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OryzaGP_2021

OryzaGP_2022

{"project":"OryzaGP_2022","denotations":[{"id":"T1","span":{"begin":255,"end":256},"obj":"http://identifiers.org/oryzabase.gene/11216"}],"text":"Enzymatic properties of a GH19 chitinase isolated from rice lacking a major loop structure involved in chitin binding.\nThe catalytic domains of family GH19 chitinases have been found to consist of a conserved, α-helical core-region and different numbers (1-6) of loop structures, located at both ends of the substrate-binding groove and which extend over the glycon- and aglycon-binding sites. We expressed, purified and enzymatically characterized a GH19 chitinase from rice, Oryza sativa L. cv. Nipponbare (OsChia2a), lacking a major loop structure (loop III) connected to the functionally important β-stranded region. The new enzyme thus contained the five remaining loop structures (loops I, II, IV, V and C-term). The OsChia2a recombinant protein catalyzed hydrolysis of chitin oligosaccharides, (GlcNAc)n (n = 3-6), with inversion of anomeric configuration, indicating that OsChia2a correctly folded without loop III. From thermal unfolding experiments and calorimetric titrations using the inactive OsChia2a mutant (OsChia2a-E68Q), in which the catalytic residue Glu68 was mutated to glutamine, we found that the binding affinities towards (GlcNAc)n (n = 2-6) were almost proportional to the degree of polymerization of (GlcNAc)n, but were much lower than those obtained for a moss GH19 chitinase having only loop III [Ohnuma T, Sørlie M, Fukuda T, Kawamoto N, Taira T, Fukamizo T. 2011. Chitin oligosaccharide binding to a family GH19 chitinase from the moss, Bryum coronatum. FEBS J. 278:3991-4001]. Nevertheless, OsChia2a exhibited significant antifungal activity. It appears that loop III connected to the β-stranded region is important for (GlcNAc)n binding, but is not essential for antifungal activity."}

sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":118},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":119,"end":393},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":394,"end":496},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":497,"end":620},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":621,"end":718},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":719,"end":923},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":924,"end":1388},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1389,"end":1394},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1395,"end":1484},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1485,"end":1492},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1493,"end":1508},"obj":"Sentence"},{"id":"TextSentencer_T12","span":{"begin":1509,"end":1574},"obj":"Sentence"},{"id":"TextSentencer_T13","span":{"begin":1575,"end":1716},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":118},"obj":"Sentence"},{"id":"T2","span":{"begin":119,"end":393},"obj":"Sentence"},{"id":"T3","span":{"begin":394,"end":496},"obj":"Sentence"},{"id":"T4","span":{"begin":497,"end":620},"obj":"Sentence"},{"id":"T5","span":{"begin":621,"end":718},"obj":"Sentence"},{"id":"T6","span":{"begin":719,"end":923},"obj":"Sentence"},{"id":"T7","span":{"begin":924,"end":1388},"obj":"Sentence"},{"id":"T8","span":{"begin":1389,"end":1394},"obj":"Sentence"},{"id":"T9","span":{"begin":1395,"end":1484},"obj":"Sentence"},{"id":"T10","span":{"begin":1485,"end":1492},"obj":"Sentence"},{"id":"T11","span":{"begin":1493,"end":1508},"obj":"Sentence"},{"id":"T12","span":{"begin":1509,"end":1574},"obj":"Sentence"},{"id":"T13","span":{"begin":1575,"end":1716},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Enzymatic properties of a GH19 chitinase isolated from rice lacking a major loop structure involved in chitin binding.\nThe catalytic domains of family GH19 chitinases have been found to consist of a conserved, α-helical core-region and different numbers (1-6) of loop structures, located at both ends of the substrate-binding groove and which extend over the glycon- and aglycon-binding sites. We expressed, purified and enzymatically characterized a GH19 chitinase from rice, Oryza sativa L. cv. Nipponbare (OsChia2a), lacking a major loop structure (loop III) connected to the functionally important β-stranded region. The new enzyme thus contained the five remaining loop structures (loops I, II, IV, V and C-term). The OsChia2a recombinant protein catalyzed hydrolysis of chitin oligosaccharides, (GlcNAc)n (n = 3-6), with inversion of anomeric configuration, indicating that OsChia2a correctly folded without loop III. From thermal unfolding experiments and calorimetric titrations using the inactive OsChia2a mutant (OsChia2a-E68Q), in which the catalytic residue Glu68 was mutated to glutamine, we found that the binding affinities towards (GlcNAc)n (n = 2-6) were almost proportional to the degree of polymerization of (GlcNAc)n, but were much lower than those obtained for a moss GH19 chitinase having only loop III [Ohnuma T, Sørlie M, Fukuda T, Kawamoto N, Taira T, Fukamizo T. 2011. Chitin oligosaccharide binding to a family GH19 chitinase from the moss, Bryum coronatum. FEBS J. 278:3991-4001]. Nevertheless, OsChia2a exhibited significant antifungal activity. It appears that loop III connected to the β-stranded region is important for (GlcNAc)n binding, but is not essential for antifungal activity."}

