Discover Community Create You

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

Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase II

21 Jan 2002

Abstract excerpt

Glutamate carboxypeptidase II (GCPII, EC 3.4.17.21) is a membrane peptidase expressed in a number of tissues such as kidney, prostate and brain. The brain form of GCPII (also known as NAALADase) cleaves N-acetyl-aspartyl glutamate to yield free glutamate. Animal model experiments show that inhibition of GCPII prevents neuronal cell death during experimental ischaemia. GCPII thus represents an important target for...

Read the complete abstract on PubMed

Topics

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

Share to Neuropeptides and Animal Physiology
Share to Peptidase Inhibition and Analysis
Share to Signaling Pathways in Disease

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 11905994
DOI: 10.1046/j.0022-3042.2001.00715.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Substrate specificity, inhibition and enzymological analysis of recombinant human glutamate carboxypeptidase IIPMID 11905994Read ↗

Mapping of the active site of glutamate carboxypeptidase II by site‐directed mutagenesisSemantic proximity Read ↗

Glutamate Carboxypeptidase II: An Overview of Structural Studies and Their Importance for Structure-Based Drug Design and Deciphering the Reaction Mechanism of the EnzymeSemantic proximity Read ↗

Deletion of the glutamate carboxypeptidase II gene in mice reveals a second enzyme activity that hydrolyzes N-acetylaspartylglutamate.Semantic proximity Read ↗

Enzyme Kinetics and Inhibition Parameters of Human Leukocyte GlucosylceramidaseSemantic proximity Read ↗

Isolation and Expression of Novel Human Glutamate Carboxypeptidases with N-Acetylated α-Linked Acidic Dipeptidase and Dipeptidyl Peptidase IV ActivitySemantic proximity Read ↗

Structural and biochemical characterization of the folyl‐poly‐γ‐<scp>l</scp>‐glutamate hydrolyzing activity of human glutamate carboxypeptidase <scp>II</scp>Semantic proximity Read ↗

In silico approaches to identify the potential inhibitors of glutamate carboxypeptidase II (GCPII) for neuroprotection.Semantic proximity Read ↗

GCPII Variants, Paralogs and OrthologsSemantic proximity Read ↗

Paradoxical role of C1561T glutamate carboxypeptidase II (GCPII) genetic polymorphism in altering disease susceptibility.Semantic proximity Read ↗

Mice lacking glutamate carboxypeptidase II are protected from peripheral neuropathy and ischemic brain injury.Semantic proximity Read ↗

The Human Asparaginase-like Protein 1 hASRGL1 Is an Ntn Hydrolase with β-Aspartyl Peptidase ActivitySemantic proximity Read ↗

The Role of D-Amino Acids in Alzheimer’s DiseaseSemantic proximity Read ↗

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