Energetic Coupling between an Oxidizable Cysteine and the Phosphorylatable N-Terminus of Human Liver Pyruvate Kinase-Reference-Cited by-同舟云学术

Energetic Coupling between an Oxidizable Cysteine and the Phosphorylatable N-Terminus of Human Liver Pyruvate Kinase

Published:2013-01-11 Issue:3 Volume:52 Page:466-476
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Holyoak Todd¹,Zhang Bing²,Deng Junpeng²,Tang Qingling¹,Prasannan Charulata B.¹,Fenton Aron W.¹

Affiliation:

1. Department of Biochemistry and Molecular Biology, The University of Kansas Medical Center, MS 3030, 3901 Rainbow Boulevard, Kansas City, Kansas 66160, United States

2. Department of Biochemistry and Molecular Biology, Oklahoma State University, 246 Noble Research Center, Stillwater, Oklahoma 74078, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi301341r

Reference32 articles.

1. The pH dependence of the allosteric response of human liver pyruvate kinase to fructose-1,6-bisphosphate, ATP, and alanine

2. Effector Analogues Detect Varied Allosteric Roles for Conserved Protein−Effector Interactions in Pyruvate Kinase Isozymes

3. Identification of Allosteric-Activating Drug Leads for Human Liver Pyruvate Kinase

4. The Impact of Ions on Allosteric Functions in Human Liver Pyruvate Kinase

5. An Activating Interaction between the Unphosphorylated N-Terminus of Human Liver Pyruvate Kinase and the Main Body of the Protein Is Interrupted by Phosphorylation

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