PubMed:21062783 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":115,"end":134},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T2","span":{"begin":852,"end":865},"obj":"https://glytoucan.org/Structures/Glycans/G00023MO"},{"id":"T3","span":{"begin":1261,"end":1280},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":115,"end":134},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":852,"end":865},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":1261,"end":1280},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00023MO"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":115,"end":134},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T2","span":{"begin":852,"end":865},"obj":"https://glytoucan.org/Structures/Glycans/G00023MO"},{"id":"T3","span":{"begin":1261,"end":1280},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":145},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":146,"end":260},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":261,"end":431},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":432,"end":615},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":616,"end":900},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":901,"end":1103},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1104,"end":1235},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1236,"end":1440},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":145},"obj":"Sentence"},{"id":"T2","span":{"begin":146,"end":260},"obj":"Sentence"},{"id":"T3","span":{"begin":261,"end":431},"obj":"Sentence"},{"id":"T4","span":{"begin":432,"end":615},"obj":"Sentence"},{"id":"T5","span":{"begin":616,"end":900},"obj":"Sentence"},{"id":"T6","span":{"begin":901,"end":1103},"obj":"Sentence"},{"id":"T7","span":{"begin":1104,"end":1235},"obj":"Sentence"},{"id":"T8","span":{"begin":1236,"end":1440},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":145},"obj":"Sentence"},{"id":"T2","span":{"begin":146,"end":260},"obj":"Sentence"},{"id":"T3","span":{"begin":261,"end":431},"obj":"Sentence"},{"id":"T4","span":{"begin":432,"end":615},"obj":"Sentence"},{"id":"T5","span":{"begin":616,"end":900},"obj":"Sentence"},{"id":"T6","span":{"begin":901,"end":1103},"obj":"Sentence"},{"id":"T7","span":{"begin":1104,"end":1235},"obj":"Sentence"},{"id":"T8","span":{"begin":1236,"end":1440},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}

{"project":"GlycoBiology-PACDB","denotations":[{"id":"_T1","span":{"begin":28,"end":50},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC249,LEC700"},{"id":"_T2","span":{"begin":392,"end":411},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC743"},{"id":"_T3","span":{"begin":392,"end":423},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC249,LEC700"},{"id":"_T4","span":{"begin":555,"end":571},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC754"},{"id":"_T5","span":{"begin":555,"end":571},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC243,LEC640"},{"id":"_T6","span":{"begin":555,"end":571},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC157,LEC407"},{"id":"_T7","span":{"begin":555,"end":571},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC487"},{"id":"_T8","span":{"begin":555,"end":571},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC636"},{"id":"_T9","span":{"begin":555,"end":571},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC244,LEC256,LEC354"},{"id":"_T10","span":{"begin":555,"end":571},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC054,LEC058,LEC073,LEC082,LEC091,LEC103,LEC109,LEC110,LEC123,LEC158,LEC179,LEC198,LEC205,LEC222,LEC223,LEC224,LEC225,LEC232,LEC298,LEC357,LEC378,LEC383,LEC388,LEC389,LEC397,LEC401,LEC410,LEC452"},{"id":"_T11","span":{"begin":555,"end":571},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC002,LEC056,LEC062,LEC069,LEC081,LEC111,LEC133,LEC171,LEC177,LEC187,LEC211,LEC242,LEC252,LEC258,LEC259,LEC260,LEC262,LEC369,LEC377,LEC422,LEC442,LEC448,LEC450,LEC451,LEC454,LEC472,LEC492,LEC620"},{"id":"_T12","span":{"begin":555,"end":576},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC636"},{"id":"_T13","span":{"begin":555,"end":576},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC295,LEC417"},{"id":"_T14","span":{"begin":555,"end":576},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC263,LEC665"},{"id":"_T15","span":{"begin":555,"end":576},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC324"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T18","span":{"begin":1410,"end":1423},"obj":"FMAID:62925"},{"id":"_T1","span":{"begin":86,"end":107},"obj":"FMAID:196731"},{"id":"_T2","span":{"begin":86,"end":107},"obj":"FMAID:82742"},{"id":"_T3","span":{"begin":115,"end":134},"obj":"FMAID:196780"},{"id":"_T4","span":{"begin":115,"end":134},"obj":"FMAID:82786"},{"id":"_T5","span":{"begin":165,"end":170},"obj":"FMAID:198663"},{"id":"_T6","span":{"begin":384,"end":388},"obj":"FMAID:198663"},{"id":"_T7","span":{"begin":837,"end":850},"obj":"FMAID:82797"},{"id":"_T8","span":{"begin":837,"end":850},"obj":"FMAID:196792"},{"id":"_T9","span":{"begin":852,"end":865},"obj":"FMAID:82783"},{"id":"_T10","span":{"begin":852,"end":865},"obj":"FMAID:196777"},{"id":"_T11","span":{"begin":1203,"end":1223},"obj":"FMAID:196731"},{"id":"_T12","span":{"begin":1203,"end":1223},"obj":"FMAID:82742"},{"id":"_T13","span":{"begin":1261,"end":1280},"obj":"FMAID:82786"},{"id":"_T14","span":{"begin":1261,"end":1280},"obj":"FMAID:196780"},{"id":"_T15","span":{"begin":1281,"end":1293},"obj":"FMAID:196733"},{"id":"_T16","span":{"begin":1281,"end":1293},"obj":"FMAID:82744"},{"id":"_T17","span":{"begin":1410,"end":1423},"obj":"FMAID:167256"},{"id":"_T19","span":{"begin":1428,"end":1439},"obj":"FMAID:196773"},{"id":"_T20","span":{"begin":1428,"end":1439},"obj":"FMAID:82780"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":28,"end":38},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/590"},{"id":"T2","span":{"begin":146,"end":156},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/590"},{"id":"T3","span":{"begin":240,"end":245},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/617048"},{"id":"T4","span":{"begin":378,"end":382},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/281823"},{"id":"T5","span":{"begin":392,"end":402},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/590"},{"id":"T6","span":{"begin":463,"end":467},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/281823"},{"id":"T7","span":{"begin":555,"end":566},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/561"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":135,"end":144},"obj":"http://purl.obolibrary.org/obo/GO_0000746"},{"id":"T2","span":{"begin":288,"end":312},"obj":"http://purl.obolibrary.org/obo/GO_0004568"},{"id":"T3","span":{"begin":901,"end":916},"obj":"http://purl.obolibrary.org/obo/GO_0003824"},{"id":"T4","span":{"begin":971,"end":980},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T5","span":{"begin":1131,"end":1140},"obj":"http://purl.obolibrary.org/obo/GO_0051235"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":487,"end":501},"obj":"http://purl.obolibrary.org/obo/GO_0008061"},{"id":"T2","span":{"begin":494,"end":501},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T3","span":{"begin":494,"end":501},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T4","span":{"begin":494,"end":501},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T5","span":{"begin":494,"end":501},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":852,"end":865},"obj":"http://purl.obolibrary.org/obo/GO_0009274"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":852,"end":865},"obj":"http://rdf.glycoinfo.org/glycan/G00023MO"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":78,"end":84},"obj":"Glycan"},{"id":"T2","span":{"begin":487,"end":493},"obj":"Glycan"},{"id":"T3","span":{"begin":758,"end":764},"obj":"Glycan"},{"id":"T4","span":{"begin":1037,"end":1043},"obj":"Glycan"},{"id":"T5","span":{"begin":1391,"end":1397},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G97099AY"},{"id":"A6","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":"A7","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G97099AY"},{"id":"A8","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G97099AY"},{"id":"A9","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G66213AR"},{"id":"A10","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G66213AR"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":28,"end":38},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":146,"end":156},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":392,"end":411},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":555,"end":571},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"590"},{"id":"A2","pred":"db_id","subj":"T2","obj":"590"},{"id":"A3","pred":"db_id","subj":"T3","obj":"28901"},{"id":"A4","pred":"db_id","subj":"T4","obj":"562"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":145},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":146,"end":260},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":261,"end":431},