The importance of arginine 171 in substrate binding by Bacillus stearothermophilus lactate dehydrogenase-Reference-Cited by-同舟云学术

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The importance of arginine 171 in substrate binding by Bacillus stearothermophilus lactate dehydrogenase

Published:1987-07 Issue:1 Volume:146 Page:346-353
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Hart Keith W.,Clarke Anthony R.,Wigley Dale B.,Chia William N.,Barstow David A.,Atkinson Tony,Holbrook J.John

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference12 articles.

1. Structure of the active ternary complex of pig heart lactate dehydrogenase with S-lac-NAD at 2.7 Å resolution

2. The 5Åresolution structure of an abortive ternary complex of lactate dehydrogenase and its comparison with the apo-enzyme

3. Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding

4. Cloning, expression and complete nucleotide sequence of the Bacillus stearothermophilusl-lactate dehydrogenase gene

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1. Exploring the Key Amino Acid Residues Surrounding the Active Center of Lactate Dehydrogenase A for the Development of Ideal Inhibitors;Molecules;2024-04-28

2. Biochemical, structural and dynamical characterizations of the lactate dehydrogenase from Selenomonas ruminantium provide information about an intermediate evolutionary step prior to complete allosteric regulation acquisition in the super family of lactate and malate dehydrogenases;Journal of Structural Biology;2023-12

3. Importance of aspartic acid side chain carboxylate‐arginine interaction in substrate selection of arginine 2,3‐aminomutase BlsG;Protein Science;2023-02-14

4. LDHA: The Obstacle to T cell responses against tumor;Frontiers in Oncology;2022-11-28

5. Structural and functional regulation of lactate dehydrogenase-A in cancer;Future Medicinal Chemistry;2020-03

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