PubMed:16503208 JSONTXT

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":967,"end":977},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G36281WI"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G36281WI"}],"text":"Structural elements in dextran glucosidase responsible for high specificity to long chain substrate.\nDextran glucosidase from Streptococcus mutans (SMDG) and Bacillus oligo-1,6-glucosidases, members of glycoside hydrolase family 13 enzymes, have the high sequence similarity. Each of them is specific to alpha-1,6-glucosidic linkage at the non-reducing end of substrate to liberate glucose. The activities toward long isomaltooligosaccharides were different in both enzymes, in which SMDG and oligo-1,6-glucosidase showed high and low activities, respectively. We determined the structural elements essential for high activity toward long-chain substrate. From conformational comparison between SMDG and B. cereus oligo-1,6-glucosidase (three-dimensional structure has been solved), Trp238 and short beta--\u003ealpha loop 4 of SMDG were considered to contribute to the high activity to long-chain substrate. W238A had similar kcat/Km value for isomaltotriose to that for isomaltose, suggesting that the affinity of subsite +2 was decreased by Trp238 replacement. Trp238 mutants as well as the chimeric enzyme having longer beta--\u003ealpha loop 4 of B. subtilis oligo-1,6-glucosidase showed lower preference for long-chain substrates, indicating that both Trp238 and short beta--\u003ealpha loop 4 were important for high activity to long-chain substrates."}

{"project":"GlyCosmos15-NCBITAXON","denotations":[{"id":"T1","span":{"begin":126,"end":146},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":158,"end":166},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":704,"end":713},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"1309"},{"id":"A2","pred":"db_id","subj":"T2","obj":"1386"},{"id":"A3","pred":"db_id","subj":"T2","obj":"55087"},{"id":"A4","pred":"db_id","subj":"T4","obj":"1396"}],"text":"Structural elements in dextran glucosidase responsible for high specificity to long chain substrate.\nDextran glucosidase from Streptococcus mutans (SMDG) and Bacillus oligo-1,6-glucosidases, members of glycoside hydrolase family 13 enzymes, have the high sequence similarity. Each of them is specific to alpha-1,6-glucosidic linkage at the non-reducing end of substrate to liberate glucose. The activities toward long isomaltooligosaccharides were different in both enzymes, in which SMDG and oligo-1,6-glucosidase showed high and low activities, respectively. We determined the structural elements essential for high activity toward long-chain substrate. From conformational comparison between SMDG and B. cereus oligo-1,6-glucosidase (three-dimensional structure has been solved), Trp238 and short beta--\u003ealpha loop 4 of SMDG were considered to contribute to the high activity to long-chain substrate. W238A had similar kcat/Km value for isomaltotriose to that for isomaltose, suggesting that the affinity of subsite +2 was decreased by Trp238 replacement. Trp238 mutants as well as the chimeric enzyme having longer beta--\u003ealpha loop 4 of B. subtilis oligo-1,6-glucosidase showed lower preference for long-chain substrates, indicating that both Trp238 and short beta--\u003ealpha loop 4 were important for high activity to long-chain substrates."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":100},"obj":"Sentence"},{"id":"T2","span":{"begin":101,"end":275},"obj":"Sentence"},{"id":"T3","span":{"begin":276,"end":390},"obj":"Sentence"},{"id":"T4","span":{"begin":391,"end":560},"obj":"Sentence"},{"id":"T5","span":{"begin":561,"end":655},"obj":"Sentence"},{"id":"T6","span":{"begin":656,"end":903},"obj":"Sentence"},{"id":"T7","span":{"begin":904,"end":1058},"obj":"Sentence"},{"id":"T8","span":{"begin":1059,"end":1343},"obj":"Sentence"}],"text":"Structural elements in dextran glucosidase responsible for high specificity to long chain substrate.