased the corresponding k(cat)/K(m) values 2 to 6-fold."}

OryzaGP_2021_FLAIR

OryzaGP_2021

Allie

{"project":"Allie","denotations":[{"id":"SS1_22341501_4_0","span":{"begin":883,"end":908},"obj":"expanded"},{"id":"SS2_22341501_4_0","span":{"begin":910,"end":912},"obj":"abbr"}],"relations":[{"id":"AE1_22341501_4_0","pred":"abbreviatedTo","subj":"SS1_22341501_4_0","obj":"SS2_22341501_4_0"}],"text":"Exchanging a single amino acid residue generates or weakens a +2 cellooligosaccharide binding subsite in rice β-glucosidases.\nOs3BGlu6, Os3BGlu7, and Os4BGlu12 are rice glycoside hydrolase family 1 β-glucosidases, the structures of which have been solved by X-ray crystallography. In complex structures, Os3BGlu7 residue Asn245 hydrogen bonds to the second sugar in the +1 subsite for laminaribiose and the third sugar in the +2 subsite for cellotetraose and cellopentaose. The corresponding Os3BGlu6 residue, Met251, appears to block the binding of cellooligosaccharides at the +2 subsite, whereas His252 in this position in Os4BGlu12 could hydrogen bond to oligosaccharides. Mutation of Os3BGlu6 Met251 to Asn resulted in a 15-fold increased k(cat)/K(m) value for hydrolysis of laminaribiose compared to wild type Os3BGlu6 and 9 to 24-fold increases for cellooligosaccharides with degrees of polymerization (DP) of 2-5. On the other hand, mutation of Os3BGlu7 Asn245 to Met decreased the k(cat)/K(m) of hydrolysis by 6.5-fold for laminaribiose and 17 to 30-fold for cellooligosaccharides with DP \u003e2, while mutation of Os4BGlu12 His252 to Met decreased the corresponding k(cat)/K(m) values 2 to 6-fold."}

OryzaGP

{"project":"OryzaGP","denotations":[{"id":"T1","span":{"begin":304,"end":312},"obj":"gene"},{"id":"T2","span":{"begin":492,"end":500},"obj":"gene"},{"id":"T3","span":{"begin":626,"end":635},"obj":"gene"}],"text":"Exchanging a single amino acid residue generates or weakens a +2 cellooligosaccharide binding subsite in rice β-glucosidases.\nOs3BGlu6, Os3BGlu7, and Os4BGlu12 are rice glycoside hydrolase family 1 β-glucosidases, the structures of which have been solved by X-ray crystallography. In complex structures, Os3BGlu7 residue Asn245 hydrogen bonds to the second sugar in the +1 subsite for laminaribiose and the third sugar in the +2 subsite for cellotetraose and cellopentaose. The corresponding Os3BGlu6 residue, Met251, appears to block the binding of cellooligosaccharides at the +2 subsite, whereas His252 in this position in Os4BGlu12 could hydrogen bond to oligosaccharides. Mutation of Os3BGlu6 Met251 to Asn resulted in a 15-fold increased k(cat)/K(m) value for hydrolysis of laminaribiose compared to wild type Os3BGlu6 and 9 to 24-fold increases for cellooligosaccharides with degrees of polymerization (DP) of 2-5. On the other hand, mutation of Os3BGlu7 Asn245 to Met decreased the k(cat)/K(m) of hydrolysis by 6.5-fold for laminaribiose and 17 to 30-fold for cellooligosaccharides with DP \u003e2, while mutation of Os4BGlu12 His252 to Met decreased the corresponding k(cat)/K(m) values 2 to 6-fold."}

