EC Number   |
|---|
    6.3.4.14 | - |
| 6.3.4.14 | crystal structure of the recombinant biotin carboxylase domain alone and in complex with soraphen A, sitting drop vapor diffusion method, crystals belong to space group P2(1), with cell parameters of a = 63.83 A, b = 96.52 A, c = 139.95 A and beta = 96.82 A |
| 6.3.4.14 | crystal structures of the biotin carboxylase domain of human acetyl-CoA carboxylase ACC2 phosphorylated by AMP-activated protein kinase AMPK. The phosphorylated Ser222 binds to the putative dimer interface of biotin carboxylase, disrupting polymerization and providing the molecular mechanism of inactivation by AMPK. The structure of the biotin carboxylase domain in complex with soraphen A, a macrocyclic polyketide natural product, shows that the compound binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMPK |
| 6.3.4.14 | enzyme in complex with ATP analogues AMP-PNP and ADP-CF2P, hanging drop vapour diffusion, from 0.1 M Bis-Tris, pH 6.5, 0.2 M CaCl2, 45% methylpentanediol, and 10% ethylene glycol or 0.1 M KCl, 3-8% PEG 8000 and 20% ethylene glycol, respectively, X-ray diffraction structure determination and analysis at 2.05 and 2.69 A resolution, respectively, structure modelling |
| 6.3.4.14 | hanging-drop vapor-diffusion method, X-ray analysis |
| 6.3.4.14 | in absence and presence of ATP. Upon ATP binding, the central B-domain closes. Residues G165 and G166 play a role in ATP binding |
| 6.3.4.14 | in complex with acetyl-CoA. Acetyl-CoA promotes a conformation for the dimer of the biotin carboxylase domain of pyruvate carboxylase that might be catalytically more competent |
| 6.3.4.14 | in complex with biotinylated biotin carboxyl carrier protein, sitting drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M Bis-Tris (pH 6.5), and 25% (w/v) PEG 3350 |
| 6.3.4.14 | in complex with hydrogencarbonate, the ATP analogue AMP-PCP, phosphonoacetamide and phosphonoformate, ADP and phosphate and the carboxybiotin analogue N1'-methoxycarbonyl biotin methyl ester. Hydrogencarbonate, phosphate, and the methyl ester of the carboxyl group of N1'-methoxycarbonyl biotin methyl ester all bind in the same pocket in the active site of biotin carboxylase |
| 6.3.4.14 | in complex with inhibitors 6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine and 6-(2,6-methoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine |
