In vivo assembly of aspartate transcarbamoylase from fragmented and circularly permuted catalytic polypeptide chains
β 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
- DOI
- 10.1110/ps.38901
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π SIMILAR VOLUMES
## Abstract Interaction between a 70βamino acid and zincβbinding 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
## 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 70βamino acid zincβcontaining po