In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains.

Abstract

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 properties characteristic of wild-type ATCase. In order to determine… (More)

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Cite this paper

@article{Ni2001InVA, title={In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains.}, author={Xinzhi Ni and Howard K Schachman}, journal={Protein science : a publication of the Protein Society}, year={2001}, volume={10 3}, pages={519-27} }