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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 dehydrogenas...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_ee3d06ba507e400089d1f6209e598b96

3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme

About this item

Full title

3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme

Publisher

London: Nature Publishing Group UK

Journal title

Communications biology, 2021-06, Vol.4 (1), p.684-684, Article 684

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Glutamate dehydrogenases (GDHs) are widespread metabolic enzymes that play key roles in nitrogen homeostasis. Large glutamate dehydrogenases composed of 180 kDa subunits (L-GDHs
180
) contain long N- and C-terminal segments flanking the catalytic core. Despite the relevance of L-GDHs
180
in bacterial physiology, the lack of structural d...

Alternative Titles

Full title

3D architecture and structural flexibility revealed in the subfamily of large glutamate dehydrogenases by a mycobacterial enzyme

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_ee3d06ba507e400089d1f6209e598b96

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_ee3d06ba507e400089d1f6209e598b96

Other Identifiers

ISSN

2399-3642

E-ISSN

2399-3642

DOI

10.1038/s42003-021-02222-x

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