OryzaGP_2021_v2

{"project":"OryzaGP_2021_v2","denotations":[{"id":"T1","span":{"begin":509,"end":517},"obj":"http://identifiers.org/oryzabase.gene/8130"},{"id":"T2","span":{"begin":723,"end":731},"obj":"http://identifiers.org/oryzabase.gene/8130"},{"id":"T3","span":{"begin":880,"end":888},"obj":"http://identifiers.org/oryzabase.gene/8130"},{"id":"T4","span":{"begin":1006,"end":1014},"obj":"http://identifiers.org/oryzabase.gene/8130"},{"id":"T5","span":{"begin":1023,"end":1031},"obj":"http://identifiers.org/oryzabase.gene/8130"},{"id":"T6","span":{"begin":1523,"end":1531},"obj":"http://identifiers.org/oryzabase.gene/8130"},{"id":"T52916","span":{"begin":509,"end":517},"obj":"http://identifiers.org/rapdb.locus/Os10g0542900"},{"id":"T86511","span":{"begin":723,"end":731},"obj":"http://identifiers.org/rapdb.locus/Os10g0542900"},{"id":"T70120","span":{"begin":880,"end":888},"obj":"http://identifiers.org/rapdb.locus/Os10g0542900"},{"id":"T38845","span":{"begin":1006,"end":1014},"obj":"http://identifiers.org/rapdb.locus/Os10g0542900"},{"id":"T34076","span":{"begin":1023,"end":1031},"obj":"http://identifiers.org/rapdb.locus/Os10g0542900"},{"id":"T30518","span":{"begin":1523,"end":1531},"obj":"http://identifiers.org/rapdb.locus/Os10g0542900"}],"text":"Enzymatic properties of a GH19 chitinase isolated from rice lacking a major loop structure involved in chitin binding.\nThe catalytic domains of family GH19 chitinases have been found to consist of a conserved, α-helical core-region and different numbers (1-6) of loop structures, located at both ends of the substrate-binding groove and which extend over the glycon- and aglycon-binding sites. We expressed, purified and enzymatically characterized a GH19 chitinase from rice, Oryza sativa L. cv. Nipponbare (OsChia2a), lacking a major loop structure (loop III) connected to the functionally important β-stranded region. The new enzyme thus contained the five remaining loop structures (loops I, II, IV, V and C-term). The OsChia2a recombinant protein catalyzed hydrolysis of chitin oligosaccharides, (GlcNAc)n (n = 3-6), with inversion of anomeric configuration, indicating that OsChia2a correctly folded without loop III. From thermal unfolding experiments and calorimetric titrations using the inactive OsChia2a mutant (OsChia2a-E68Q), in which the catalytic residue Glu68 was mutated to glutamine, we found that the binding affinities towards (GlcNAc)n (n = 2-6) were almost proportional to the degree of polymerization of (GlcNAc)n, but were much lower than those obtained for a moss GH19 chitinase having only loop III [Ohnuma T, Sørlie M, Fukuda T, Kawamoto N, Taira T, Fukamizo T. 2011. Chitin oligosaccharide binding to a family GH19 chitinase from the moss, Bryum coronatum. FEBS J. 278:3991-4001]. Nevertheless, OsChia2a exhibited significant antifungal activity. It appears that loop III connected to the β-stranded region is important for (GlcNAc)n binding, but is not essential for antifungal activity."}