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":432,"end":615},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":616,"end":900},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":901,"end":1103},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1104,"end":1235},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1236,"end":1440},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":145},"obj":"Sentence"},{"id":"T2","span":{"begin":146,"end":260},"obj":"Sentence"},{"id":"T3","span":{"begin":261,"end":431},"obj":"Sentence"},{"id":"T4","span":{"begin":432,"end":615},"obj":"Sentence"},{"id":"T5","span":{"begin":616,"end":900},"obj":"Sentence"},{"id":"T6","span":{"begin":901,"end":1103},"obj":"Sentence"},{"id":"T7","span":{"begin":1104,"end":1235},"obj":"Sentence"},{"id":"T8","span":{"begin":1236,"end":1440},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":145},"obj":"Sentence"},{"id":"T2","span":{"begin":146,"end":260},"obj":"Sentence"},{"id":"T3","span":{"begin":261,"end":431},"obj":"Sentence"},{"id":"T4","span":{"begin":432,"end":615},"obj":"Sentence"},{"id":"T5","span":{"begin":616,"end":900},"obj":"Sentence"},{"id":"T6","span":{"begin":901,"end":1103},"obj":"Sentence"},{"id":"T7","span":{"begin":1104,"end":1235},"obj":"Sentence"},{"id":"T8","span":{"begin":1236,"end":1440},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":145},"obj":"Sentence"},{"id":"T2","span":{"begin":146,"end":260},"obj":"Sentence"},{"id":"T3","span":{"begin":261,"end":431},"obj":"Sentence"},{"id":"T4","span":{"begin":432,"end":615},"obj":"Sentence"},{"id":"T5","span":{"begin":616,"end":900},"obj":"Sentence"},{"id":"T6","span":{"begin":901,"end":1103},"obj":"Sentence"},{"id":"T7","span":{"begin":1104,"end":1235},"obj":"Sentence"},{"id":"T8","span":{"begin":1236,"end":1440},"obj":"Sentence"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":78,"end":84},"obj":"Glycan"},{"id":"T2","span":{"begin":487,"end":493},"obj":"Glycan"},{"id":"T3","span":{"begin":758,"end":764},"obj":"Glycan"},{"id":"T4","span":{"begin":1037,"end":1043},"obj":"Glycan"},{"id":"T5","span":{"begin":1391,"end":1397},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G97099AY"},{"id":"A6","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":"A7","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G97099AY"},{"id":"A8","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G97099AY"},{"id":"A9","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G97099AY"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G66213AR"},{"id":"A10","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G66213AR"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":28,"end":38},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":146,"end":156},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":392,"end":411},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":555,"end":571},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"590"},{"id":"A2","pred":"db_id","subj":"T2","obj":"590"},{"id":"A3","pred":"db_id","subj":"T3","obj":"28901"},{"id":"A4","pred":"db_id","subj":"T4","obj":"562"}],"text":"Characterization of a novel Salmonella Typhimurium chitinase which hydrolyzes chitin, chitooligosaccharides and an N-acetyllactosamine conjugate.\nSalmonella contain genes annotated as chitinases; however, their chitinolytic activities have never been verified. We now demonstrate such an activity for a chitinase assigned to glycoside hydrolase family 18 encoded by the SL0018 (chiA) gene in Salmonella enterica Typhimurium SL1344. A C-terminal truncated form of chiA lacking a putative chitin-binding domain was amplified by PCR, cloned and expressed in Escherichia coli BL21 (DE3) with an N-terminal (His)(6) tag. The purified enzyme hydrolyzes 4-nitrophenyl N,N'-diacetyl-β-D-chitobioside, 4-nitrophenyl β-D-N,N',N″-triacetylchitotriose and carboxymethyl chitin Remazol Brilliant Violet but does not act on 4-nitrophenyl N-acetyl-β-D-glucosaminide, peptidoglycan or 4-nitrophenyl β-D-cellobioside. Enzyme activity was also characterized by directly monitoring product formation using (1)H-nuclear magnetic resonance which showed that chitin is a substrate with the release of N,N'-diacetylchitobiose. Hydrolysis occurs with the retention of configuration and the enzyme acts on only the β-anomers of chitooligosaccharide substrates. The enzyme also released N-acetyllactosamine disaccharide from Galβ1 → 4GlcNAcβ-O-(CH(2))(8)CONH(CH(2))(2)NHCO-tetramethylrhodamine, a model substrate for LacNAc terminating glycoproteins and glycolipids."}