Heterotropic interactions in aspartate transcarbamoylase: turning allosteric ATP activation into inhibition as a consequence of a single tyrosine to phenylalanine mutation.
Aspartate transcarbamoylase (EC 2.1.3.2) is extensively studied as a model for cooperativity and allostery. This enzyme shows cooperativity between the catalytic sites, and its activity is feedback inhibited by CTP and activated by ATP. These regulatory processes involve several interfaces between c...
I tiakina i:
| I whakaputaina i: | Proc Natl Acad Sci U S A |
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| Ngā kaituhi matua: | , , , , , , , , |
| Hōputu: | Artigo |
| Reo: | Inglês |
| I whakaputaina: |
National Academy of Sciences
1991
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| Ngā marau: | |
| Urunga tuihono: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC52676/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1924381/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.88.20.9180 |
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