Contribution of an aspartate residue, D114, in the active site of clostridial glutamate dehydrogenase to the enzyme’s unusual pH dependence-Reference-Cited by-同舟云学术

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Contribution of an aspartate residue, D114, in the active site of clostridial glutamate dehydrogenase to the enzyme’s unusual pH dependence

Published:2001-01 Issue:1-2 Volume:1544 Page:10-17
ISSN:0167-4838
Container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Author:

Coughlan Suzie,Wang Xing-Guo,Britton K.Linda,Stillman Timothy J.,Rice David W.,Chiaraluce Roberta,Consalvi Valerio,Scandurra Roberto,Engel Paul C.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Structural Biology

Reference21 articles.

1. Two Pathways of Glutamate Fermentation by Anaerobic Bacteria

2. Amino Acid Degradation by Anaerobic Bacteria

3. Subunit assembly and active site location in the structure of glutamate dehydrogenase

4. Conformational Flexibility in Glutamate Dehydrogenase

5. Alteration in relative activities of phenylalanine dehydrogenase towards different substrates by site-directed mutagenesis

Cited by 4 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Challenges and Adaptations of Life in Alkaline Habitats;Alkaliphiles in Biotechnology;2019

2. Cloning, molecular modeling, and docking analysis of alkali-thermostable β-mannanase from Bacillus nealsonii PN-11;Applied Microbiology and Biotechnology;2015-05-13

3. Structural Analysis of Alkaline β-Mannanase from Alkaliphilic Bacillus sp. N16-5: Implications for Adaptation to Alkaline Conditions;PLoS ONE;2011-01-28

4. Fermentation acids inhibit amino acid deamination by Clostridium sporogenes MD1 via a mechanism involving a decline in intracellular glutamate rather than protonmotive force;Microbiology;2006-09-01

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