Oryza_sentences

{"project":"Oryza_sentences","blocks":[{"id":"T1","span":{"begin":0,"end":125},"obj":"Sentence"},{"id":"T2","span":{"begin":126,"end":280},"obj":"Sentence"},{"id":"T3","span":{"begin":281,"end":473},"obj":"Sentence"},{"id":"T4","span":{"begin":474,"end":676},"obj":"Sentence"},{"id":"T5","span":{"begin":677,"end":921},"obj":"Sentence"},{"id":"T6","span":{"begin":922,"end":1203},"obj":"Sentence"}],"text":"Exchanging a single amino acid residue generates or weakens a +2 cellooligosaccharide binding subsite in rice β-glucosidases.\nOs3BGlu6, Os3BGlu7, and Os4BGlu12 are rice glycoside hydrolase family 1 β-glucosidases, the structures of which have been solved by X-ray crystallography. In complex structures, Os3BGlu7 residue Asn245 hydrogen bonds to the second sugar in the +1 subsite for laminaribiose and the third sugar in the +2 subsite for cellotetraose and cellopentaose. The corresponding Os3BGlu6 residue, Met251, appears to block the binding of cellooligosaccharides at the +2 subsite, whereas His252 in this position in Os4BGlu12 could hydrogen bond to oligosaccharides. Mutation of Os3BGlu6 Met251 to Asn resulted in a 15-fold increased k(cat)/K(m) value for hydrolysis of laminaribiose compared to wild type Os3BGlu6 and 9 to 24-fold increases for cellooligosaccharides with degrees of polymerization (DP) of 2-5. On the other hand, mutation of Os3BGlu7 Asn245 to Met decreased the k(cat)/K(m) of hydrolysis by 6.5-fold for laminaribiose and 17 to 30-fold for cellooligosaccharides with DP \u003e2, while mutation of Os4BGlu12 His252 to Met decreased the corresponding k(cat)/K(m) values 2 to 6-fold."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":105,"end":109},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":164,"end":168},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":746,"end":749},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":992,"end":995},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":1174,"end":1177},"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":"9685"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9685"},{"id":"A5","pred":"db_id","subj":"T5","obj":"9685"}],"text":"Exchanging a single amino acid residue generates or weakens a +2 cellooligosaccharide binding subsite in rice β-glucosidases.\nOs3BGlu6, Os3BGlu7, and Os4BGlu12 are rice glycoside hydrolase family 1 β-glucosidases, the structures of which have been solved by X-ray crystallography. In complex structures, Os3BGlu7 residue Asn245 hydrogen bonds to the second sugar in the +1 subsite for laminaribiose and the third sugar in the +2 subsite for cellotetraose and cellopentaose. The corresponding Os3BGlu6 residue, Met251, appears to block the binding of cellooligosaccharides at the +2 subsite, whereas His252 in this position in Os4BGlu12 could hydrogen bond to oligosaccharides. Mutation of Os3BGlu6 Met251 to Asn resulted in a 15-fold increased k(cat)/K(m) value for hydrolysis of laminaribiose compared to wild type Os3BGlu6 and 9 to 24-fold increases for cellooligosaccharides with degrees of polymerization (DP) of 2-5. On the other hand, mutation of Os3BGlu7 Asn245 to Met decreased the k(cat)/K(m) of hydrolysis by 6.5-fold for laminaribiose and 17 to 30-fold for cellooligosaccharides with DP \u003e2, while mutation of Os4BGlu12 His252 to Met decreased the corresponding k(cat)/K(m) values 2 to 6-fold."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":935,"end":939},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002398"}],"text":"Exchanging a single amino acid residue generates or weakens a +2 cellooligosaccharide binding subsite in rice β-glucosidases.\nOs3BGlu6, Os3BGlu7, and Os4BGlu12 are rice glycoside hydrolase family 1 β-glucosidases, the structures of which have been solved by X-ray crystallography. In complex structures, Os3BGlu7 residue Asn245 hydrogen bonds to the second sugar in the +1 subsite for laminaribiose and the third sugar in the +2 subsite for cellotetraose and cellopentaose. The corresponding Os3BGlu6 residue, Met251, appears to block the binding of cellooligosaccharides at the +2 subsite, whereas His252 in this position in Os4BGlu12 could hydrogen bond to oligosaccharides. Mutation of Os3BGlu6 Met251 to Asn resulted in a 15-fold increased k(cat)/K(m) value for hydrolysis of laminaribiose compared to wild type Os3BGlu6 and 9 to 24-fold increases for cellooligosaccharides with degrees of polymerization (DP) of 2-5. On the other hand, mutation of Os3BGlu7 Asn245 to Met decreased the k(cat)/K(m) of hydrolysis by 6.5-fold for laminaribiose and 17 to 30-fold for cellooligosaccharides with DP \u003e2, while mutation of Os4BGlu12 His252 to Met decreased the corresponding k(cat)/K(m) values 2 to 6-fold."}

Anatomy-MAT

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":935,"end":939},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000091"}],"text":"Exchanging a single amino acid residue generates or weakens a +2 cellooligosaccharide binding subsite in rice β-glucosidases.\nOs3BGlu6, Os3BGlu7, and Os4BGlu12 are rice glycoside hydrolase family 1 β-glucosidases, the structures of which have been solved by X-ray crystallography. In complex structures, Os3BGlu7 residue Asn245 hydrogen bonds to the second sugar in the +1 subsite for laminaribiose and the third sugar in the +2 subsite for cellotetraose and cellopentaose. The corresponding Os3BGlu6 residue, Met251, appears to block the binding of cellooligosaccharides at the +2 subsite, whereas His252 in this position in Os4BGlu12 could hydrogen bond to oligosaccharides. Mutation of Os3BGlu6 Met251 to Asn resulted in a 15-fold increased k(cat)/K(m) value for hydrolysis of laminaribiose compared to wild type Os3BGlu6 and 9 to 24-fold increases for cellooligosaccharides with degrees of polymerization (DP) of 2-5. On the other hand, mutation of Os3BGlu7 Asn245 to Met decreased the k(cat)/K(m) of hydrolysis by 6.5-fold for laminaribiose and 17 to 30-fold for cellooligosaccharides with DP \u003e2, while mutation of Os4BGlu12 His252 to Met decreased the corresponding k(cat)/K(m) values 2 to 6-fold."}