PubMed:758954 JSONTXT

{"project":"Test-Species-PubTator","denotations":[{"id":"1","span":{"begin":21,"end":41},"obj":"Species"},{"id":"18","span":{"begin":248,"end":268},"obj":"Species"},{"id":"19","span":{"begin":599,"end":621},"obj":"Chemical"},{"id":"20","span":{"begin":758,"end":771},"obj":"Chemical"},{"id":"21","span":{"begin":817,"end":830},"obj":"Chemical"},{"id":"22","span":{"begin":898,"end":905},"obj":"Chemical"},{"id":"23","span":{"begin":919,"end":926},"obj":"Chemical"},{"id":"24","span":{"begin":968,"end":979},"obj":"Chemical"},{"id":"25","span":{"begin":984,"end":997},"obj":"Chemical"},{"id":"26","span":{"begin":1004,"end":1015},"obj":"Chemical"},{"id":"27","span":{"begin":1053,"end":1060},"obj":"Chemical"},{"id":"28","span":{"begin":1092,"end":1104},"obj":"Chemical"},{"id":"29","span":{"begin":1161,"end":1172},"obj":"Chemical"},{"id":"30","span":{"begin":1174,"end":1187},"obj":"Chemical"},{"id":"31","span":{"begin":1193,"end":1206},"obj":"Chemical"},{"id":"32","span":{"begin":1238,"end":1255},"obj":"Chemical"},{"id":"33","span":{"begin":1311,"end":1323},"obj":"Chemical"}],"attributes":[{"id":"A1","pred":"resolved_to","subj":"1","obj":"316"},{"id":"A18","pred":"resolved_to","subj":"18","obj":"316"},{"id":"A19","pred":"resolved_to","subj":"19","obj":"MESH:D012967"},{"id":"A20","pred":"resolved_to","subj":"20","obj":"MESH:C008315"},{"id":"A21","pred":"resolved_to","subj":"21","obj":"MESH:C009819"},{"id":"A22","pred":"resolved_to","subj":"22","obj":"MESH:D005947"},{"id":"A23","pred":"resolved_to","subj":"23","obj":"MESH:D008320"},{"id":"A24","pred":"resolved_to","subj":"24","obj":"MESH:C008317"},{"id":"A25","pred":"resolved_to","subj":"25","obj":"MESH:C009819"},{"id":"A26","pred":"resolved_to","subj":"26","obj":"MESH:C008317"},{"id":"A27","pred":"resolved_to","subj":"27","obj":"MESH:D005947"},{"id":"A28","pred":"resolved_to","subj":"28","obj":"MESH:C101184"},{"id":"A29","pred":"resolved_to","subj":"29","obj":"MESH:C008317"},{"id":"A30","pred":"resolved_to","subj":"30","obj":"MESH:C009819"},{"id":"A31","pred":"resolved_to","subj":"31","obj":"MESH:C019193"},{"id":"A32","pred":"resolved_to","subj":"32","obj":"-"},{"id":"A33","pred":"resolved_to","subj":"33","obj":"MESH:C016549"}],"text":"Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase.\nAmylomaltase and disproportionating enzyme (D-enzyme) were purified to homogeneity from cell-free extracts of Pseudomonas stutzeri using a six-step procedure. The presence of both glycosyltransferases in the same organism has not been reported before. Molecular weight determination by gel chromatography gave a value of 74,000 for the amylomaltase and 115 000 for the D-enzyme. Two subunits of different molecular weight were found in each enzyme as proved by sodium dodecyl sulfate-gel electrophoresis. The optimum pH of amylomaltase and D-enzyme activity is 7.6--7.7. Action of both glycosyltransferases on different maltodextrins showed that amylomaltase is most active with maltotetraose, and the Km value for this substrate is 7.1 mM. D-Enzyme catalyzed glucose release from maltose (Km = 8.3 mM) at a higher rate than from maltotriose and maltotetraose. With maltotriose as initial substrate, D-enzyme forms glucose, maltopentaose, maltoheptaose, maltononaose, maltoundecaose as major products. Amylomaltase acts on maltotriose, maltotetraose, and maltopentaose to form a series of homologous 1,4-alpha-glucans. No essential chain-lengthening reaction occurred with maltohexaose."}

{"project":"Test-Species-PubDictionaries","denotations":[{"id":"T1","span":{"begin":21,"end":32},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":248,"end":259},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"286"},{"id":"A2","pred":"db_id","subj":"T2","obj":"286"}],"text":"Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase.\nAmylomaltase and disproportionating enzyme (D-enzyme) were purified to homogeneity from cell-free extracts of Pseudomonas stutzeri using a six-step procedure. The presence of both glycosyltransferases in the same organism has not been reported before. Molecular weight determination by gel chromatography gave a value of 74,000 for the amylomaltase and 115 000 for the D-enzyme. Two subunits of different molecular weight were found in each enzyme as proved by sodium dodecyl sulfate-gel electrophoresis. The optimum pH of amylomaltase and D-enzyme activity is 7.6--7.7. Action of both glycosyltransferases on different maltodextrins showed that amylomaltase is most active with maltotetraose, and the Km value for this substrate is 7.1 mM. D-Enzyme catalyzed glucose release from maltose (Km = 8.3 mM) at a higher rate than from maltotriose and maltotetraose. With maltotriose as initial substrate, D-enzyme forms glucose, maltopentaose, maltoheptaose, maltononaose, maltoundecaose as major products. Amylomaltase acts on maltotriose, maltotetraose, and maltopentaose to form a series of homologous 1,4-alpha-glucans. No essential chain-lengthening reaction occurred with maltohexaose."}

{"project":"Test-Species-PubDictionaries-PubMedBERT","denotations":[{"id":"T1","span":{"begin":21,"end":41},"obj":"Species"},{"id":"T2","span":{"begin":248,"end":268},"obj":"Species"},{"id":"T3","span":{"begin":346,"end":350},"obj":"Species"},{"id":"T4","span":{"begin":1124,"end":1129},"obj":"Species"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"578833"},{"id":"A2","pred":"db_id","subj":"T2","obj":"578833"},{"id":"A3","pred":"db_id","subj":"T3","obj":"582003"},{"id":"A4","pred":"db_id","subj":"T4","obj":"1925465"}],"text":"Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase.\nAmylomaltase and disproportionating enzyme (D-enzyme) were purified to homogeneity from cell-free extracts of Pseudomonas stutzeri using a six-step procedure. The presence of both glycosyltransferases in the same organism has not been reported before. Molecular weight determination by gel chromatography gave a value of 74,000 for the amylomaltase and 115 000 for the D-enzyme. Two subunits of different molecular weight were found in each enzyme as proved by sodium dodecyl sulfate-gel electrophoresis. The optimum pH of amylomaltase and D-enzyme activity is 7.6--7.7. Action of both glycosyltransferases on different maltodextrins showed that amylomaltase is most active with maltotetraose, and the Km value for this substrate is 7.1 mM. D-Enzyme catalyzed glucose release from maltose (Km = 8.3 mM) at a higher rate than from maltotriose and maltotetraose. With maltotriose as initial substrate, D-enzyme forms glucose, maltopentaose, maltoheptaose, maltononaose, maltoundecaose as major products. Amylomaltase acts on maltotriose, maltotetraose, and maltopentaose to form a series of homologous 1,4-alpha-glucans. No essential chain-lengthening reaction occurred with maltohexaose."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":919,"end":926},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G44653LT"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G44653LT"}],"text":"Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase.\nAmylomaltase and disproportionating enzyme (D-enzyme) were purified to homogeneity from cell-free extracts of Pseudomonas stutzeri using a six-step procedure. The presence of both glycosyltransferases in the same organism has not been reported before. Molecular weight determination by gel chromatography gave a value of 74,000 for the amylomaltase and 115 000 for the D-enzyme. Two subunits of different molecular weight were found in each enzyme as proved by sodium dodecyl sulfate-gel electrophoresis. The optimum pH of amylomaltase and D-enzyme activity is 7.6--7.7. Action of both glycosyltransferases on different maltodextrins showed that amylomaltase is most active with maltotetraose, and the Km value for this substrate is 7.1 mM. D-Enzyme catalyzed glucose release from maltose (Km = 8.3 mM) at a higher rate than from maltotriose and maltotetraose. With maltotriose as initial substrate, D-enzyme forms glucose, maltopentaose, maltoheptaose, maltononaose, maltoundecaose as major products. Amylomaltase acts on maltotriose, maltotetraose, and maltopentaose to form a series of homologous 1,4-alpha-glucans. No essential chain-lengthening reaction occurred with maltohexaose."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":919,"end":926},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G44653LT"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G44653LT"}],"text":"Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase.\nAmylomaltase and disproportionating enzyme (D-enzyme) were purified to homogeneity from cell-free extracts of Pseudomonas stutzeri using a six-step procedure. The presence of both glycosyltransferases in the same organism has not been reported before. Molecular weight determination by gel chromatography gave a value of 74,000 for the amylomaltase and 115 000 for the D-enzyme. Two subunits of different molecular weight were found in each enzyme as proved by sodium dodecyl sulfate-gel electrophoresis. The optimum pH of amylomaltase and D-enzyme activity is 7.6--7.7. Action of both glycosyltransferases on different maltodextrins showed that amylomaltase is most active with maltotetraose, and the Km value for this substrate is 7.1 mM. D-Enzyme catalyzed glucose release from maltose (Km = 8.3 mM) at a higher rate than from maltotriose and maltotetraose. With maltotriose as initial substrate, D-enzyme forms glucose, maltopentaose, maltoheptaose, maltononaose, maltoundecaose as major products. Amylomaltase acts on maltotriose, maltotetraose, and maltopentaose to form a series of homologous 1,4-alpha-glucans. No essential chain-lengthening reaction occurred with maltohexaose."}

{"project":"Organism-PubDic","denotations":[{"id":"T1","span":{"begin":21,"end":32},"obj":"Species"},{"id":"T2","span":{"begin":248,"end":259},"obj":"Species"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"286"},{"id":"A2","pred":"db_id","subj":"T2","obj":"286"}],"text":"Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase.\nAmylomaltase and disproportionating enzyme (D-enzyme) were purified to homogeneity from cell-free extracts of Pseudomonas stutzeri using a six-step procedure. The presence of both glycosyltransferases in the same organism has not been reported before. Molecular weight determination by gel chromatography gave a value of 74,000 for the amylomaltase and 115 000 for the D-enzyme. Two subunits of different molecular weight were found in each enzyme as proved by sodium dodecyl sulfate-gel electrophoresis. The optimum pH of amylomaltase and D-enzyme activity is 7.6--7.7. Action of both glycosyltransferases on different maltodextrins showed that amylomaltase is most active with maltotetraose, and the Km value for this substrate is 7.1 mM. D-Enzyme catalyzed glucose release from maltose (Km = 8.3 mM) at a higher rate than from maltotriose and maltotetraose. With maltotriose as initial substrate, D-enzyme forms glucose, maltopentaose, maltoheptaose, maltononaose, maltoundecaose as major products. Amylomaltase acts on maltotriose, maltotetraose, and maltopentaose to form a series of homologous 1,4-alpha-glucans. No essential chain-lengthening reaction occurred with maltohexaose."}

{"project":"Organism-PubTator","denotations":[{"id":"1","span":{"begin":21,"end":41},"obj":"Species"},{"id":"18","span":{"begin":248,"end":268},"obj":"Species"}],"attributes":[{"id":"A1","pred":"db_id","subj":"1","obj":"316"},{"id":"A18","pred":"db_id","subj":"18","obj":"316"}],"text":"Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase.\nAmylomaltase and disproportionating enzyme (D-enzyme) were purified to homogeneity from cell-free extracts of Pseudomonas stutzeri using a six-step procedure. The presence of both glycosyltransferases in the same organism has not been reported before. Molecular weight determination by gel chromatography gave a value of 74,000 for the amylomaltase and 115 000 for the D-enzyme. Two subunits of different molecular weight were found in each enzyme as proved by sodium dodecyl sulfate-gel electrophoresis. The optimum pH of amylomaltase and D-enzyme activity is 7.6--7.7. Action of both glycosyltransferases on different maltodextrins showed that amylomaltase is most active with maltotetraose, and the Km value for this substrate is 7.1 mM. D-Enzyme catalyzed glucose release from maltose (Km = 8.3 mM) at a higher rate than from maltotriose and maltotetraose. With maltotriose as initial substrate, D-enzyme forms glucose, maltopentaose, maltoheptaose, maltononaose, maltoundecaose as major products. Amylomaltase acts on maltotriose, maltotetraose, and maltopentaose to form a series of homologous 1,4-alpha-glucans. No essential chain-lengthening reaction occurred with maltohexaose."}

