> top > docs > PubMed:8702587 > annotations

PubMed:8702587 JSONTXT

Annnotations TAB JSON ListView MergeView

sentences

Id Subject Object Predicate Lexical cue
T1 0-44 Sentence denotes Isocitrate dehydrogenase kinase/phosphatase.
T2 45-110 Sentence denotes Kinetic characteristics of the wild-type and two mutant proteins.
T3 111-225 Sentence denotes Isocitrate dehydrogenase (IDH) of Escherichia coli is regulated by a bifunctional protein, IDH kinase/phosphatase.
T4 226-332 Sentence denotes In addition to the kinase and phosphatase activities, this protein catalyzes an intrinsic ATPase reaction.
T5 333-416 Sentence denotes The initial velocity kinetics of these activities exhibited extensive similarities.
T6 417-494 Sentence denotes IDH kinase and phosphatase both yielded intersecting double-reciprocal plots.
T7 495-699 Sentence denotes In addition, we observed similar values for the kinetic constants describing interactions of the kinase and phosphatase with their protein substrates and the interactions of all three activities with ATP.
T8 700-858 Sentence denotes In contrast, while the maximum velocities of IDH kinase and IDH phosphatase were nearly equal, they were 10-fold less than the maximum velocity of the ATPase.
T9 859-1011 Sentence denotes Although the IDH phosphatase reaction required either ATP or ADP, it was not supported by the nonhydrolyzable ATP analogue 5'-adenylyl imidodiphosphate.
T10 1012-1138 Sentence denotes The kinetic properties of wild-type IDH kinase/phosphatase were compared with those of two mutant derivatives of this protein.
T11 1139-1216 Sentence denotes The mutations in these proteins selectively inhibit IDH phosphatase activity.
T12 1217-1400 Sentence denotes Inhibition of IDH phosphatase resulted from three factors: decreases in the maximum velocities, reduced affinities for phospho-IDH, and a loss of coupling between ATP and phospho-IDH.
T13 1401-1549 Sentence denotes These mutations also affected the properties of IDH kinase, increasing the maximum velocities and decreasing the affinities for ATP and phospho-IDH.
T14 1550-1622 Sentence denotes The intrinsic ATPase activities also exhibited reduced affinity for ATP.
T15 1623-1748 Sentence denotes These results are discussed in the context of a model which proposes that all three activities occur at the same active site.
T1 0-44 Sentence denotes Isocitrate dehydrogenase kinase/phosphatase.
T2 45-110 Sentence denotes Kinetic characteristics of the wild-type and two mutant proteins.
T3 111-225 Sentence denotes Isocitrate dehydrogenase (IDH) of Escherichia coli is regulated by a bifunctional protein, IDH kinase/phosphatase.
T4 226-332 Sentence denotes In addition to the kinase and phosphatase activities, this protein catalyzes an intrinsic ATPase reaction.
T5 333-416 Sentence denotes The initial velocity kinetics of these activities exhibited extensive similarities.
T6 417-494 Sentence denotes IDH kinase and phosphatase both yielded intersecting double-reciprocal plots.
T7 495-699 Sentence denotes In addition, we observed similar values for the kinetic constants describing interactions of the kinase and phosphatase with their protein substrates and the interactions of all three activities with ATP.
T8 700-858 Sentence denotes In contrast, while the maximum velocities of IDH kinase and IDH phosphatase were nearly equal, they were 10-fold less than the maximum velocity of the ATPase.
T9 859-1011 Sentence denotes Although the IDH phosphatase reaction required either ATP or ADP, it was not supported by the nonhydrolyzable ATP analogue 5'-adenylyl imidodiphosphate.
T10 1012-1138 Sentence denotes The kinetic properties of wild-type IDH kinase/phosphatase were compared with those of two mutant derivatives of this protein.
T11 1139-1216 Sentence denotes The mutations in these proteins selectively inhibit IDH phosphatase activity.
T12 1217-1400 Sentence denotes Inhibition of IDH phosphatase resulted from three factors: decreases in the maximum velocities, reduced affinities for phospho-IDH, and a loss of coupling between ATP and phospho-IDH.
T13 1401-1549 Sentence denotes These mutations also affected the properties of IDH kinase, increasing the maximum velocities and decreasing the affinities for ATP and phospho-IDH.
T14 1550-1622 Sentence denotes The intrinsic ATPase activities also exhibited reduced affinity for ATP.
T15 1623-1748 Sentence denotes These results are discussed in the context of a model which proposes that all three activities occur at the same active site.

mondo_disease

Id Subject Object Predicate Lexical cue mondo_id
T1 137-140 Disease denotes IDH http://purl.obolibrary.org/obo/MONDO_0017326
T2 202-205 Disease denotes IDH http://purl.obolibrary.org/obo/MONDO_0017326
T3 417-420 Disease denotes IDH http://purl.obolibrary.org/obo/MONDO_0017326
T4 745-748 Disease denotes IDH http://purl.obolibrary.org/obo/MONDO_0017326
T5 760-763 Disease denotes IDH http://purl.obolibrary.org/obo/MONDO_0017326
T6 872-875 Disease denotes IDH http://purl.obolibrary.org/obo/MONDO_0017326
T7 1048-1051 Disease denotes IDH http://purl.obolibrary.org/obo/MONDO_0017326
T8 1191-1194 Disease denotes IDH http://purl.obolibrary.org/obo/MONDO_0017326
T9 1231-1234 Disease denotes IDH http://purl.obolibrary.org/obo/MONDO_0017326
T10 1344-1347 Disease denotes IDH http://purl.obolibrary.org/obo/MONDO_0017326
T11 1396-1399 Disease denotes IDH http://purl.obolibrary.org/obo/MONDO_0017326
T12 1449-1452 Disease denotes IDH http://purl.obolibrary.org/obo/MONDO_0017326
T13 1545-1548 Disease denotes IDH http://purl.obolibrary.org/obo/MONDO_0017326

NCBITAXON

Id Subject Object Predicate Lexical cue db_id
T1 145-161 OrganismTaxon denotes Escherichia coli 562