Changes in stability and allosteric properties of aspartate transcarbamoylase resulting from amino acid substitutions in the zinc-binding domain of the regulatory chains.
Changes in subunit interaction energies linked to the allosteric transition of the regulatory enzyme aspartate transcarbamoylase (ATCase; EC 2.1.3.2) from Escherichia coli are localized in part at interfaces between the six catalytic (c) and six regulatory (r) polypeptide chains. Site-directed mutag...
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| Veröffentlicht in: | Proc Natl Acad Sci U S A |
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| Hauptverfasser: | , , |
| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
National Academy of Sciences
1989
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| Schlagworte: | |
| Online-Zugang: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC287071/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/2566165/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.86.9.3094 |
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