Investigation of the Roles of Allosteric Domain Arginine, Aspartate, and Glutamate Residues of Rhizobium etli Pyruvate Carboxylase in Relation to Its Activation by Acetyl CoA-Reference-Cited by-同舟云学术

Investigation of the Roles of Allosteric Domain Arginine, Aspartate, and Glutamate Residues of Rhizobium etli Pyruvate Carboxylase in Relation to Its Activation by Acetyl CoA

Published:2016-07-15 Issue:30 Volume:55 Page:4220-4228
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Sirithanakorn Chaiyos¹,Jitrapakdee Sarawut¹,Attwood Paul V.²

Affiliation:

1. Department of Biochemistry, Faculty of Science, Mahidol University, Bangkok 10400, Thailand

2. School of Chemistry and Biochemistry, The University of Western Australia, 35 Stirling Highway, Crawley, WA 6009, Australia

Funder

Thailand Research Fund

Mahidol University

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.6b00548

Reference31 articles.

1. Structure, mechanism and regulation of pyruvate carboxylase

2. Pyruvate Carboxylase Plays a Crucial Role in Carbon Metabolism of Extra- and Intracellularly ReplicatingListeria monocytogenes

3. Decreased levels of metabolic enzymes in pancreatic islets of patients with type 2 diabetes

4. Targeting Pyruvate Carboxylase Reduces Gluconeogenesis and Adiposity and Improves Insulin Resistance

5. Pyruvate Carboxylase Is Up-Regulated in Breast Cancer and Essential to Support Growth and Invasion of MDA-MB-231 Cells

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