Effects of Macromolecular Crowding on the Intrinsic Catalytic Efficiency and Structure of Enterobactin-Specific Isochorismate Synthase
Macromolecular crowding was found to significantly enhance the intrinsic catalytic efficiency of the enterobactin-specific isochorismate synthase by inducing structural change in the enzyme. This finding provides the first experimental evidence that macromolecular crowding directly affects protein s...
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| Veröffentlicht in: | Journal of the American Chemical Society 2007-01, Vol.129 (4), p.730-731 |
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| container_title | Journal of the American Chemical Society |
| container_volume | 129 |
| creator | Jiang, Ming Guo, Zhihong |
| description | Macromolecular crowding was found to significantly enhance the intrinsic catalytic efficiency of the enterobactin-specific isochorismate synthase by inducing structural change in the enzyme. This finding provides the first experimental evidence that macromolecular crowding directly affects protein structure and function in the absence of crowding-susceptible macromolecular association. |
| doi_str_mv | 10.1021/ja065064+ |
| format | Article |
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| issn | 0002-7863 1520-5126 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_68944967 |
| source | MEDLINE; ACS Publications |
| subjects | Catalysis Enterobactin - chemistry Escherichia coli - enzymology Escherichia coli Proteins - chemistry Intramolecular Transferases - chemistry Protein Conformation |
| title | Effects of Macromolecular Crowding on the Intrinsic Catalytic Efficiency and Structure of Enterobactin-Specific Isochorismate Synthase |
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