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Interaction between polypeptide chains within the catalytic subunit of aspartate transcarbamylase

✍ Scribed by Elizabeth Heyde

Book ID
115733354
Publisher
Elsevier Science
Year
1973
Weight
421 KB
Volume
293
Category
Article
ISSN
0005-2744

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Association of the catalytic subunit of
Association of the catalytic subunit of aspartate transcarbamoylase with a zinc-containing polypeptide fragment of the regulatory chain leads to increases in thermal stability
✍ Cynthia B. Peterson; Bin-Bing Zhou; Durwynne Hsieh; Angela N.H. Creager; H. K. S πŸ“‚ Article πŸ“… 2008 πŸ› Cold Spring Harbor Laboratory Press 🌐 English βš– 788 KB

## 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