ArticleThe Journal of biological chemistry2013
Novel insights into eukaryotic γ-glutamyltranspeptidase 1 from the crystal structure of the glutamate-bound human enzyme.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 78 citations in OpenAlex.
- Naphthalimide-Based Fluorescent Probe for Portable and Rapid Response to γ-Glutamyl Transpeptidase.Molecules (Basel, Switzerland) · 2025Article
- Enzymatically catalyzed molecular aggregation.Nature communications · 2024Article
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- New Insight into the Substrate Selectivity of Bovine Milk γ-glutamyl Transferase via Structural and Molecular Dynamics Predictions.Molecules (Basel, Switzerland) · 2023Article
- Affinity purification, identification, and biochemical characterization of Gamma-glutamyl transpeptidase, a membrane anchored enzyme of Gigantocotyle explanatum.Parasitology research · 2023Article
- Design and evaluation of novel analogs of 2-amino-4-boronobutanoic acid (ABBA) as inhibitors of human gamma-glutamyl transpeptidase.Bioorganic & medicinal chemistry · 2022Article
- Binding of Gamma-Glutamyl Transferase to TLR4 Signalling Allows Tissue Factor Activation in Monocytes.International journal of molecular sciences · 2022Article
- Isolation and characterization of a salt-tolerant γ-glutamyl transpeptidase from xerophilic3 Biotech · 2022Article
- Review
- Activation and thermal stabilization of a recombinant γ-glutamyltranspeptidase from Bacillus licheniformis ATCC 27811 by monovalent cations.Applied microbiology and biotechnology · 2022Article
- Exploration of the regulatory mechanisms of regeneration, anti-oxidation, anti-aging and the immune response at the post-molt stage ofFrontiers in physiology · 2022Article
- Fluorescent probes for visualizing ROS-associated proteins in disease.Chemical science · 2021Review
- Norcyanine-Carbamates Are Versatile Near-Infrared Fluorogenic Probes.Journal of the American Chemical Society · 2021Article
- A Systematic Review of Serum γ-Glutamyltransferase as a Prognostic Biomarker in Patients with Genitourinary Cancer.Antioxidants (Basel, Switzerland) · 2021Review
- Bacterial Gamma-Glutamyl Transpeptidase, an Emerging Biocatalyst: Insights Into Structure-Function Relationship and Its Biotechnological Applications.Frontiers in microbiology · 2021Review
- The enzymology of human eicosanoid pathways: the lipoxygenase branches.Molecular biology reports · 2020Review
- Bacterial γ-glutamyltranspeptidases, physiological function, structure, catalytic mechanism and application.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2020Article
- Probing the Interactions of Sulfur-Containing Histidine Compounds with Human Gamma-Glutamyl Transpeptidase.Marine drugs · 2019Article
- Mutational Analysis of a Highly Conserved PLSSMXP Sequence in the Small Subunit ofBiomolecules · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The enzyme γ-glutamyltranspeptidase 1 (GGT1) is a conserved member of the N-terminal nucleophile hydrolase family that cleaves the γ-glutamyl bond of glutathione and other γ-glutamyl compounds. In animals, GGT1 is expressed on the surface of the cell and has critical roles in maintaining cysteine levels in the body and regulating intracellular redox status. Expression of GGT1 has been implicated as a potentiator of asthma, cardiovascular disease, and cancer. The rational design of effective inhibitors of human GGT1 (hGGT1) has been delayed by the lack of a reliable structural model. The available crystal structures of several bacterial GGTs have been of limited use due to differences in the catalytic behavior of bacterial and mammalian GGTs. We report the high resolution (1.67 Å) crystal structure of glutamate-bound hGGT1, the first of any eukaryotic GGT. Comparisons of the active site architecture of hGGT1 with those of its bacterial orthologs highlight key differences in the residues responsible for substrate binding, including a bimodal switch in the orientation of the catalytic nucleophile (Thr-381) that is unique to the human enzyme. Compared with several bacterial counterparts, the lid loop in the crystal structure of hGGT1 adopts an open conformation that allows greater access to the active site. The hGGT1 structure also revealed tightly bound chlorides near the catalytic residue that may contribute to catalytic activity. These are absent in the bacterial GGTs. These differences between bacterial and mammalian GGTs and the new structural data will accelerate the development of new therapies for GGT1-dependent diseases.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.