{"project":"Organism-PubDic-Bert-9","denotations":[{"id":"T1","span":{"begin":21,"end":41},"obj":"Species"},{"id":"T2","span":{"begin":248,"end":268},"obj":"Species"},{"id":"T3","span":{"begin":1124,"end":1129},"obj":"Species"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"578833"},{"id":"A2","pred":"db_id","subj":"T2","obj":"578833"},{"id":"A3","pred":"db_id","subj":"T3","obj":"1925465"}],"text":"Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase.\nAmylomaltase and disproportionating enzyme (D-enzyme) were purified to homogeneity from cell-free extracts of Pseudomonas stutzeri using a six-step procedure. The presence of both glycosyltransferases in the same organism has not been reported before. Molecular weight determination by gel chromatography gave a value of 74,000 for the amylomaltase and 115 000 for the D-enzyme. Two subunits of different molecular weight were found in each enzyme as proved by sodium dodecyl sulfate-gel electrophoresis. The optimum pH of amylomaltase and D-enzyme activity is 7.6--7.7. Action of both glycosyltransferases on different maltodextrins showed that amylomaltase is most active with maltotetraose, and the Km value for this substrate is 7.1 mM. D-Enzyme catalyzed glucose release from maltose (Km = 8.3 mM) at a higher rate than from maltotriose and maltotetraose. With maltotriose as initial substrate, D-enzyme forms glucose, maltopentaose, maltoheptaose, maltononaose, maltoundecaose as major products. Amylomaltase acts on maltotriose, maltotetraose, and maltopentaose to form a series of homologous 1,4-alpha-glucans. No essential chain-lengthening reaction occurred with maltohexaose."}

{"project":"Organism-PubDic-Bert-8","denotations":[{"id":"T1","span":{"begin":21,"end":41},"obj":"Species"},{"id":"T2","span":{"begin":248,"end":268},"obj":"Species"},{"id":"T3","span":{"begin":346,"end":350},"obj":"Species"},{"id":"T4","span":{"begin":1124,"end":1129},"obj":"Species"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"578833"},{"id":"A2","pred":"db_id","subj":"T2","obj":"578833"},{"id":"A3","pred":"db_id","subj":"T3","obj":"582003"},{"id":"A4","pred":"db_id","subj":"T4","obj":"1925465"}],"text":"Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase.\nAmylomaltase and disproportionating enzyme (D-enzyme) were purified to homogeneity from cell-free extracts of Pseudomonas stutzeri using a six-step procedure. The presence of both glycosyltransferases in the same organism has not been reported before. Molecular weight determination by gel chromatography gave a value of 74,000 for the amylomaltase and 115 000 for the D-enzyme. Two subunits of different molecular weight were found in each enzyme as proved by sodium dodecyl sulfate-gel electrophoresis. The optimum pH of amylomaltase and D-enzyme activity is 7.6--7.7. Action of both glycosyltransferases on different maltodextrins showed that amylomaltase is most active with maltotetraose, and the Km value for this substrate is 7.1 mM. D-Enzyme catalyzed glucose release from maltose (Km = 8.3 mM) at a higher rate than from maltotriose and maltotetraose. With maltotriose as initial substrate, D-enzyme forms glucose, maltopentaose, maltoheptaose, maltononaose, maltoundecaose as major products. Amylomaltase acts on maltotriose, maltotetraose, and maltopentaose to form a series of homologous 1,4-alpha-glucans. No essential chain-lengthening reaction occurred with maltohexaose."}

{"project":"Organism-Gold","denotations":[{"id":"T1","span":{"begin":21,"end":41},"obj":"Species"},{"id":"T2","span":{"begin":248,"end":268},"obj":"Species"}],"attributes":[{"id":"A3","pred":"db_id","subj":"T1","obj":"316"},{"id":"A2","pred":"db_id","subj":"T2","obj":"316"}],"text":"Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase.