✦ LIBER ✦

Effect of Amino Acid Substitutions on the Catalytic and Regulatory Properties of Aspartate Transcarbamoylase

✍ Scribed by Ellen A. Robey, Susan R. Wente, David W. Markby, Andrew Flint, Ying R. Yang and H. K. Schachman

Book ID: 123633187
Publisher: National Academy of Sciences
Year: 1986
Tongue: English
Weight: 957 KB
Volume: 83
Category: Article
ISSN: 0027-8424
DOI: 10.2307/28068

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Changes in Stability and Allosteric Prop

Changes in Stability and Allosteric Properties of Aspartate Transcarbamoylase Resulting from Amino Acid Substitutions in the Zinc-Binding Domain of the Regulatory Chains

✍ Edward Eisenstein, David W. Markby and H. K. Schachman 📂 Article 📅 1989 🏛 National Academy of Sciences 🌐 English ⚖ 948 KB

Alteration of the allosteric properties

Alteration of the allosteric properties of aspartate transcarbamoylase by pyridoxylation of the catalytic and regulatory subunits

✍ Blackburn, Michael N.; Schachman, Howard K. 📂 Article 📅 1976 🏛 American Chemical Society 🌐 English ⚖ 903 KB

The Influence of the Regulatory Chain Am

The Influence of the Regulatory Chain Amino Acids Glu-62 and IIe-12 on the Heterotropic Properties of Escherichia coli Aspartate Transcarbamoylase †

✍ Dutta, Malini; Kantrowitz, Evan R. 📂 Article 📅 1998 🏛 American Chemical Society 🌐 English ⚖ 127 KB

[Part 1: Biological Sciences] || Amino A

[Part 1: Biological Sciences] || Amino Acid Sequence of the Catalytic Subunit of Aspartate Transcarbamoylase from Escherichia coli

✍ William H. Konigsberg and Louis Henderson 📂 Article 📅 1983 🏛 National Academy of Sciences 🌐 English ⚖ 774 KB

A Single Amino Acid Substitution in the

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

✍ Kimberly A. Stieglitz; Styliani C. Pastra-Landis; Jiarong Xia; Hiro Tsuruta; Eva 📂 Article 📅 2005 🏛 Elsevier Science 🌐 English ⚖ 475 KB

A 70-amino acid zinc-binding polypeptide

A 70-amino acid zinc-binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer

✍ Bin-Bing Zhou; Grover L. Waldrop; Lawrence Lum; H. K. Schachman 📂 Article 📅 2008 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 873 KB

## 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