BciA forms a functional oligomeric complex consisting of at least three rigid dimers. BciA requires NADPH as an electron donor for its C8-vinyl reduction activity. The BciA oligomer shows 90fold higher kcat values compared to the dimer. On the other hand, the dimer shows the similar kcat values both on the high and low NaCl concentrations. These suggests that disassembly of the oligomer to the dimer induces a structural change around the catalytic site of the enzyme, thereby decreasing the enzymatic activity of the dimer. In contrast, the Km value for the oligomer is comparable to that for the dimer, suggesting that the affinity of BciA for the substrate DV-Chlide a is retained following disassembly of the oligomer to the dimer. The oligomerization of BciA does not cause any allosteric effect on binding of DV-Chlide a at the catalytic center
BciA forms a functional oligomeric complex consisting of at least three rigid dimers. BciA requires NADPH as an electron donor for its C8-vinyl reduction activity. The BciA oligomer shows 90fold higher kcat values compared to the dimer. On the other hand, the dimer shows the similar kcat values both on the high and low NaCl concentrations. These suggests that disassembly of the oligomer to the dimer induces a structural change around the catalytic site of the enzyme, thereby decreasing the enzymatic activity of the dimer. In contrast, the Km value for the oligomer is comparable to that for the dimer, suggesting that the affinity of BciA for the substrate DV-Chlide a is retained following disassembly of the oligomer to the dimer. The oligomerization of BciA does not cause any allosteric effect on binding of DV-Chlide a at the catalytic center
BciA forms a functional oligomeric complex consisting of at least three rigid dimers. BciA requires NADPH as an electron donor for its C8-vinyl reduction activity. The BciA oligomer shows 90fold higher kcat values compared to the dimer. On the other hand, the dimer shows the similar kcat values both on the high and low NaCl concentrations. These suggests that disassembly of the oligomer to the dimer induces a structural change around the catalytic site of the enzyme, thereby decreasing the enzymatic activity of the dimer. In contrast, the Km value for the oligomer is comparable to that for the dimer, suggesting that the affinity of BciA for the substrate DV-Chlide a is retained following disassembly of the oligomer to the dimer. The oligomerization of BciA does not cause any allosteric effect on binding of DV-Chlide a at the catalytic center
BciA forms a functional oligomeric complex consisting of at least three rigid dimers. BciA requires NADPH as an electron donor for its C8-vinyl reduction activity. The BciA oligomer shows 90fold higher kcat values compared to the dimer. On the other hand, the dimer shows the similar kcat values both on the high and low NaCl concentrations. These suggests that disassembly of the oligomer to the dimer induces a structural change around the catalytic site of the enzyme, thereby decreasing the enzymatic activity of the dimer. In contrast, the Km value for the oligomer is comparable to that for the dimer, suggesting that the affinity of BciA for the substrate DV-Chlide a is retained following disassembly of the oligomer to the dimer. The oligomerization of BciA does not cause any allosteric effect on binding of DV-Chlide a at the catalytic center
BciA forms a functional oligomeric complex consisting of at least three rigid dimers. BciA requires NADPH as an electron donor for its C8-vinyl reduction activity. The BciA oligomer shows 90fold higher kcat values compared to the dimer. On the other hand, the dimer shows the similar kcat values both on the high and low NaCl concentrations. These suggests that disassembly of the oligomer to the dimer induces a structural change around the catalytic site of the enzyme, thereby decreasing the enzymatic activity of the dimer. In contrast, the Km value for the oligomer is comparable to that for the dimer, suggesting that the affinity of BciA for the substrate DV-Chlide a is retained following disassembly of the oligomer to the dimer. The oligomerization of BciA does not cause any allosteric effect on binding of DV-Chlide a at the catalytic center