Variable subunit structure of lysine-sensitive aspartylkinase from Escherichia coli TIR-8
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00733a009
Cited by 25 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Structures of R- and T-state Escherichia coli Aspartokinase III;Journal of Biological Chemistry;2006-10
2. Structures of R- and T-stateEscherichia coliAspartokinase III;Journal of Biological Chemistry;2006-08-12
3. Site-directed Mutagenesis of Escherichia coli Acetylglutamate Kinase and Aspartokinase III Probes the Catalytic and Substrate-binding Mechanisms of these Amino Acid Kinase Family Enzymes and Allows Three-dimensional Modelling of Aspartokinase;Journal of Molecular Biology;2003-11
4. Recovery of Catalytic Activity from an Inactive Aggregated Mutant of l-Aspartase;Biochemical and Biophysical Research Communications;1999-10
5. Specificity of Aspartokinase III fromEscherichia coliand an Examination of Important Catalytic Residues;Archives of Biochemistry and Biophysics;1996-11
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