\nAmylomaltase and disproportionating enzyme (D-enzyme) were purified to homogeneity from cell-free extracts of Pseudomonas stutzeri using a six-step procedure. The presence of both glycosyltransferases in the same organism has not been reported before. Molecular weight determination by gel chromatography gave a value of 74,000 for the amylomaltase and 115 000 for the D-enzyme. Two subunits of different molecular weight were found in each enzyme as proved by sodium dodecyl sulfate-gel electrophoresis. The optimum pH of amylomaltase and D-enzyme activity is 7.6--7.7. Action of both glycosyltransferases on different maltodextrins showed that amylomaltase is most active with maltotetraose, and the Km value for this substrate is 7.1 mM. D-Enzyme catalyzed glucose release from maltose (Km = 8.3 mM) at a higher rate than from maltotriose and maltotetraose. With maltotriose as initial substrate, D-enzyme forms glucose, maltopentaose, maltoheptaose, maltononaose, maltoundecaose as major products. Amylomaltase acts on maltotriose, maltotetraose, and maltopentaose to form a series of homologous 1,4-alpha-glucans. No essential chain-lengthening reaction occurred with maltohexaose."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":351,"end":359},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000468"}],"text":"Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase.\nAmylomaltase and disproportionating enzyme (D-enzyme) were purified to homogeneity from cell-free extracts of Pseudomonas stutzeri using a six-step procedure. The presence of both glycosyltransferases in the same organism has not been reported before. Molecular weight determination by gel chromatography gave a value of 74,000 for the amylomaltase and 115 000 for the D-enzyme. Two subunits of different molecular weight were found in each enzyme as proved by sodium dodecyl sulfate-gel electrophoresis. The optimum pH of amylomaltase and D-enzyme activity is 7.6--7.7. Action of both glycosyltransferases on different maltodextrins showed that amylomaltase is most active with maltotetraose, and the Km value for this substrate is 7.1 mM. D-Enzyme catalyzed glucose release from maltose (Km = 8.3 mM) at a higher rate than from maltotriose and maltotetraose. With maltotriose as initial substrate, D-enzyme forms glucose, maltopentaose, maltoheptaose, maltononaose, maltoundecaose as major products. Amylomaltase acts on maltotriose, maltotetraose, and maltopentaose to form a series of homologous 1,4-alpha-glucans. No essential chain-lengthening reaction occurred with maltohexaose."}

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":21,"end":32},"obj":"Organism"},{"id":"T2","span":{"begin":248,"end":259},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"286"},{"id":"A2","pred":"db_id","subj":"T2","obj":"286"}],"text":"Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase.\nAmylomaltase and disproportionating enzyme (D-enzyme) were purified to homogeneity from cell-free extracts of Pseudomonas stutzeri using a six-step procedure. The presence of both glycosyltransferases in the same organism has not been reported before. Molecular weight determination by gel chromatography gave a value of 74,000 for the amylomaltase and 115 000 for the D-enzyme. Two subunits of different molecular weight were found in each enzyme as proved by sodium dodecyl sulfate-gel electrophoresis. The optimum pH of amylomaltase and D-enzyme activity is 7.6--7.7. Action of both glycosyltransferases on different maltodextrins showed that amylomaltase is most active with maltotetraose, and the Km value for this substrate is 7.1 mM. D-Enzyme catalyzed glucose release from maltose (Km = 8.3 mM) at a higher rate than from maltotriose and maltotetraose. With maltotriose as initial substrate, D-enzyme forms glucose, maltopentaose, maltoheptaose, maltononaose, maltoundecaose as major products. Amylomaltase acts on maltotriose, maltotetraose, and maltopentaose to form a series of homologous 1,4-alpha-glucans. No essential chain-lengthening reaction occurred with maltohexaose."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":42},"obj":"Sentence"},{"id":"T2","span":{"begin":43,"end":46},"obj":"Sentence"},{"id":"T3","span":{"begin":47,"end":137},"obj":"Sentence"},{"id":"T4","span":{"begin":138,"end":296},"obj":"Sentence"},{"id":"T5","span":{"begin":297,"end":389},"obj":"Sentence"},{"id":"T6","span":{"begin":390,"end":516},"obj":"Sentence"},{"id":"T7","span":{"begin":517,"end":642},"obj":"Sentence"},{"id":"T8","span":{"begin":643,"end":708},"obj":"Sentence"},{"id":"T9","span":{"begin":709,"end":878},"obj":"Sentence"},{"id":"T10","span":{"begin":879,"end":998},"obj":"Sentence"},{"id":"T11","span":{"begin":999,"end":1139},"obj":"Sentence"},{"id":"T12","span":{"begin":1140,"end":1256},"obj":"Sentence"},{"id":"T13","span":{"begin":1257,"end":1324},"obj":"Sentence"}],"text":"Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase.