Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: Implications for allosteric regulation

A central problem in understanding enzyme regulation is to define the conformational states that account for allosteric changes in catalytic activity. For Escherichia coli aspartate transcarbamoylase (ATCase; EC 2.1.3.2) the active, relaxed (R state) holoenzyme is generally assumed to be represented...

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Hlavní autoři: Endrizzi, James A., Beernink, Peter T., Alber, Tom, Schachman, H. K.
Médium: Artigo
Jazyk:Inglês
Vydáno: The National Academy of Sciences 2000
Témata:
Biological Sciences
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC25784/
https://ncbi.nlm.nih.gov/pubmed/10805770
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