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

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

Journal of neurochemistry - 1 Apr 2015

Mastorodemos Vasileios, Kanavouras Konstantinos, Sundaram Shobana, Providaki Maria, Petraki Zoe, Kokkinidis Michael, Zaganas Ioannis, Logothetis Diomedes E, Plaitakis Andreas

Abstract excerpt

Glutamate Dehydrogenase (GDH) is central to the metabolism of glutamate, a major excitatory transmitter in mammalian central nervous system (CNS). hGDH1 is activated by ADP and L-leucine and powerfully inhibited by GTP. Besides this housekeeping hGDH1, duplication led to an hGDH2 isoform that is expressed in the human brain dissociating its function from GTP control. The novel enzyme has reduced basal activity...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Amino Acid Substitution

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Computer Simulation

Share to Glutamate Dehydrogenase

Share to Hot Temperature

Share to Isoenzymes

Share to Mutagenesis, Site-Directed

Share to Protein Denaturation

Source

Identifiers

PMID: 25620628
DOI: 10.1111/jnc.13019

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

Side-chain interactions in the regulatory domain of human glutamate dehydrogenase determine basal activity and regulation.PMID 25620628Read ↗

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

Properties and molecular evolution of human GLUD2 (neural and testicular tissue-specific) glutamate dehydrogenase.Semantic proximity Read ↗

Allosteric regulation of glutamate dehydrogenase deamination activity.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 ↗

Important role of Ser443 in different thermal stability of human glutamate dehydrogenase isozymes.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 ↗

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

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

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

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

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

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