\nAmylomaltase and disproportionating enzyme (D-enzyme) were purified to homogeneity from cell-free extracts of Pseudomonas stutzeri using a six-step procedure. The presence of both glycosyltransferases in the same organism has not been reported before. Molecular weight determination by gel chromatography gave a value of 74,000 for the amylomaltase and 115 000 for the D-enzyme. Two subunits of different molecular weight were found in each enzyme as proved by sodium dodecyl sulfate-gel electrophoresis. The optimum pH of amylomaltase and D-enzyme activity is 7.6--7.7. Action of both glycosyltransferases on different maltodextrins showed that amylomaltase is most active with maltotetraose, and the Km value for this substrate is 7.1 mM. D-Enzyme catalyzed glucose release from maltose (Km = 8.3 mM) at a higher rate than from maltotriose and maltotetraose. With maltotriose as initial substrate, D-enzyme forms glucose, maltopentaose, maltoheptaose, maltononaose, maltoundecaose as major products. Amylomaltase acts on maltotriose, maltotetraose, and maltopentaose to form a series of homologous 1,4-alpha-glucans. No essential chain-lengthening reaction occurred with maltohexaose."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":21,"end":32},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":248,"end":259},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"286"},{"id":"A2","pred":"db_id","subj":"T2","obj":"286"}],"text":"Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase.\nAmylomaltase and disproportionating enzyme (D-enzyme) were purified to homogeneity from cell-free extracts of Pseudomonas stutzeri using a six-step procedure. The presence of both glycosyltransferases in the same organism has not been reported before. Molecular weight determination by gel chromatography gave a value of 74,000 for the amylomaltase and 115 000 for the D-enzyme. Two subunits of different molecular weight were found in each enzyme as proved by sodium dodecyl sulfate-gel electrophoresis. The optimum pH of amylomaltase and D-enzyme activity is 7.6--7.7. Action of both glycosyltransferases on different maltodextrins showed that amylomaltase is most active with maltotetraose, and the Km value for this substrate is 7.1 mM. D-Enzyme catalyzed glucose release from maltose (Km = 8.3 mM) at a higher rate than from maltotriose and maltotetraose. With maltotriose as initial substrate, D-enzyme forms glucose, maltopentaose, maltoheptaose, maltononaose, maltoundecaose as major products. Amylomaltase acts on maltotriose, maltotetraose, and maltopentaose to form a series of homologous 1,4-alpha-glucans. No essential chain-lengthening reaction occurred with maltohexaose."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":351,"end":359},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000468"}],"text":"Starch metabolism in Pseudomonas stutzeri. II. Purification and properties of a dextrin glycosyl-transferase (D-enzyme) and amylomaltase.\nAmylomaltase and disproportionating enzyme (D-enzyme) were purified to homogeneity from cell-free extracts of Pseudomonas stutzeri using a six-step procedure. The presence of both glycosyltransferases in the same organism has not been reported before. Molecular weight determination by gel chromatography gave a value of 74,000 for the amylomaltase and 115 000 for the D-enzyme. Two subunits of different molecular weight were found in each enzyme as proved by sodium dodecyl sulfate-gel electrophoresis. The optimum pH of amylomaltase and D-enzyme activity is 7.6--7.7. Action of both glycosyltransferases on different maltodextrins showed that amylomaltase is most active with maltotetraose, and the Km value for this substrate is 7.1 mM. D-Enzyme catalyzed glucose release from maltose (Km = 8.3 mM) at a higher rate than from maltotriose and maltotetraose. With maltotriose as initial substrate, D-enzyme forms glucose, maltopentaose, maltoheptaose, maltononaose, maltoundecaose as major products. Amylomaltase acts on maltotriose, maltotetraose, and maltopentaose to form a series of homologous 1,4-alpha-glucans. No essential chain-lengthening reaction occurred with maltohexaose."}