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In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains
Previous studies on Escherichia coli aspartate transcarbamoylase (ATCase) demonstrated that active, stable enzyme was formed in vivo from complementing polypeptides of the catalytic (c) chain encoded by gene fragments derived from the pyrBI operon. However, the enzyme lacked the allosteric propertie...
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| Hlavní autoři: | , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Cold Spring Harbor Laboratory Press
2001
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2374128/ https://ncbi.nlm.nih.gov/pubmed/11344320 |
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