3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenas...
3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme
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Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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English
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Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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Summary Glutamate dehydrogenases (GDHs) are widespread metabolic enzymes that play key roles in nitrogen homeostasis. Large glutamate dehydrogenases composed of 180 kDa subunits (L-GDHs180) contain long N- and C-terminal segments flanking the catalytic core. Despite the relevance of L-GDHs180 in bacterial physiology, the lack of structural data for...
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3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme
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TN_cdi_proquest_journals_2507169125
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2507169125
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E-ISSN
2692-8205
DOI
10.1101/2020.11.14.381715
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https://www.proquest.com/docview/2507169125?pq-origsite=primo&accountid=13902
