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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| 出版年: | Proc Natl Acad Sci U S A |
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| 主要な著者: | , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
National Academy of Sciences
1981
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| 主題: | |
| オンライン･アクセス: | 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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