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PubMed:8288583 JSONTXT

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sentences

Id Subject Object Predicate Lexical cue
T1 0-185 Sentence denotes The active site of hamster 3-hydroxy-3-methylglutaryl-CoA reductase resides at the subunit interface and incorporates catalytically essential acidic residues from separate polypeptides.
T2 186-449 Sentence denotes We employed site-directed mutagenesis based on sequence comparisons and characterization of purified mutant enzymes to identify Glu558 and Asp766 of Syrian hamster 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase (EC 1.1.1.34) as essential for catalysis.
T3 450-605 Sentence denotes Mutant enzymes E558D, E558Q, and D766N had wild-type Km values for (S)-HMG-CoA and NADPH, but exhibited less than 0.5% of the wild-type catalytic activity.
T4 606-711 Sentence denotes The inactive mutant polypeptides E558Q and D766N nevertheless can associate to generate an active enzyme.
T5 712-852 Sentence denotes In vitro, 6% of the wild-type activity was observed when mutant polypeptides E558D and D766N were mixed in the absence of chaotropic agents.
T6 853-993 Sentence denotes When mutant polypeptides E558Q and D766N were co-expressed in Escherichia coli, the resulting purified enzyme had 25% of wild-type activity.
T7 994-1215 Sentence denotes Hamster HMG-CoA reductase thus is a two-site, dimeric enzyme whose subunits associate to form an active site in which each monomer contributes at least one residue (e.g. Glu558 from one monomer and Asp766 from the other).
T8 1216-1338 Sentence denotes The wild-type enzyme behaves as a dimer during size exclusion chromatography and has one HMG-CoA binding site per monomer.
T9 1339-1468 Sentence denotes Syrian hamster HMG-CoA reductase thus appears to be a homodimer with two active sites which are located at the subunit interface.
T1 0-185 Sentence denotes The active site of hamster 3-hydroxy-3-methylglutaryl-CoA reductase resides at the subunit interface and incorporates catalytically essential acidic residues from separate polypeptides.
T2 186-449 Sentence denotes We employed site-directed mutagenesis based on sequence comparisons and characterization of purified mutant enzymes to identify Glu558 and Asp766 of Syrian hamster 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase (EC 1.1.1.34) as essential for catalysis.
T3 450-605 Sentence denotes Mutant enzymes E558D, E558Q, and D766N had wild-type Km values for (S)-HMG-CoA and NADPH, but exhibited less than 0.5% of the wild-type catalytic activity.
T4 606-711 Sentence denotes The inactive mutant polypeptides E558Q and D766N nevertheless can associate to generate an active enzyme.
T5 712-852 Sentence denotes In vitro, 6% of the wild-type activity was observed when mutant polypeptides E558D and D766N were mixed in the absence of chaotropic agents.
T6 853-993 Sentence denotes When mutant polypeptides E558Q and D766N were co-expressed in Escherichia coli, the resulting purified enzyme had 25% of wild-type activity.
T7 994-1215 Sentence denotes Hamster HMG-CoA reductase thus is a two-site, dimeric enzyme whose subunits associate to form an active site in which each monomer contributes at least one residue (e.g. Glu558 from one monomer and Asp766 from the other).
T8 1216-1338 Sentence denotes The wild-type enzyme behaves as a dimer during size exclusion chromatography and has one HMG-CoA binding site per monomer.
T9 1339-1468 Sentence denotes Syrian hamster HMG-CoA reductase thus appears to be a homodimer with two active sites which are located at the subunit interface.

NCBITAXON

Id Subject Object Predicate Lexical cue db_id
T1 335-349 OrganismTaxon denotes Syrian hamster 10036
T2 915-931 OrganismTaxon denotes Escherichia coli 562
T3 1339-1353 OrganismTaxon denotes Syrian hamster 10036