Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Allosteric regulation of glutamate dehydrogenase deamination activity.

Scientific reports - 5 Oct 2020

Bera Soumen, Rashid Mubasher, Medvinsky Alexander B, Sun Gui-Quan, Li Bai-Lian, Acquisti Claudia, Sljoka Adnan, Chakraborty Amit

Abstract excerpt

Glutamate dehydrogenase (GDH) is a key enzyme interlinking carbon and nitrogen metabolism. Recent discoveries of the GDH specific role in breast cancer, hyperinsulinism/hyperammonemia (HI/HA) syndrome, and neurodegenerative diseases have reinvigorated interest on GDH regulation, which remains poorly understood despite extensive and long standing studies. Notwithstanding the growing evidence of the complexity of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Hyperammonemia
Share to Adenosine Diphosphate

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Biophysics

Share to Cryoelectron Microscopy

Share to Deamination

Share to Glutamate Dehydrogenase

Share to Guanosine Triphosphate

Source

Open in PubMed Open full text

Identifiers

PMID: 33020580
DOI: 10.1038/s41598-020-73743-4
PMCID: PMC7536180

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Allosteric regulation of glutamate dehydrogenase deamination activity.PMID 33020580Read ↗

The structure of apo human glutamate dehydrogenase details subunit communication and allostery.Semantic proximity Read ↗

Side-chain interactions in the regulatory domain of human glutamate dehydrogenase determine basal activity and regulation.Semantic proximity Read ↗

Hyperinsulinism associated with GLUD1 mutation: allosteric regulation and functional characterization of p.G446V glutamate dehydrogenase.Semantic proximity Read ↗

Evolutionary Changes in Primate Glutamate Dehydrogenases 1 and 2 Influence the Protein Regulation by Ligands, Targeting and Posttranslational Modifications.Semantic proximity Read ↗

Expression, purification and characterization of human glutamate dehydrogenase (GDH) allosteric regulatory mutations.Semantic proximity Read ↗

The odyssey of a young gene: structure-function studies in human glutamate dehydrogenases reveal evolutionary-acquired complex allosteric regulation mechanisms.Semantic proximity Read ↗

Mutations in human GLUD2 glutamate dehydrogenase affecting basal activity and regulation.Semantic proximity Read ↗

Deregulation of glutamate dehydrogenase in human neurologic disorders.Semantic proximity Read ↗

The human GLUD2 glutamate dehydrogenase: localization and functional aspects.Semantic proximity Read ↗

Structure of NADP(+)-dependent glutamate dehydrogenase from Escherichia coli--reflections on the basis of coenzyme specificity in the family of glutamate dehydrogenases.Semantic proximity Read ↗

Crystal structure of glutamate dehydrogenase 2, a positively selected novel human enzyme involved in brain biology and cancer pathophysiology.Semantic proximity Read ↗

Single amino acid substitution (G456A) in the vicinity of the GTP binding domain of human housekeeping glutamate dehydrogenase markedly attenuates GTP inhibition and abolishes the cooperative behavior of the enzyme.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.