\nDextran glucosidase from Streptococcus mutans (SMDG) and Bacillus oligo-1,6-glucosidases, members of glycoside hydrolase family 13 enzymes, have the high sequence similarity. Each of them is specific to alpha-1,6-glucosidic linkage at the non-reducing end of substrate to liberate glucose. The activities toward long isomaltooligosaccharides were different in both enzymes, in which SMDG and oligo-1,6-glucosidase showed high and low activities, respectively. We determined the structural elements essential for high activity toward long-chain substrate. From conformational comparison between SMDG and B. cereus oligo-1,6-glucosidase (three-dimensional structure has been solved), Trp238 and short beta--\u003ealpha loop 4 of SMDG were considered to contribute to the high activity to long-chain substrate. W238A had similar kcat/Km value for isomaltotriose to that for isomaltose, suggesting that the affinity of subsite +2 was decreased by Trp238 replacement. Trp238 mutants as well as the chimeric enzyme having longer beta--\u003ealpha loop 4 of B. subtilis oligo-1,6-glucosidase showed lower preference for long-chain substrates, indicating that both Trp238 and short beta--\u003ealpha loop 4 were important for high activity to long-chain substrates."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":967,"end":977},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G36281WI"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G36281WI"}],"text":"Structural elements in dextran glucosidase responsible for high specificity to long chain substrate.\nDextran glucosidase from Streptococcus mutans (SMDG) and Bacillus oligo-1,6-glucosidases, members of glycoside hydrolase family 13 enzymes, have the high sequence similarity. Each of them is specific to alpha-1,6-glucosidic linkage at the non-reducing end of substrate to liberate glucose. The activities toward long isomaltooligosaccharides were different in both enzymes, in which SMDG and oligo-1,6-glucosidase showed high and low activities, respectively. We determined the structural elements essential for high activity toward long-chain substrate. From conformational comparison between SMDG and B. cereus oligo-1,6-glucosidase (three-dimensional structure has been solved), Trp238 and short beta--\u003ealpha loop 4 of SMDG were considered to contribute to the high activity to long-chain substrate. W238A had similar kcat/Km value for isomaltotriose to that for isomaltose, suggesting that the affinity of subsite +2 was decreased by Trp238 replacement. Trp238 mutants as well as the chimeric enzyme having longer beta--\u003ealpha loop 4 of B. subtilis oligo-1,6-glucosidase showed lower preference for long-chain substrates, indicating that both Trp238 and short beta--\u003ealpha loop 4 were important for high activity to long-chain substrates."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":126,"end":146},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":158,"end":166},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":704,"end":713},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"1309"},{"id":"A2","pred":"db_id","subj":"T2","obj":"1386"},{"id":"A3","pred":"db_id","subj":"T2","obj":"55087"},{"id":"A4","pred":"db_id","subj":"T4","obj":"1396"}],"text":"Structural elements in dextran glucosidase responsible for high specificity to long chain substrate.\nDextran glucosidase from Streptococcus mutans (SMDG) and Bacillus oligo-1,6-glucosidases, members of glycoside hydrolase family 13 enzymes, have the high sequence similarity. Each of them is specific to alpha-1,6-glucosidic linkage at the non-reducing end of substrate to liberate glucose. The activities toward long isomaltooligosaccharides were different in both enzymes, in which SMDG and oligo-1,6-glucosidase showed high and low activities, respectively. We determined the structural elements essential for high activity toward long-chain substrate. From conformational comparison between SMDG and B. cereus oligo-1,6-glucosidase (three-dimensional structure has been solved), Trp238 and short beta--\u003ealpha loop 4 of SMDG were considered to contribute to the high activity to long-chain substrate. W238A had similar kcat/Km value for isomaltotriose to that for isomaltose, suggesting that the affinity of subsite +2 was decreased by Trp238 replacement. Trp238 mutants as well as the chimeric enzyme having longer beta--\u003ealpha loop 4 of B. subtilis oligo-1,6-glucosidase showed lower preference for long-chain substrates, indicating that both Trp238 and short beta--\u003ealpha loop 4 were important for high activity to long-chain substrates."}