OryzaGP_2021_FLAIR

NGLY1-deficiency

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":802,"end":808},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":1148,"end":1154},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T3","span":{"begin":1228,"end":1234},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T4","span":{"begin":1653,"end":1659},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"Enzymatic properties of a GH19 chitinase isolated from rice lacking a major loop structure involved in chitin binding.\nThe catalytic domains of family GH19 chitinases have been found to consist of a conserved, α-helical core-region and different numbers (1-6) of loop structures, located at both ends of the substrate-binding groove and which extend over the glycon- and aglycon-binding sites. We expressed, purified and enzymatically characterized a GH19 chitinase from rice, Oryza sativa L. cv. Nipponbare (OsChia2a), lacking a major loop structure (loop III) connected to the functionally important β-stranded region. The new enzyme thus contained the five remaining loop structures (loops I, II, IV, V and C-term). The OsChia2a recombinant protein catalyzed hydrolysis of chitin oligosaccharides, (GlcNAc)n (n = 3-6), with inversion of anomeric configuration, indicating that OsChia2a correctly folded without loop III. From thermal unfolding experiments and calorimetric titrations using the inactive OsChia2a mutant (OsChia2a-E68Q), in which the catalytic residue Glu68 was mutated to glutamine, we found that the binding affinities towards (GlcNAc)n (n = 2-6) were almost proportional to the degree of polymerization of (GlcNAc)n, but were much lower than those obtained for a moss GH19 chitinase having only loop III [Ohnuma T, Sørlie M, Fukuda T, Kawamoto N, Taira T, Fukamizo T. 2011. Chitin oligosaccharide binding to a family GH19 chitinase from the moss, Bryum coronatum. FEBS J. 278:3991-4001]. Nevertheless, OsChia2a exhibited significant antifungal activity. It appears that loop III connected to the β-stranded region is important for (GlcNAc)n binding, but is not essential for antifungal activity."}

Glycan-GlyCosmos

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":103,"end":109},"obj":"Glycan"},{"id":"T2","span":{"begin":776,"end":782},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G97099AY"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G97099AY"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY"}],"text":"Enzymatic properties of a GH19 chitinase isolated from rice lacking a major loop structure involved in chitin binding.\nThe catalytic domains of family GH19 chitinases have been found to consist of a conserved, α-helical core-region and different numbers (1-6) of loop structures, located at both ends of the substrate-binding groove and which extend over the glycon- and aglycon-binding sites. We expressed, purified and enzymatically characterized a GH19 chitinase from rice, Oryza sativa L. cv. Nipponbare (OsChia2a), lacking a major loop structure (loop III) connected to the functionally important β-stranded region. The new enzyme thus contained the five remaining loop structures (loops I, II, IV, V and C-term). The OsChia2a recombinant protein catalyzed hydrolysis of chitin oligosaccharides, (GlcNAc)n (n = 3-6), with inversion of anomeric configuration, indicating that OsChia2a correctly folded without loop III. From thermal unfolding experiments and calorimetric titrations using the inactive OsChia2a mutant (OsChia2a-E68Q), in which the catalytic residue Glu68 was mutated to glutamine, we found that the binding affinities towards (GlcNAc)n (n = 2-6) were almost proportional to the degree of polymerization of (GlcNAc)n, but were much lower than those obtained for a moss GH19 chitinase having only loop III [Ohnuma T, Sørlie M, Fukuda T, Kawamoto N, Taira T, Fukamizo T. 2011. Chitin oligosaccharide binding to a family GH19 chitinase from the moss, Bryum coronatum. FEBS J. 278:3991-4001]. Nevertheless, OsChia2a exhibited significant antifungal activity. It appears that loop III connected to the β-stranded region is important for (GlcNAc)n binding, but is not essential for antifungal activity."}

