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

✍ Scribed by Xinhai Ni; Howard K. Schachman


Book ID
111753371
Publisher
Cold Spring Harbor Laboratory Press
Year
2001
Tongue
English
Weight
284 KB
Volume
10
Category
Article
ISSN
0961-8368

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A 70-amino acid zinc-binding polypeptide
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## Abstract Interaction between a 70‐amino acid and zinc‐binding polypeptide from the regulatory chain and the catalytic (C) trimer of aspartate transcarbamoylase (ATCase) leads to dramatic changes in enzyme activity and affinity for active site ligands. The hypothesis that the complex between a C

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## Abstract The regulatory enzyme aspartate transcarbamoylase (ATCase), comprising 2 catalytic (C) trimers and 3 regulatory (R) dimers, owes its stability to the manifold interchain interactions among the 12 polypeptide chains. With the availability of a recombinant 70‐amino acid zinc‐containing po