Structural Analysis of Substrate and Effector Binding in Mycobacterium tuberculosis d-3-Phosphoglycerate Dehydrogenase-Reference-Cited by-同舟云学术

Structural Analysis of Substrate and Effector Binding in Mycobacterium tuberculosis d-3-Phosphoglycerate Dehydrogenase

Published:2008-07-16 Issue:32 Volume:47 Page:8271-8282
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Dey Sanghamitra¹,Burton Rodney L.¹,Grant Gregory A.¹,Sacchettini James C.¹

Affiliation:

1. Department of Biochemistry & Biophysics, Texas A&M University, College Station, Texas 77843, and Department of Developmental Biology and Department of Medicine, Washington University School of Medicine, 660 South Euclid Avenue, Box 8103, St. Louis, Missouri 63110

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi800212b

Reference34 articles.

1. Crystal Structure of Mycobacterium tuberculosis D-3-Phosphoglycerate Dehydrogenase

2. The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase

3. Vmax Regulation through Domain and Subunit Changes. The Active Form of Phosphoglycerate Dehydrogenase,

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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