GlyCosmos15-NCBITAXON

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":55,"end":59},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":471,"end":475},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":477,"end":489},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":1368,"end":1373},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":1468,"end":1483},"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"},{"id":"A4","pred":"db_id","subj":"T4","obj":"700687"},{"id":"A5","pred":"db_id","subj":"T5","obj":"216087"}],"text":"Enzymatic properties of a GH19 chitinase isolated from rice lacking a major loop structure involved in chitin binding.\nThe catalytic domains of family GH19 chitinases have been found to consist of a conserved, α-helical core-region and different numbers (1-6) of loop structures, located at both ends of the substrate-binding groove and which extend over the glycon- and aglycon-binding sites. We expressed, purified and enzymatically characterized a GH19 chitinase from rice, Oryza sativa L. cv. Nipponbare (OsChia2a), lacking a major loop structure (loop III) connected to the functionally important β-stranded region. The new enzyme thus contained the five remaining loop structures (loops I, II, IV, V and C-term). The OsChia2a recombinant protein catalyzed hydrolysis of chitin oligosaccharides, (GlcNAc)n (n = 3-6), with inversion of anomeric configuration, indicating that OsChia2a correctly folded without loop III. From thermal unfolding experiments and calorimetric titrations using the inactive OsChia2a mutant (OsChia2a-E68Q), in which the catalytic residue Glu68 was mutated to glutamine, we found that the binding affinities towards (GlcNAc)n (n = 2-6) were almost proportional to the degree of polymerization of (GlcNAc)n, but were much lower than those obtained for a moss GH19 chitinase having only loop III [Ohnuma T, Sørlie M, Fukuda T, Kawamoto N, Taira T, Fukamizo T. 2011. Chitin oligosaccharide binding to a family GH19 chitinase from the moss, Bryum coronatum. FEBS J. 278:3991-4001]. Nevertheless, OsChia2a exhibited significant antifungal activity. It appears that loop III connected to the β-stranded region is important for (GlcNAc)n binding, but is not essential for antifungal activity."}

GlyCosmos15-UBERON

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":326,"end":332},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0004704"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0006846"},{"id":"A3","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0014764"}],"text":"Enzymatic properties of a GH19 chitinase isolated from rice lacking a major loop structure involved in chitin binding.\nThe catalytic domains of family GH19 chitinases have been found to consist of a conserved, α-helical core-region and different numbers (1-6) of loop structures, located at both ends of the substrate-binding groove and which extend over the glycon- and aglycon-binding sites. We expressed, purified and enzymatically characterized a GH19 chitinase from rice, Oryza sativa L. cv. Nipponbare (OsChia2a), lacking a major loop structure (loop III) connected to the functionally important β-stranded region. The new enzyme thus contained the five remaining loop structures (loops I, II, IV, V and C-term). The OsChia2a recombinant protein catalyzed hydrolysis of chitin oligosaccharides, (GlcNAc)n (n = 3-6), with inversion of anomeric configuration, indicating that OsChia2a correctly folded without loop III. From thermal unfolding experiments and calorimetric titrations using the inactive OsChia2a mutant (OsChia2a-E68Q), in which the catalytic residue Glu68 was mutated to glutamine, we found that the binding affinities towards (GlcNAc)n (n = 2-6) were almost proportional to the degree of polymerization of (GlcNAc)n, but were much lower than those obtained for a moss GH19 chitinase having only loop III [Ohnuma T, Sørlie M, Fukuda T, Kawamoto N, Taira T, Fukamizo T. 2011. Chitin oligosaccharide binding to a family GH19 chitinase from the moss, Bryum coronatum. FEBS J. 278:3991-4001]. Nevertheless, OsChia2a exhibited significant antifungal activity. It appears that loop III connected to the β-stranded region is important for (GlcNAc)n binding, but is not essential for antifungal activity."}

