Changes in the hydrogen exchange kinetics of Escherichia coli aspartate transcarbamylase produced by effector binding and subunit association.
Large changes in solvent accessibility to aspartate transcarbamylase (aspartate carbamoyltransferase, carbamoylphosphate:L-aspartate carbamoyltransferase, EC 2.1.3.2), as monitored by tritium exchange, result from binding of substrates and substrate analogs to the catalytic subunit (c3), binding of...
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| Опубликовано в:: | Proc Natl Acad Sci U S A |
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| Главные авторы: | , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
National Academy of Sciences
1981
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC349129/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7031660/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.78.11.6759 |
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