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. |
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. |
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. |
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. |
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. |
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. |
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). |
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. |
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. |
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. |