Role of the Anion-Binding Site in Catalysis and Regulation of Mycobacterium tuberculosis d-3-Phosphoglycerate Dehydrogenase
Author:
Affiliation:
1. Department of Developmental Biology
2. Department of Medicine
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi900172q
Reference18 articles.
1. Crystal Structure of Mycobacterium tuberculosis D-3-Phosphoglycerate Dehydrogenase
2. The Mechanism of Velocity Modulated Allosteric Regulation in −3-Phosphoglycerate Dehydrogenase SITE-DIRECTED MUTAGENESIS OF EFFECTOR BINDING SITE RESIDUES
3. D-3-Phosphoglycerate Dehydrogenase from Mycobacterium tuberculosis Is a Link between the Escherichia coli and Mammalian Enzymes
4. The ACT Domain: A Small Molecule Binding Domain and Its Role as a Common Regulatory Element
5. A Novel Mechanism for Substrate Inhibition in Mycobacterium tuberculosis d-3-Phosphoglycerate Dehydrogenase
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1. Determinants of substrate specificity in D-3-phosphoglycerate dehydrogenase. Conversion of the M. tuberculosis enzyme from one that does not use α-ketoglutarate as a substrate to one that does;Archives of Biochemistry and Biophysics;2019-08
2. Targeting the Serine Pathway: A Promising Approach against Tuberculosis?;Pharmaceuticals;2019-04-30
3. D-3-Phosphoglycerate Dehydrogenase;Frontiers in Molecular Biosciences;2018-12-13
4. Fe-S-Basedl-Serine Dehydratases;Encyclopedia of Inorganic and Bioinorganic Chemistry;2016-06-15
5. Mutagenic and chemical analyses provide new insight into enzyme activation and mechanism of the type 2 iron-sulfur l-serine dehydratase from Legionella pneumophila;Archives of Biochemistry and Biophysics;2016-04
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