EC Number   |
|---|
    6.4.1.1 | biotin carboxylase subunit |
| 6.4.1.1 | C-terminal region, and wild-type and F1077A mutant enzymes, microseeding, room temprarture, sitting drop method using a reservoir solution containing 0.8% w/v PEG 3350 and 90 mM MnCl for the wild-type and 15% w/v PEG 3350 and 200 mM ammonium tartrate for the mutant, X-ray diffraction structure determination and analysis at 2.8 A resolution |
| 6.4.1.1 | complete structure of pyruvate carboxylase at 2.0 A resolution, domain architecture of pyruvate carboxylase |
| 6.4.1.1 | crystal structure analysis |
| 6.4.1.1 | crystal structures of biotin carboxylase domain deletion mutant and of mutant K419A/E421A/E422A reveal an alpha2beta4 stoichiometry |
| 6.4.1.1 | crystal structures of mutant T882A pyruvate carboxylase are determined cocrystallized with phosphonoacetate and MgADP |
| 6.4.1.1 | in complex with coenzyme A, symmetrical tetramer with one coenzyme A molecule bound to each monomer. Presence of acetyl-CoA promotes a conformation for the dimer of the biotin carboxylase domain of pyruvate carboxylase that might be catalytically more competent |
| 6.4.1.1 | in complex with cyclic di-3',5'-adenosine monophosphate |
| 6.4.1.1 | modeling of three-dimensional structure |
| 6.4.1.1 | purified enzyme in presence of 5 mM ATP and 5 mM oxaloacetic acid, sitting drop method, room temperature, the reservoir solution contains 20% w/v PEG 3350 and 200 mM ammonium tartrate, X-ray diffraction structure determination and analysis at 2.8 A resolution |