sentences

GlyCosmos15-Sentences

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":118},"obj":"Sentence"},{"id":"T2","span":{"begin":119,"end":393},"obj":"Sentence"},{"id":"T3","span":{"begin":394,"end":496},"obj":"Sentence"},{"id":"T4","span":{"begin":497,"end":620},"obj":"Sentence"},{"id":"T5","span":{"begin":621,"end":718},"obj":"Sentence"},{"id":"T6","span":{"begin":719,"end":923},"obj":"Sentence"},{"id":"T7","span":{"begin":924,"end":1394},"obj":"Sentence"},{"id":"T8","span":{"begin":1395,"end":1484},"obj":"Sentence"},{"id":"T9","span":{"begin":1485,"end":1508},"obj":"Sentence"},{"id":"T10","span":{"begin":1509,"end":1574},"obj":"Sentence"},{"id":"T11","span":{"begin":1575,"end":1716},"obj":"Sentence"}],"text":"Enzymatic properties of a GH19 chitinase isolated from rice lacking a major loop structure involved in chitin binding.\nThe catalytic domains of family GH19 chitinases have been found to consist of a conserved, α-helical core-region and different numbers (1-6) of loop structures, located at both ends of the substrate-binding groove and which extend over the glycon- and aglycon-binding sites. We expressed, purified and enzymatically characterized a GH19 chitinase from rice, Oryza sativa L. cv. Nipponbare (OsChia2a), lacking a major loop structure (loop III) connected to the functionally important β-stranded region. The new enzyme thus contained the five remaining loop structures (loops I, II, IV, V and C-term). The OsChia2a recombinant protein catalyzed hydrolysis of chitin oligosaccharides, (GlcNAc)n (n = 3-6), with inversion of anomeric configuration, indicating that OsChia2a correctly folded without loop III. From thermal unfolding experiments and calorimetric titrations using the inactive OsChia2a mutant (OsChia2a-E68Q), in which the catalytic residue Glu68 was mutated to glutamine, we found that the binding affinities towards (GlcNAc)n (n = 2-6) were almost proportional to the degree of polymerization of (GlcNAc)n, but were much lower than those obtained for a moss GH19 chitinase having only loop III [Ohnuma T, Sørlie M, Fukuda T, Kawamoto N, Taira T, Fukamizo T. 2011. Chitin oligosaccharide binding to a family GH19 chitinase from the moss, Bryum coronatum. FEBS J. 278:3991-4001]. Nevertheless, OsChia2a exhibited significant antifungal activity. It appears that loop III connected to the β-stranded region is important for (GlcNAc)n binding, but is not essential for antifungal activity."}

