Glutamate Dehydrogenase from Thermus thermophilus Is Activated by AMP and Leucine as a Complex with Catalytically Inactive Adenine Phosphoribosyltransferase Homolog

Glutamate dehydrogenase (GDH) from a thermophilic bacterium, Thermus thermophilus, is composed of two heterologous subunits, GdhA and GdhB. In the heterocomplex, GdhB acts as the catalytic subunit, whereas GdhA lacks enzymatic activity and acts as the regulatory subunit for activation by leucine. In...

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Shranjeno v:
Bibliografske podrobnosti
izdano v:J Bacteriol
Main Authors: Tomita, Takeo, Matsushita, Hajime, Yoshida, Ayako, Kosono, Saori, Yoshida, Minoru, Kuzuyama, Tomohisa, Nishiyama, Makoto
Format: Artigo
Jezik:Inglês
Izdano: American Society for Microbiology 2019
Teme:
Research Article
Online dostop:https://ncbi.nlm.nih.gov/pmc/articles/PMC6597394/
https://ncbi.nlm.nih.gov/pubmed/31036724
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JB.00710-18
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