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A Single Amino Acid Substitution in the Active Site of Escherichia coli Aspartate Transcarbamoylase Prevents the Allosteric Transition

✍ Scribed by Kimberly A. Stieglitz; Styliani C. Pastra-Landis; Jiarong Xia; Hiro Tsuruta; Evan R. Kantrowitz


Book ID
116662116
Publisher
Elsevier Science
Year
2005
Tongue
English
Weight
475 KB
Volume
349
Category
Article
ISSN
0022-2836

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## Abstract Aspartate transcarbamoylase from __Escherichia coli__ shows homotropic cooperativity for aspartate as well as hetero‐tropic regulation by nucleotides. Structurally, it consists of two trimeric catalytic subunits and three dimeric regulatory subunits, each chain being comprised of two do