GlyCosmos15-Glycan

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":103,"end":109},"obj":"Glycan"},{"id":"T2","span":{"begin":776,"end":782},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G97099AY"},{"id":"A3","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G97099AY"},{"id":"A4","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY"}],"text":"Enzymatic properties of a GH19 chitinase isolated from rice lacking a major loop structure involved in chitin binding.\nThe catalytic domains of family GH19 chitinases have been found to consist of a conserved, α-helical core-region and different numbers (1-6) of loop structures, located at both ends of the substrate-binding groove and which extend over the glycon- and aglycon-binding sites. We expressed, purified and enzymatically characterized a GH19 chitinase from rice, Oryza sativa L. cv. Nipponbare (OsChia2a), lacking a major loop structure (loop III) connected to the functionally important β-stranded region. The new enzyme thus contained the five remaining loop structures (loops I, II, IV, V and C-term). The OsChia2a recombinant protein catalyzed hydrolysis of chitin oligosaccharides, (GlcNAc)n (n = 3-6), with inversion of anomeric configuration, indicating that OsChia2a correctly folded without loop III. From thermal unfolding experiments and calorimetric titrations using the inactive OsChia2a mutant (OsChia2a-E68Q), in which the catalytic residue Glu68 was mutated to glutamine, we found that the binding affinities towards (GlcNAc)n (n = 2-6) were almost proportional to the degree of polymerization of (GlcNAc)n, but were much lower than those obtained for a moss GH19 chitinase having only loop III [Ohnuma T, Sørlie M, Fukuda T, Kawamoto N, Taira T, Fukamizo T. 2011. Chitin oligosaccharide binding to a family GH19 chitinase from the moss, Bryum coronatum. FEBS J. 278:3991-4001]. Nevertheless, OsChia2a exhibited significant antifungal activity. It appears that loop III connected to the β-stranded region is important for (GlcNAc)n binding, but is not essential for antifungal activity."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":55,"end":59},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":471,"end":475},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":477,"end":489},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":1368,"end":1373},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":1468,"end":1483},"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"},{"id":"A4","pred":"db_id","subj":"T4","obj":"700687"},{"id":"A5","pred":"db_id","subj":"T5","obj":"216087"}],"text":"Enzymatic properties of a GH19 chitinase isolated from rice lacking a major loop structure involved in chitin binding.\nThe catalytic domains of family GH19 chitinases have been found to consist of a conserved, α-helical core-region and different numbers (1-6) of loop structures, located at both ends of the substrate-binding groove and which extend over the glycon- and aglycon-binding sites. We expressed, purified and enzymatically characterized a GH19 chitinase from rice, Oryza sativa L. cv. Nipponbare (OsChia2a), lacking a major loop structure (loop III) connected to the functionally important β-stranded region. The new enzyme thus contained the five remaining loop structures (loops I, II, IV, V and C-term). The OsChia2a recombinant protein catalyzed hydrolysis of chitin oligosaccharides, (GlcNAc)n (n = 3-6), with inversion of anomeric configuration, indicating that OsChia2a correctly folded without loop III. From thermal unfolding experiments and calorimetric titrations using the inactive OsChia2a mutant (OsChia2a-E68Q), in which the catalytic residue Glu68 was mutated to glutamine, we found that the binding affinities towards (GlcNAc)n (n = 2-6) were almost proportional to the degree of polymerization of (GlcNAc)n, but were much lower than those obtained for a moss GH19 chitinase having only loop III [Ohnuma T, Sørlie M, Fukuda T, Kawamoto N, Taira T, Fukamizo T. 2011. Chitin oligosaccharide binding to a family GH19 chitinase from the moss, Bryum coronatum. FEBS J. 278:3991-4001]. Nevertheless, OsChia2a exhibited significant antifungal activity. It appears that loop III connected to the β-stranded region is important for (GlcNAc)n binding, but is not essential for antifungal activity."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":326,"end":332},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0004704"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0006846"},{"id":"A3","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0014764"}],"text":"Enzymatic properties of a GH19 chitinase isolated from rice lacking a major loop structure involved in chitin binding.\nThe catalytic domains of family GH19 chitinases have been found to consist of a conserved, α-helical core-region and different numbers (1-6) of loop structures, located at both ends of the substrate-binding groove and which extend over the glycon- and aglycon-binding sites. We expressed, purified and enzymatically characterized a GH19 chitinase from rice, Oryza sativa L. cv. Nipponbare (OsChia2a), lacking a major loop structure (loop III) connected to the functionally important β-stranded region. The new enzyme thus contained the five remaining loop structures (loops I, II, IV, V and C-term). The OsChia2a recombinant protein catalyzed hydrolysis of chitin oligosaccharides, (GlcNAc)n (n = 3-6), with inversion of anomeric configuration, indicating that OsChia2a correctly folded without loop III. From thermal unfolding experiments and calorimetric titrations using the inactive OsChia2a mutant (OsChia2a-E68Q), in which the catalytic residue Glu68 was mutated to glutamine, we found that the binding affinities towards (GlcNAc)n (n = 2-6) were almost proportional to the degree of polymerization of (GlcNAc)n, but were much lower than those obtained for a moss GH19 chitinase having only loop III [Ohnuma T, Sørlie M, Fukuda T, Kawamoto N, Taira T, Fukamizo T. 2011. Chitin oligosaccharide binding to a family GH19 chitinase from the moss, Bryum coronatum. FEBS J. 278:3991-4001]. Nevertheless, OsChia2a exhibited significant antifungal activity. It appears that loop III connected to the β-stranded region is important for (GlcNAc)n binding, but is not essential for antifungal activity."}